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Revision d1814339

Added by Chloé QUIGNOT over 1 year ago

  • ID d1814339bd81941d18ebe39ba4d6ab379da4404a
  • Parent 6e2a7cf4

add xray structure of SEC39

View differences:

example_tmalign/8FTU.pdb
HEADER TRANSPORT PROTEIN 13-JAN-23 8FTU
TITLE CRYSTAL STRUCTURE OF THE SNARE USE1 BOUND TO DSL1 COMPLEX SUBUNITS
TITLE 2 SEC39 AND DSL1, REVISED USE1 STRUCTURE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN TRANSPORT PROTEIN SEC39;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: VESICLE TRANSPORT PROTEIN USE1;
COMPND 7 CHAIN: B;
COMPND 8 ENGINEERED: YES;
COMPND 9 MOL_ID: 3;
COMPND 10 MOLECULE: PROTEIN TRANSPORT PROTEIN DSL1;
COMPND 11 CHAIN: C;
COMPND 12 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: KLUYVEROMYCES LACTIS NRRL Y-1140;
SOURCE 3 ORGANISM_TAXID: 284590;
SOURCE 4 STRAIN: ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 /
SOURCE 5 WM37;
SOURCE 6 ATCC: 8585;
SOURCE 7 GENE: KLLA0_B05115G;
SOURCE 8 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;
SOURCE 9 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 10 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 11 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 12 EXPRESSION_SYSTEM_PLASMID: PQLINKH;
SOURCE 13 MOL_ID: 2;
SOURCE 14 ORGANISM_SCIENTIFIC: KLUYVEROMYCES LACTIS NRRL Y-1140;
SOURCE 15 ORGANISM_TAXID: 284590;
SOURCE 16 STRAIN: ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 /
SOURCE 17 WM37;
SOURCE 18 ATCC: 8585;
SOURCE 19 GENE: KLLA0_F06644G;
SOURCE 20 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;
SOURCE 21 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 22 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 23 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 24 EXPRESSION_SYSTEM_PLASMID: PQLINKH;
SOURCE 25 MOL_ID: 3;
SOURCE 26 ORGANISM_SCIENTIFIC: KLUYVEROMYCES LACTIS NRRL Y-1140;
SOURCE 27 ORGANISM_TAXID: 284590;
SOURCE 28 STRAIN: ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 /
SOURCE 29 WM37;
SOURCE 30 ATCC: 8585;
SOURCE 31 GENE: KLLA0_C02695G;
SOURCE 32 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;
SOURCE 33 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 34 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 35 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 36 EXPRESSION_SYSTEM_PLASMID: PQLINKH
KEYWDS MEMBRANE TRAFFICKING, SNARE PROTEIN, COPI, VESICLE, MULTISUBUNIT
KEYWDS 2 TETHERING COMPLEX, DSL1 COMPLEX, CATCHR COMPLEX, TRANSPORT PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR S.M.TRAVIS,P.D.JEFFREY,F.M.HUGHSON
REVDAT 1 01-MAR-23 8FTU 0
SPRSDE 01-MAR-23 8FTU 6WC4
JRNL AUTH K.A.DAMICO,A.E.STANTON,J.D.SHIRKEY,S.M.TRAVIS,P.D.JEFFREY,
JRNL AUTH 2 F.M.HUGHSON
JRNL TITL STRUCTURE OF A MEMBRANE TETHERING COMPLEX INCORPORATING
JRNL TITL 2 MULTIPLE SNARES.
JRNL REF BIORXIV 2023
JRNL REFN ISSN 2692-8205
JRNL PMID 36778436
JRNL DOI 10.1101/2023.01.30.526244
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH S.M.TRAVIS,K.DAMICO,I.M.YU,C.MCMAHON,S.HAMID,
REMARK 1 AUTH 2 G.RAMIREZ-ARELLANO,P.D.JEFFREY,F.M.HUGHSON
REMARK 1 TITL STRUCTURAL BASIS FOR THE BINDING OF SNARES TO THE
REMARK 1 TITL 2 MULTISUBUNIT TETHERING COMPLEX DSL1.
REMARK 1 REF J BIOL CHEM V. 295 10125 2020
REMARK 1 REFN ESSN 1083-351X
REMARK 1 PMID 32409579
REMARK 1 DOI 10.1093/NAR/GKW408
REMARK 2
REMARK 2 RESOLUTION. 5.73 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.17.1-3660-000
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 5.73
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.60
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.360
REMARK 3 COMPLETENESS FOR RANGE (%) : 74.5
REMARK 3 NUMBER OF REFLECTIONS : 7036
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.278
REMARK 3 R VALUE (WORKING SET) : 0.276
REMARK 3 FREE R VALUE : 0.298
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 9.990
REMARK 3 FREE R VALUE TEST SET COUNT : 703
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 29.6000 - 9.7000 0.99 1735 191 0.2411 0.2565
REMARK 3 2 9.7000 - 7.7400 1.00 1699 190 0.2611 0.2986
REMARK 3 3 7.7400 - 6.7800 1.00 1679 186 0.3496 0.3805
REMARK 3 4 6.7800 - 6.1600 0.61 1033 116 0.3962 0.4269
REMARK 3 5 6.1600 - 5.7300 0.11 187 20 0.4503 0.3472
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 1.060
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 40.420
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 317.2
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.014 8410
REMARK 3 ANGLE : 1.856 11381
REMARK 3 CHIRALITY : 0.093 1318
REMARK 3 PLANARITY : 0.012 1433
REMARK 3 DIHEDRAL : 26.119 3152
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 1
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: ALL
REMARK 3 ORIGIN FOR THE GROUP (A): 9.1493 40.5827 -30.9085
REMARK 3 T TENSOR
REMARK 3 T11: 1.5118 T22: 2.9094
REMARK 3 T33: 2.3294 T12: -0.1687
REMARK 3 T13: 0.4767 T23: -0.0933
REMARK 3 L TENSOR
REMARK 3 L11: 0.0895 L22: -0.0833
REMARK 3 L33: 3.4210 L12: 0.1443
REMARK 3 L13: 1.4967 L23: 0.4588
REMARK 3 S TENSOR
REMARK 3 S11: -0.5382 S12: 0.0509 S13: -0.0973
REMARK 3 S21: -0.6452 S22: -0.0569 S23: 0.1933
REMARK 3 S31: -1.4366 S32: 0.1049 S33: -0.1822
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 8FTU COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 18-JAN-23.
REMARK 100 THE DEPOSITION ID IS D_1000271365.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 14-JUN-18
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS-II
REMARK 200 BEAMLINE : 17-ID-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97932
REMARK 200 MONOCHROMATOR : SI(111) SILICON CRYSTAL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 9M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS 0.7.3, STARANISO 2.0.8
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 7053
REMARK 200 RESOLUTION RANGE HIGH (A) : 5.726
REMARK 200 RESOLUTION RANGE LOW (A) : 29.601
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 74.7
REMARK 200 DATA REDUNDANCY : 6.800
REMARK 200 R MERGE (I) : 0.11500
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 10.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 5.73
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 6.65
REMARK 200 COMPLETENESS FOR SHELL (%) : 29.8
REMARK 200 DATA REDUNDANCY IN SHELL : 6.40
REMARK 200 R MERGE FOR SHELL (I) : 1.81400
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.100
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER 2.8.3
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: THIN RECTANGULAR PLATES, 200 X 200 X 20 UM
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 80.48
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 6.88
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M TRIS, PH 7.5, 0.1 M NACL, 8%
REMARK 280 (W/V) PEG 3350, 10% (V/V) ETHYLENE GLYCOL, 1 MM DITHIOTHREITOL.
REMARK 280 CRYOPROTECTED WITH 30% (V/V) ETHYLENE GLYCOL, VAPOR DIFFUSION,
REMARK 280 HANGING DROP, TEMPERATURE 295K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
REMARK 290 4555 -X+1/2,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 120.39500
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 43.92300
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 120.39500
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 43.92300
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3730 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 51750 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -27.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A -26
REMARK 465 LYS A -25
REMARK 465 HIS A -24
REMARK 465 HIS A -23
REMARK 465 HIS A -22
REMARK 465 HIS A -21
REMARK 465 HIS A -20
REMARK 465 HIS A -19
REMARK 465 HIS A -18
REMARK 465 GLY A -17
REMARK 465 ALA A -16
REMARK 465 ALA A -15
REMARK 465 GLY A -14
REMARK 465 THR A -13
REMARK 465 SER A -12
REMARK 465 LEU A -11
REMARK 465 TYR A -10
REMARK 465 LYS A -9
REMARK 465 LYS A -8
REMARK 465 ALA A -7
REMARK 465 GLY A -6
REMARK 465 LEU A -5
REMARK 465 VAL A -4
REMARK 465 PRO A -3
REMARK 465 ARG A -2
REMARK 465 GLY A -1
REMARK 465 SER A 0
REMARK 465 ILE A 278
REMARK 465 PRO A 279
REMARK 465 GLU A 367
REMARK 465 SER A 368
REMARK 465 SER A 369
REMARK 465 THR A 370
REMARK 465 LEU A 371
REMARK 465 PHE A 372
REMARK 465 ASP A 373
REMARK 465 LYS A 374
REMARK 465 LEU A 375
REMARK 465 LEU A 639
REMARK 465 GLU A 640
REMARK 465 ASN A 641
REMARK 465 THR A 642
REMARK 465 GLN A 643
REMARK 465 ARG A 644
REMARK 465 SER A 645
REMARK 465 ASN A 646
REMARK 465 ASP A 647
REMARK 465 ASN A 648
REMARK 465 PHE A 649
REMARK 465 MET A 650
REMARK 465 SER A 651
REMARK 465 ASP A 652
REMARK 465 VAL A 653
REMARK 465 SER A 654
REMARK 465 THR A 655
REMARK 465 ASN A 656
REMARK 465 VAL A 657
REMARK 465 GLY A 658
REMARK 465 ASN A 659
REMARK 465 PHE A 660
REMARK 465 LEU A 661
REMARK 465 SER A 662
REMARK 465 GLY A 663
REMARK 465 LYS A 664
REMARK 465 PHE A 665
REMARK 465 GLN A 666
REMARK 465 TRP A 667
REMARK 465 ASN A 668
REMARK 465 ILE A 669
REMARK 465 GLY A 670
REMARK 465 GLY A 671
REMARK 465 ALA A 672
REMARK 465 MET B 1
REMARK 465 GLY B 2
REMARK 465 SER B 3
REMARK 465 MET B 4
REMARK 465 THR B 5
REMARK 465 THR B 6
REMARK 465 ASP B 7
REMARK 465 LEU B 8
REMARK 465 GLN B 27
REMARK 465 ASP B 28
REMARK 465 ASP B 29
REMARK 465 GLU B 30
REMARK 465 LYS B 104
REMARK 465 ARG B 105
REMARK 465 ARG B 106
REMARK 465 TYR B 107
REMARK 465 SER B 108
REMARK 465 VAL B 109
REMARK 465 ASP B 110
REMARK 465 PHE B 111
REMARK 465 ASP B 112
REMARK 465 ALA B 113
REMARK 465 MET C 419
REMARK 465 GLY C 420
REMARK 465 SER C 421
REMARK 465 GLU C 422
REMARK 465 ASN C 423
REMARK 465 GLY C 509
REMARK 465 ASP C 510
REMARK 465 GLY C 511
REMARK 465 ASP C 512
REMARK 465 GLY C 513
REMARK 465 THR C 775
REMARK 465 ASP C 776
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 TYR A 613 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 TYR B 20 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LYS B 103 CG CD CE NZ
REMARK 470 GLU C 688 CG CD OE1 OE2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 OH TYR A 226 CG PRO A 255 2.02
REMARK 500 O ASN C 613 N GLN C 617 2.06
REMARK 500 O TYR C 638 N ALA C 643 2.06
REMARK 500 CB SER A 343 CD1 ILE A 383 2.07
REMARK 500 OG1 THR A 83 OH TYR B 95 2.08
REMARK 500 OG1 THR A 83 CZ TYR B 95 2.15
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 LEU A 63 86.32 -67.94
REMARK 500 GLU A 87 42.56 -106.14
REMARK 500 LYS A 137 1.64 58.84
REMARK 500 ILE A 161 -59.09 -122.57
REMARK 500 LYS A 195 99.62 -66.96
REMARK 500 GLU A 211 -66.93 -123.17
REMARK 500 ILE A 229 -63.80 -105.07
REMARK 500 LEU A 256 32.61 -86.92
REMARK 500 ASN A 505 68.77 -112.01
REMARK 500 ASP A 586 18.25 55.91
REMARK 500 ILE C 538 4.03 -175.92
REMARK 500 SER C 541 -55.25 59.60
REMARK 500 PRO C 584 14.08 -69.08
REMARK 500 THR C 642 -66.37 -132.30
REMARK 500 LEU C 667 -77.18 -106.51
REMARK 500 ASN C 703 -6.09 -55.62
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 6WC4 RELATED DB: PDB
REMARK 900 6WC4 CONTAINS A PRIOR MODEL OF THE STRUCTURE, SUPERCEDED BY THIS ONE
DBREF 8FTU A 1 672 UNP Q6CWC7 Q6CWC7_KLULA 1 672
DBREF 8FTU B 4 113 UNP Q6CL08 Q6CL08_KLULA 1 110
DBREF 8FTU C 422 456 UNP Q6CUS2 Q6CUS2_KLULA 332 366
DBREF 8FTU C 514 776 UNP Q6CUS2 Q6CUS2_KLULA 424 686
SEQADV 8FTU MET A -26 UNP Q6CWC7 EXPRESSION TAG
SEQADV 8FTU LYS A -25 UNP Q6CWC7 EXPRESSION TAG
SEQADV 8FTU HIS A -24 UNP Q6CWC7 EXPRESSION TAG
SEQADV 8FTU HIS A -23 UNP Q6CWC7 EXPRESSION TAG
SEQADV 8FTU HIS A -22 UNP Q6CWC7 EXPRESSION TAG
SEQADV 8FTU HIS A -21 UNP Q6CWC7 EXPRESSION TAG
SEQADV 8FTU HIS A -20 UNP Q6CWC7 EXPRESSION TAG
SEQADV 8FTU HIS A -19 UNP Q6CWC7 EXPRESSION TAG
SEQADV 8FTU HIS A -18 UNP Q6CWC7 EXPRESSION TAG
SEQADV 8FTU GLY A -17 UNP Q6CWC7 EXPRESSION TAG
SEQADV 8FTU ALA A -16 UNP Q6CWC7 EXPRESSION TAG
SEQADV 8FTU ALA A -15 UNP Q6CWC7 EXPRESSION TAG
SEQADV 8FTU GLY A -14 UNP Q6CWC7 EXPRESSION TAG
SEQADV 8FTU THR A -13 UNP Q6CWC7 EXPRESSION TAG
SEQADV 8FTU SER A -12 UNP Q6CWC7 EXPRESSION TAG
SEQADV 8FTU LEU A -11 UNP Q6CWC7 EXPRESSION TAG
SEQADV 8FTU TYR A -10 UNP Q6CWC7 EXPRESSION TAG
SEQADV 8FTU LYS A -9 UNP Q6CWC7 EXPRESSION TAG
SEQADV 8FTU LYS A -8 UNP Q6CWC7 EXPRESSION TAG
SEQADV 8FTU ALA A -7 UNP Q6CWC7 EXPRESSION TAG
SEQADV 8FTU GLY A -6 UNP Q6CWC7 EXPRESSION TAG
SEQADV 8FTU LEU A -5 UNP Q6CWC7 EXPRESSION TAG
SEQADV 8FTU VAL A -4 UNP Q6CWC7 EXPRESSION TAG
SEQADV 8FTU PRO A -3 UNP Q6CWC7 EXPRESSION TAG
SEQADV 8FTU ARG A -2 UNP Q6CWC7 EXPRESSION TAG
SEQADV 8FTU GLY A -1 UNP Q6CWC7 EXPRESSION TAG
SEQADV 8FTU SER A 0 UNP Q6CWC7 EXPRESSION TAG
SEQADV 8FTU MET B 1 UNP Q6CL08 EXPRESSION TAG
SEQADV 8FTU GLY B 2 UNP Q6CL08 EXPRESSION TAG
SEQADV 8FTU SER B 3 UNP Q6CL08 EXPRESSION TAG
SEQADV 8FTU MET C 419 UNP Q6CUS2 EXPRESSION TAG
SEQADV 8FTU GLY C 420 UNP Q6CUS2 EXPRESSION TAG
SEQADV 8FTU SER C 421 UNP Q6CUS2 EXPRESSION TAG
SEQADV 8FTU GLY C 509 UNP Q6CUS2 LINKER
SEQADV 8FTU ASP C 510 UNP Q6CUS2 LINKER
SEQADV 8FTU GLY C 511 UNP Q6CUS2 LINKER
SEQADV 8FTU ASP C 512 UNP Q6CUS2 LINKER
SEQADV 8FTU GLY C 513 UNP Q6CUS2 LINKER
SEQRES 1 A 699 MET LYS HIS HIS HIS HIS HIS HIS HIS GLY ALA ALA GLY
SEQRES 2 A 699 THR SER LEU TYR LYS LYS ALA GLY LEU VAL PRO ARG GLY
SEQRES 3 A 699 SER MET ASN PRO GLN LEU TYR LEU CYS ALA SER VAL PHE
SEQRES 4 A 699 ILE THR ARG GLY ASP VAL LYS SER VAL SER GLU ILE TYR
SEQRES 5 A 699 GLN GLY LEU GLN SER ASP ALA GLU ARG LEU GLN TYR LEU
SEQRES 6 A 699 LYS LEU LEU CYS VAL MET TRP PRO GLU LEU ASP ALA PRO
SEQRES 7 A 699 THR ASN ILE SER PHE VAL LEU LYS ASP ILE GLU LEU ASN
SEQRES 8 A 699 GLY MET ASP GLU SER SER VAL LEU VAL SER LEU ILE GLN
SEQRES 9 A 699 GLU ASP SER SER LEU THR ALA ILE SER GLU MET ASP VAL
SEQRES 10 A 699 ASN THR ILE SER LYS ARG VAL ASN ALA LEU ALA SER TYR
SEQRES 11 A 699 VAL GLU GLU THR LEU ILE GLY PHE ASN ILE HIS ILE ARG
SEQRES 12 A 699 GLU THR HIS MET LEU GLU ASP PHE ILE ARG ALA ARG THR
SEQRES 13 A 699 LEU VAL VAL ASN SER LEU SER LYS ASP ALA LEU CYS SER
SEQRES 14 A 699 LEU GLU LEU LEU ALA ASN SER THR SER LYS SER LEU VAL
SEQRES 15 A 699 SER TRP LEU ASP GLY ILE LEU LYS PRO LEU ASP HIS LEU
SEQRES 16 A 699 ASN ARG ARG LEU ASP THR LYS LEU SER ILE PHE GLN PHE
SEQRES 17 A 699 GLU ASN LEU SER ALA GLN ASP ALA VAL SER GLU MET TRP
SEQRES 18 A 699 LYS LEU PRO VAL LYS GLU VAL SER VAL VAL ARG SER MET
SEQRES 19 A 699 MET LYS TYR GLU VAL GLU PRO TYR LEU LYS PHE GLN GLY
SEQRES 20 A 699 SER TYR THR PRO PHE TYR GLU VAL ILE PHE ASN PRO ASP
SEQRES 21 A 699 ASN PHE PRO LEU ASP SER ILE ASN ASN PHE GLN ILE TYR
SEQRES 22 A 699 LYS TYR LEU SER SER GLN PRO THR PRO LEU ASP THR LYS
SEQRES 23 A 699 PHE ASN GLU THR LYS TRP ASN ILE LEU TYR SER ASN GLY
SEQRES 24 A 699 LYS ASN LEU ALA SER ILE PRO LEU PRO ASN LEU VAL PHE
SEQRES 25 A 699 GLU LEU GLU SER LEU ILE LYS SER PHE GLY ASP ASP SER
SEQRES 26 A 699 GLN ILE PHE SER GLY ILE SER LEU ASN GLU TRP LEU VAL
SEQRES 27 A 699 ASN LEU LYS PHE MET ASN ALA MET ASP ILE LYS ASP LEU
SEQRES 28 A 699 LYS SER LEU LYS LYS LEU GLN ASN GLU ASP SER VAL VAL
SEQRES 29 A 699 GLN THR SER TYR PHE SER ILE ILE THR GLN ASN MET PHE
SEQRES 30 A 699 GLN GLY HIS ILE ASP ILE LYS THR VAL GLN ASN VAL VAL
SEQRES 31 A 699 GLU PHE ILE GLU SER SER THR LEU PHE ASP LYS LEU THR
SEQRES 32 A 699 ASN GLU LEU GLN THR SER ILE LEU LEU GLU SER LEU LEU
SEQRES 33 A 699 LYS LEU GLY LYS PHE ASP ILE LEU GLU GLN PHE VAL SER
SEQRES 34 A 699 THR SER GLY VAL LYS ILE GLN ASP LYS VAL ILE ILE GLN
SEQRES 35 A 699 HIS PHE TRP ARG PHE PHE ASN ILE ALA SER ASN GLY SER
SEQRES 36 A 699 LEU SER ASP PRO ASP MET LYS ASN ALA ASN ARG THR LEU
SEQRES 37 A 699 ASN LEU LEU SER ASN LYS GLU THR HIS SER ASN LEU TYR
SEQRES 38 A 699 ASP ILE LEU THR ILE VAL ASP ARG LEU SER HIS TYR SER
SEQRES 39 A 699 LEU SER PHE LYS ARG GLY MET PRO PHE LYS PRO ALA HIS
SEQRES 40 A 699 ILE SER GLU PHE LYS ALA ASN PRO MET GLU ILE VAL GLU
SEQRES 41 A 699 LYS LEU LEU ASP LEU ASN PRO LYS LEU ARG LYS ASN ILE
SEQRES 42 A 699 GLU VAL THR PHE ASP ILE LEU LYS GLU LEU TYR THR ALA
SEQRES 43 A 699 LEU GLN VAL THR PRO SER ASP LYS ASP PHE THR LYS GLU
SEQRES 44 A 699 TYR SER LYS LEU LEU SER GLU HIS ILE ASN ASN LEU LEU
SEQRES 45 A 699 ALA ASN GLY ASP PHE LYS PHE ALA PHE ASP GLN ALA ILE
SEQRES 46 A 699 ASN LEU ILE GLU ARG PRO ASP ALA ALA GLU HIS TRP VAL
SEQRES 47 A 699 THR ILE PHE GLN VAL GLY LYS TYR ILE ASP PRO ASN TRP
SEQRES 48 A 699 LEU ASP ALA GLU ILE PRO THR GLU ILE ILE TYR LEU GLN
SEQRES 49 A 699 LEU GLY ILE VAL SER LYS LEU LEU HIS ILE CYS PRO GLU
SEQRES 50 A 699 LYS GLU TYR GLU VAL ILE THR SER GLN TRP SER GLY LEU
SEQRES 51 A 699 GLU LEU GLU LEU SER THR ARG ASN LEU ILE SER ASP LYS
SEQRES 52 A 699 TYR SER LEU GLU ASN THR GLN ARG SER ASN ASP ASN PHE
SEQRES 53 A 699 MET SER ASP VAL SER THR ASN VAL GLY ASN PHE LEU SER
SEQRES 54 A 699 GLY LYS PHE GLN TRP ASN ILE GLY GLY ALA
SEQRES 1 B 113 MET GLY SER MET THR THR ASP LEU ASP THR LEU SER ASP
SEQRES 2 B 113 GLN LEU ARG LYS ASN TYR TYR ARG ASP LEU SER LEU PHE
SEQRES 3 B 113 GLN ASP ASP GLU ASP PRO PHE TYR HIS TYR LEU ILE SER
SEQRES 4 B 113 THR LYS LEU ALA THR ASN LEU ASN THR VAL ARG LYS LEU
SEQRES 5 B 113 ALA ILE LYS ASP ASN LEU ASP ASP PRO SER SER ASP ALA
SEQRES 6 B 113 ILE ASP ARG TYR GLN LYS ASN PHE SER ARG LEU GLU GLU
SEQRES 7 B 113 SER VAL SER SER ILE SER PHE SER LYS ALA SER LYS LEU
SEQRES 8 B 113 GLN GLN LYS TYR ASP ALA TYR GLN GLU SER GLN LYS LYS
SEQRES 9 B 113 ARG ARG TYR SER VAL ASP PHE ASP ALA
SEQRES 1 C 306 MET GLY SER GLU ASN ILE TYR THR THR LEU LYS PHE GLU
SEQRES 2 C 306 SER MET MET GLN GLN ARG VAL ILE GLN ILE ARG SER ILE
SEQRES 3 C 306 PRO GLU GLU GLU TYR HIS GLU LEU VAL SER VAL GLN GLY
SEQRES 4 C 306 ASP GLY ASP GLY PRO ILE GLN VAL SER VAL PHE VAL GLN
SEQRES 5 C 306 SER ALA ALA LYS VAL PHE THR GLU PHE GLU GLN GLY CYS
SEQRES 6 C 306 ASP THR ILE GLY ARG SER LYS VAL GLU SER ILE TYR LEU
SEQRES 7 C 306 TYR LYS PHE ASN LEU LEU GLN THR ALA PHE PHE ALA MET
SEQRES 8 C 306 VAL SER GLU LYS VAL ASN ASP TRP THR GLN LEU TYR LYS
SEQRES 9 C 306 ASP VAL ARG TYR LEU TYR THR GLU ASN PRO LYS LEU LEU
SEQRES 10 C 306 GLN LEU MET GLU LEU ASN SER ARG ARG LEU ASP LEU ASN
SEQRES 11 C 306 LEU ASN LEU ILE LYS LYS THR ILE TYR LYS LEU VAL ASN
SEQRES 12 C 306 ASP GLN LEU GLN GLU LEU LYS ASP ASN GLU ARG THR PRO
SEQRES 13 C 306 ASP TRP ASP ILE THR ILE SER SER LEU LEU PRO TYR LEU
SEQRES 14 C 306 LYS LYS THR ALA LEU PRO THR LEU TYR LYS LEU GLU ASP
SEQRES 15 C 306 ASN THR ILE LEU VAL ALA LEU ILE ARG TYR ILE VAL HIS
SEQRES 16 C 306 ASP LEU VAL ILE ASP ASN ILE LEU HIS TRP ARG VAL ILE
SEQRES 17 C 306 SER GLU LYS SER SER GLU ASN LEU SER GLU PHE ILE MET
SEQRES 18 C 306 LEU LEU LEU SER GLY LEU GLU ILE PRO ARG LEU ASN LEU
SEQRES 19 C 306 ILE GLU THR TYR ARG HIS SER ARG GLU LYS LEU GLY ILE
SEQRES 20 C 306 LEU SER LYS ILE LEU THR ALA HIS LEU LYS ASP ILE LEU
SEQRES 21 C 306 GLU MET PHE TYR GLU GLY GLU PHE PHE LEU PHE GLU THR
SEQRES 22 C 306 ASP GLU ILE VAL GLN TRP ILE ILE LEU LEU PHE ALA ASP
SEQRES 23 C 306 THR PRO THR ARG ARG ASP CYS ILE ASP GLU ILE ARG ARG
SEQRES 24 C 306 VAL ARG GLU GLU ALA THR ASP
HELIX 1 AA1 ASN A 2 ARG A 15 1 14
HELIX 2 AA2 ASP A 17 GLY A 27 1 11
HELIX 3 AA3 SER A 30 TRP A 45 1 16
HELIX 4 AA4 ALA A 50 LYS A 59 5 10
HELIX 5 AA5 ASP A 67 ASP A 79 1 13
HELIX 6 AA6 LEU A 82 GLU A 87 1 6
HELIX 7 AA7 ASP A 89 PHE A 111 1 23
HELIX 8 AA8 ARG A 116 THR A 118 5 3
HELIX 9 AA9 HIS A 119 LYS A 137 1 19
HELIX 10 AB1 SER A 142 ASN A 148 1 7
HELIX 11 AB2 SER A 151 ILE A 161 1 11
HELIX 12 AB3 ILE A 161 ASP A 173 1 13
HELIX 13 AB4 SER A 177 ASN A 183 1 7
HELIX 14 AB5 SER A 185 LYS A 195 1 11
HELIX 15 AB6 GLU A 200 GLU A 211 1 12
HELIX 16 AB7 GLU A 211 GLY A 220 1 10
HELIX 17 AB8 TYR A 222 ILE A 229 1 8
HELIX 18 AB9 SER A 239 SER A 250 1 12
HELIX 19 AC1 ASP A 257 GLY A 272 1 16
HELIX 20 AC2 LYS A 273 SER A 277 5 5
HELIX 21 AC3 ASN A 282 SER A 293 1 12
HELIX 22 AC4 ASP A 297 SER A 302 5 6
HELIX 23 AC5 SER A 305 LYS A 314 1 10
HELIX 24 AC6 PHE A 315 ASP A 320 1 6
HELIX 25 AC7 ASP A 323 GLN A 331 1 9
HELIX 26 AC8 ASP A 334 PHE A 350 1 17
HELIX 27 AC9 ASP A 355 ILE A 366 1 12
HELIX 28 AD1 ASN A 377 LEU A 391 1 15
HELIX 29 AD2 LYS A 393 GLY A 405 1 13
HELIX 30 AD3 GLN A 409 ALA A 424 1 16
HELIX 31 AD4 ASP A 431 LEU A 443 1 13
HELIX 32 AD5 LYS A 447 THR A 449 5 3
HELIX 33 AD6 HIS A 450 HIS A 465 1 16
HELIX 34 AD7 LYS A 477 ASN A 487 5 11
HELIX 35 AD8 PRO A 488 ASN A 499 1 12
HELIX 36 AD9 PRO A 500 ARG A 503 5 4
HELIX 37 AE1 ASN A 505 GLN A 521 1 17
HELIX 38 AE2 PHE A 529 ASN A 547 1 19
HELIX 39 AE3 ASP A 549 GLU A 562 1 14
HELIX 40 AE4 ASP A 565 GLU A 568 5 4
HELIX 41 AE5 HIS A 569 LYS A 578 1 10
HELIX 42 AE6 TRP A 584 GLU A 588 5 5
HELIX 43 AE7 PRO A 590 LEU A 605 1 16
HELIX 44 AE8 PRO A 609 LYS A 611 5 3
HELIX 45 AE9 GLU A 612 ARG A 630 1 19
HELIX 46 AF1 THR B 10 LEU B 25 1 16
HELIX 47 AF2 PRO B 32 ASP B 60 1 29
HELIX 48 AF3 ASP B 64 LYS B 103 1 40
HELIX 49 AF4 TYR C 425 SER C 443 1 19
HELIX 50 AF5 PRO C 445 TYR C 449 5 5
HELIX 51 AF6 VAL C 519 ASP C 536 1 18
HELIX 52 AF7 ILE C 546 VAL C 566 1 21
HELIX 53 AF8 ASP C 568 ASN C 583 1 16
HELIX 54 AF9 LEU C 586 ASN C 622 1 37
HELIX 55 AG1 TRP C 628 SER C 633 1 6
HELIX 56 AG2 SER C 634 THR C 642 1 9
HELIX 57 AG3 THR C 642 LEU C 650 1 9
HELIX 58 AG4 ASP C 652 LEU C 667 1 16
HELIX 59 AG5 LEU C 667 TRP C 675 1 9
HELIX 60 AG6 SER C 679 LEU C 697 1 19
HELIX 61 AG7 ILE C 699 ASN C 703 5 5
HELIX 62 AG8 ILE C 705 THR C 723 1 19
HELIX 63 AG9 HIS C 725 GLU C 735 1 11
HELIX 64 AH1 GLU C 742 PHE C 754 1 13
HELIX 65 AH2 THR C 757 ALA C 774 1 18
SHEET 1 AA1 2 SER A 469 LYS A 471 0
SHEET 2 AA1 2 MET A 474 PRO A 475 -1 O MET A 474 N LYS A 471
SHEET 1 AA2 2 LEU C 452 SER C 454 0
SHEET 2 AA2 2 GLN C 516 SER C 518 -1 O VAL C 517 N VAL C 453
CISPEP 1 THR A 254 PRO A 255 0 -27.45
CRYST1 240.790 87.846 161.431 90.00 107.61 90.00 C 1 2 1 4
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.004153 0.000000 0.001318 0.00000
SCALE2 0.000000 0.011384 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006499 0.00000
ATOM 1 N MET A 1 32.257 86.895 60.660 1.00303.38 N
ANISOU 1 N MET A 1 43435 34521 37315 6614 -4490 7456 N
ATOM 2 CA MET A 1 31.472 86.410 61.786 1.00301.10 C
ANISOU 2 CA MET A 1 42362 34589 37454 7169 -4306 7141 C
ATOM 3 C MET A 1 32.322 86.253 63.048 1.00297.69 C
ANISOU 3 C MET A 1 41632 34093 37382 6858 -3993 7336 C
ATOM 4 O MET A 1 33.525 85.970 62.985 1.00295.51 O
ANISOU 4 O MET A 1 41456 33654 37172 6270 -3671 7750 O
ATOM 5 CB MET A 1 30.857 85.057 61.425 1.00298.28 C
ANISOU 5 CB MET A 1 41143 34755 37436 7529 -3826 7005 C
ATOM 6 CG MET A 1 29.833 85.169 60.294 1.00301.56 C
ANISOU 6 CG MET A 1 41723 35304 37553 7883 -4156 6693 C
ATOM 7 SD MET A 1 29.018 83.599 59.916 1.00298.47 S
ANISOU 7 SD MET A 1 40051 35664 37692 7977 -3508 6326 S
ATOM 8 CE MET A 1 28.093 83.353 61.456 1.00296.82 C
ANISOU 8 CE MET A 1 39167 35805 37805 8803 -3472 6056 C
ATOM 9 N ASN A 2 31.682 86.363 64.215 1.00293.15 N
ANISOU 9 N ASN A 2 40642 33684 37057 7227 -4041 7015 N
ATOM 10 CA ASN A 2 32.302 85.943 65.472 1.00289.19 C
ANISOU 10 CA ASN A 2 39701 33208 36969 7024 -3699 7077 C
ATOM 11 C ASN A 2 32.893 84.515 65.336 1.00284.40 C
ANISOU 11 C ASN A 2 38390 32918 36753 6807 -2925 7279 C
ATOM 12 O ASN A 2 32.140 83.592 65.023 1.00283.11 O
ANISOU 12 O ASN A 2 37516 33213 36842 7145 -2603 7104 O
ATOM 13 CB ASN A 2 31.251 86.025 66.589 1.00289.12 C
ANISOU 13 CB ASN A 2 39213 33455 37184 7523 -3800 6618 C
ATOM 14 CG ASN A 2 31.724 85.504 67.939 1.00284.90 C
ANISOU 14 CG ASN A 2 38184 33000 37064 7375 -3452 6559 C
ATOM 15 OD1 ASN A 2 32.760 84.888 68.119 1.00281.43 O
ANISOU 15 OD1 ASN A 2 37600 32538 36793 6972 -3004 6803 O
ATOM 16 ND2 ASN A 2 30.954 85.740 68.963 1.00285.14 N
ANISOU 16 ND2 ASN A 2 37919 33174 37245 7683 -3581 6217 N
ATOM 17 N PRO A 3 34.195 84.295 65.628 1.00335.13 N
ANISOU 17 N PRO A 3 44827 39190 43318 6180 -2543 7646 N
ATOM 18 CA PRO A 3 34.838 82.982 65.552 1.00330.73 C
ANISOU 18 CA PRO A 3 43412 38973 43278 5792 -1727 7911 C
ATOM 19 C PRO A 3 34.085 81.877 66.289 1.00327.34 C
ANISOU 19 C PRO A 3 41913 39072 43391 6173 -1276 7584 C
ATOM 20 O PRO A 3 33.937 80.776 65.771 1.00325.28 O
ANISOU 20 O PRO A 3 40915 39197 43478 6060 -788 7565 O
ATOM 21 CB PRO A 3 36.221 83.188 66.185 1.00328.81 C
ANISOU 21 CB PRO A 3 43396 38470 43068 5114 -1529 8165 C
ATOM 22 CG PRO A 3 36.540 84.621 65.798 1.00333.24 C
ANISOU 22 CG PRO A 3 45155 38489 42973 4946 -2241 8236 C
ATOM 23 CD PRO A 3 35.186 85.309 65.949 1.00336.49 C
ANISOU 23 CD PRO A 3 45807 38860 43185 5686 -2886 7841 C
ATOM 24 N GLN A 4 33.569 82.168 67.483 1.00309.68 N
ANISOU 24 N GLN A 4 39603 36879 41184 6507 -1468 7186 N
ATOM 25 CA GLN A 4 32.819 81.197 68.277 1.00306.75 C
ANISOU 25 CA GLN A 4 38297 37012 41241 6780 -1089 6795 C
ATOM 26 C GLN A 4 31.479 80.861 67.612 1.00308.58 C
ANISOU 26 C GLN A 4 38202 37608 41436 7286 -1220 6443 C
ATOM 27 O GLN A 4 31.119 79.687 67.537 1.00306.02 O
ANISOU 27 O GLN A 4 37030 37754 41490 7264 -723 6294 O
ATOM 28 CB GLN A 4 32.613 81.750 69.694 1.00306.42 C
ANISOU 28 CB GLN A 4 38388 36877 41159 6940 -1343 6464 C
ATOM 29 CG GLN A 4 33.940 81.941 70.443 1.00304.07 C
ANISOU 29 CG GLN A 4 38300 36299 40934 6426 -1138 6757 C
ATOM 30 CD GLN A 4 33.729 82.557 71.821 1.00303.95 C
ANISOU 30 CD GLN A 4 38459 36169 40857 6594 -1437 6435 C
ATOM 31 OE1 GLN A 4 33.156 83.620 71.974 1.00307.47 O
ANISOU 31 OE1 GLN A 4 39471 36348 41006 6889 -2102 6239 O
ATOM 32 NE2 GLN A 4 34.212 81.941 72.874 1.00299.99 N
ANISOU 32 NE2 GLN A 4 37468 35845 40671 6357 -977 6394 N
ATOM 33 N LEU A 5 30.789 81.865 67.058 1.00216.93 N
ANISOU 33 N LEU A 5 27274 25781 29367 7665 -1882 6304 N
ATOM 34 CA LEU A 5 29.543 81.671 66.315 1.00219.19 C
ANISOU 34 CA LEU A 5 27346 26386 29551 8126 -2058 5972 C
ATOM 35 C LEU A 5 29.774 80.884 65.022 1.00218.53 C
ANISOU 35 C LEU A 5 26977 26493 29563 7976 -1692 6266 C
ATOM 36 O LEU A 5 28.993 79.987 64.730 1.00217.59 O
ANISOU 36 O LEU A 5 26144 26855 29673 8153 -1418 5990 O
ATOM 37 CB LEU A 5 28.882 83.034 66.039 1.00224.38 C
ANISOU 37 CB LEU A 5 28840 26711 29701 8465 -2849 5805 C
ATOM 38 CG LEU A 5 27.502 82.953 65.354 1.00227.14 C
ANISOU 38 CG LEU A 5 28998 27398 29908 8947 -3062 5407 C
ATOM 39 CD1 LEU A 5 26.467 82.220 66.211 1.00225.48 C
ANISOU 39 CD1 LEU A 5 27933 27701 30040 9170 -2816 4919 C
ATOM 40 CD2 LEU A 5 26.985 84.364 65.084 1.00232.40 C
ANISOU 40 CD2 LEU A 5 30500 27735 30067 9178 -3754 5305 C
ATOM 41 N TYR A 6 30.858 81.151 64.287 1.00233.77 N
ANISOU 41 N TYR A 6 29413 28071 31340 7460 -1653 6727 N
ATOM 42 CA TYR A 6 31.224 80.410 63.076 1.00233.03 C
ANISOU 42 CA TYR A 6 29083 28136 31322 6866 -1286 6748 C
ATOM 43 C TYR A 6 31.454 78.915 63.364 1.00228.31 C
ANISOU 43 C TYR A 6 27400 28005 31344 6537 -506 6689 C
ATOM 44 O TYR A 6 30.954 78.049 62.641 1.00227.70 O
ANISOU 44 O TYR A 6 26782 28306 31428 6490 -233 6472 O
ATOM 45 CB TYR A 6 32.475 81.056 62.462 1.00234.20 C
ANISOU 45 CB TYR A 6 30016 27812 31158 6171 -1398 7138 C
ATOM 46 CG TYR A 6 32.911 80.437 61.147 1.00233.96 C
ANISOU 46 CG TYR A 6 29853 27912 31128 5550 -1086 7179 C
ATOM 47 CD1 TYR A 6 33.969 79.506 61.113 1.00230.34 C
ANISOU 47 CD1 TYR A 6 28875 27605 31039 4842 -437 7371 C
ATOM 48 CD2 TYR A 6 32.251 80.792 59.955 1.00237.44 C
ANISOU 48 CD2 TYR A 6 30694 28333 31192 5700 -1455 7012 C
ATOM 49 CE1 TYR A 6 34.380 78.949 59.888 1.00230.28 C
ANISOU 49 CE1 TYR A 6 28754 27732 31011 4285 -164 7402 C
ATOM 50 CE2 TYR A 6 32.640 80.212 58.732 1.00237.24 C
ANISOU 50 CE2 TYR A 6 30535 28437 31167 5135 -1167 7045 C
ATOM 51 CZ TYR A 6 33.706 79.288 58.697 1.00233.67 C
ANISOU 51 CZ TYR A 6 29562 28145 31076 4429 -521 7240 C
ATOM 52 OH TYR A 6 34.092 78.728 57.522 1.00233.56 O
ANISOU 52 OH TYR A 6 29416 28274 31052 3900 -249 7265 O
ATOM 53 N LEU A 7 32.145 78.595 64.464 1.00276.59 N
ANISOU 53 N LEU A 7 33183 34101 37808 6350 -161 6864 N
ATOM 54 CA LEU A 7 32.353 77.208 64.889 1.00272.14 C
ANISOU 54 CA LEU A 7 31618 33952 37832 6086 545 6803 C
ATOM 55 C LEU A 7 31.042 76.543 65.323 1.00271.50 C
ANISOU 55 C LEU A 7 30797 34362 38000 6698 625 6414 C
ATOM 56 O LEU A 7 30.750 75.440 64.863 1.00269.81 O
ANISOU 56 O LEU A 7 29898 34549 38069 6539 1040 6242 O
ATOM 57 CB LEU A 7 33.401 77.144 66.011 1.00269.07 C
ANISOU 57 CB LEU A 7 31133 33384 37717 5777 834 7086 C
ATOM 58 CG LEU A 7 34.812 77.608 65.608 1.00269.22 C
ANISOU 58 CG LEU A 7 31747 33003 37542 5067 866 7482 C
ATOM 59 CD1 LEU A 7 35.715 77.584 66.840 1.00266.28 C
ANISOU 59 CD1 LEU A 7 31258 32478 37440 4863 1117 7730 C
ATOM 60 CD2 LEU A 7 35.453 76.733 64.544 1.00267.94 C
ANISOU 60 CD2 LEU A 7 31276 33028 37502 4402 1323 7534 C
ATOM 61 N CYS A 8 30.222 77.205 66.144 1.00259.75 N
ANISOU 61 N CYS A 8 29571 32861 36260 7142 200 6046 N
ATOM 62 CA CYS A 8 28.907 76.686 66.531 1.00259.76 C
ANISOU 62 CA CYS A 8 29111 33311 36273 7401 176 5407 C
ATOM 63 C CYS A 8 28.002 76.460 65.309 1.00262.17 C
ANISOU 63 C CYS A 8 29285 33874 36452 7678 53 5239 C
ATOM 64 O CYS A 8 27.420 75.386 65.166 1.00260.57 O
ANISOU 64 O CYS A 8 28444 34102 36457 7522 387 4906 O
ATOM 65 CB CYS A 8 28.258 77.652 67.533 1.00261.79 C
ANISOU 65 CB CYS A 8 29797 33416 36253 7782 -356 5078 C
ATOM 66 SG CYS A 8 29.110 77.554 69.131 1.00258.07 S
ANISOU 66 SG CYS A 8 29241 32813 35999 7414 -94 5118 S
ATOM 67 N ALA A 9 27.947 77.423 64.386 1.00182.99 N
ANISOU 67 N ALA A 9 19921 23560 26047 8008 -423 5474 N
ATOM 68 CA ALA A 9 27.198 77.323 63.138 1.00185.50 C
ANISOU 68 CA ALA A 9 20219 24075 26186 8286 -576 5375 C
ATOM 69 C ALA A 9 27.601 76.097 62.315 1.00182.91 C
ANISOU 69 C ALA A 9 19287 24017 26194 7718 22 5431 C
ATOM 70 O ALA A 9 26.735 75.368 61.838 1.00182.97 O
ANISOU 70 O ALA A 9 18753 24457 26310 7892 165 5147 O
ATOM 71 CB ALA A 9 27.438 78.592 62.322 1.00189.55 C
ANISOU 71 CB ALA A 9 21797 24087 26137 8339 -1172 5555 C
ATOM 72 N SER A 10 28.901 75.817 62.187 1.00216.61 N
ANISOU 72 N SER A 10 23622 28057 30623 7000 383 5751 N
ATOM 73 CA SER A 10 29.381 74.651 61.432 1.00214.15 C
ANISOU 73 CA SER A 10 22775 27982 30610 6398 950 5774 C
ATOM 74 C SER A 10 28.874 73.315 61.994 1.00210.87 C
ANISOU 74 C SER A 10 21316 28096 30708 6477 1467 5557 C
ATOM 75 O SER A 10 28.604 72.380 61.236 1.00210.07 O
ANISOU 75 O SER A 10 20735 28315 30768 6280 1774 5409 O
ATOM 76 CB SER A 10 30.906 74.677 61.363 1.00212.40 C
ANISOU 76 CB SER A 10 22826 27432 30444 5662 1214 6158 C
ATOM 77 OG SER A 10 31.490 74.312 62.589 1.00209.09 O
ANISOU 77 OG SER A 10 22029 27021 30393 5551 1547 6294 O
ATOM 78 N VAL A 11 28.661 73.228 63.311 1.00207.99 N
ANISOU 78 N VAL A 11 20805 27791 30432 6554 1491 5341 N
ATOM 79 CA VAL A 11 28.091 72.042 63.965 1.00205.20 C
ANISOU 79 CA VAL A 11 19982 27788 30197 6201 1781 4788 C
ATOM 80 C VAL A 11 26.613 71.889 63.604 1.00207.47 C
ANISOU 80 C VAL A 11 20152 28391 30285 6549 1507 4279 C
ATOM 81 O VAL A 11 26.196 70.807 63.201 1.00206.19 O
ANISOU 81 O VAL A 11 19624 28508 30212 6237 1750 3976 O
ATOM 82 CB VAL A 11 28.288 72.104 65.489 1.00203.05 C
ANISOU 82 CB VAL A 11 19792 27412 29946 6077 1780 4643 C
ATOM 83 CG1 VAL A 11 27.678 70.887 66.188 1.00200.33 C
ANISOU 83 CG1 VAL A 11 19113 27354 29650 5714 1964 4086 C
ATOM 84 CG2 VAL A 11 29.774 72.149 65.861 1.00200.56 C
ANISOU 84 CG2 VAL A 11 19553 26800 29849 5674 2093 5131 C
ATOM 85 N PHE A 12 25.822 72.961 63.675 1.00214.76 N
ANISOU 85 N PHE A 12 21438 29243 30918 7170 971 4173 N
ATOM 86 CA PHE A 12 24.409 72.918 63.278 1.00217.37 C
ANISOU 86 CA PHE A 12 21668 29855 31069 7520 686 3714 C
ATOM 87 C PHE A 12 24.230 72.627 61.784 1.00218.82 C
ANISOU 87 C PHE A 12 21730 30198 31213 7572 755 3814 C
ATOM 88 O PHE A 12 23.385 71.813 61.412 1.00218.75 O
ANISOU 88 O PHE A 12 21354 30511 31248 7460 864 3433 O
ATOM 89 CB PHE A 12 23.726 74.231 63.672 1.00221.09 C
ANISOU 89 CB PHE A 12 22647 30146 31212 8136 67 3609 C
ATOM 90 CG PHE A 12 23.613 74.416 65.167 1.00219.89 C
ANISOU 90 CG PHE A 12 22516 29909 31123 8085 -11 3395 C
ATOM 91 CD1 PHE A 12 22.781 73.561 65.913 1.00218.39 C
ANISOU 91 CD1 PHE A 12 21878 30001 31100 7863 137 2918 C
ATOM 92 CD2 PHE A 12 24.313 75.451 65.811 1.00220.42 C
ANISOU 92 CD2 PHE A 12 23097 29584 31069 8238 -263 3675 C
ATOM 93 CE1 PHE A 12 22.627 73.756 67.295 1.00217.47 C
ANISOU 93 CE1 PHE A 12 21787 29799 31041 7829 42 2729 C
ATOM 94 CE2 PHE A 12 24.177 75.628 67.197 1.00219.35 C
ANISOU 94 CE2 PHE A 12 22962 29383 30999 8193 -338 3463 C
ATOM 95 CZ PHE A 12 23.312 74.799 67.933 1.00217.95 C
ANISOU 95 CZ PHE A 12 22305 29511 30994 8010 -189 2993 C
ATOM 96 N ILE A 13 25.083 73.212 60.936 1.00201.68 N
ANISOU 96 N ILE A 13 19869 27776 28983 7673 712 4348 N
ATOM 97 CA ILE A 13 25.108 72.967 59.490 1.00202.87 C
ANISOU 97 CA ILE A 13 19924 28038 29121 7686 799 4534 C
ATOM 98 C ILE A 13 25.375 71.489 59.191 1.00199.44 C
ANISOU 98 C ILE A 13 18843 27886 29050 7013 1419 4398 C
ATOM 99 O ILE A 13 24.616 70.874 58.449 1.00200.08 O
ANISOU 99 O ILE A 13 18657 28261 29101 6991 1473 4103 O
ATOM 100 CB ILE A 13 26.126 73.918 58.812 1.00204.53 C
ANISOU 100 CB ILE A 13 21048 27674 28990 7313 537 4850 C
ATOM 101 CG1 ILE A 13 25.567 75.357 58.789 1.00208.88 C
ANISOU 101 CG1 ILE A 13 22439 27919 29006 7889 -208 4791 C
ATOM 102 CG2 ILE A 13 26.457 73.460 57.384 1.00204.81 C
ANISOU 102 CG2 ILE A 13 21135 27715 28970 6803 722 4884 C
ATOM 103 CD1 ILE A 13 26.584 76.432 58.390 1.00210.68 C
ANISOU 103 CD1 ILE A 13 23648 27534 28866 7540 -532 5123 C
ATOM 104 N THR A 14 26.405 70.888 59.793 1.00225.40 N
ANISOU 104 N THR A 14 21951 31066 32625 6433 1846 4554 N
ATOM 105 CA THR A 14 26.731 69.465 59.560 1.00222.13 C
ANISOU 105 CA THR A 14 21132 30829 32436 5726 2345 4362 C
ATOM 106 C THR A 14 25.694 68.500 60.132 1.00220.83 C
ANISOU 106 C THR A 14 20766 30922 32217 5560 2331 3712 C
ATOM 107 O THR A 14 25.548 67.386 59.626 1.00219.36 O
ANISOU 107 O THR A 14 20365 30895 32087 5150 2552 3457 O
ATOM 108 CB THR A 14 28.114 69.092 60.105 1.00218.77 C
ANISOU 108 CB THR A 14 20704 30179 32239 5148 2722 4646 C
ATOM 109 OG1 THR A 14 28.280 69.485 61.444 1.00217.65 O
ANISOU 109 OG1 THR A 14 20739 29874 32083 5219 2610 4624 O
ATOM 110 CG2 THR A 14 29.230 69.748 59.303 1.00219.80 C
ANISOU 110 CG2 THR A 14 20909 30095 32509 5130 2841 5297 C
ATOM 111 N ARG A 15 24.935 68.919 61.150 1.00211.59 N
ANISOU 111 N ARG A 15 19692 29773 30928 5880 2034 3429 N
ATOM 112 CA ARG A 15 23.789 68.173 61.701 1.00211.14 C
ANISOU 112 CA ARG A 15 19440 29946 30837 5810 1944 2831 C
ATOM 113 C ARG A 15 22.507 68.315 60.871 1.00214.47 C
ANISOU 113 C ARG A 15 19753 30604 31130 6205 1691 2570 C
ATOM 114 O ARG A 15 21.545 67.607 61.155 1.00214.28 O
ANISOU 114 O ARG A 15 19521 30755 31139 6092 1659 2111 O
ATOM 115 CB ARG A 15 23.557 68.604 63.155 1.00210.68 C
ANISOU 115 CB ARG A 15 19507 29795 30749 5954 1747 2665 C
ATOM 116 CG ARG A 15 24.673 68.098 64.082 1.00206.73 C
ANISOU 116 CG ARG A 15 19060 29117 30372 5452 2031 2788 C
ATOM 117 CD ARG A 15 24.466 68.692 65.472 1.00206.62 C
ANISOU 117 CD ARG A 15 19190 29002 30312 5655 1812 2670 C
ATOM 118 NE ARG A 15 25.538 68.326 66.422 1.00202.97 N
ANISOU 118 NE ARG A 15 18822 28358 29938 5228 2049 2813 N
ATOM 119 CZ ARG A 15 25.593 68.772 67.665 1.00202.27 C
ANISOU 119 CZ ARG A 15 18869 28158 29825 5319 1920 2764 C
ATOM 120 NH1 ARG A 15 24.634 69.509 68.125 1.00204.83 N
ANISOU 120 NH1 ARG A 15 19238 28529 30058 5774 1565 2541 N
ATOM 121 NH2 ARG A 15 26.599 68.523 68.458 1.00199.15 N
ANISOU 121 NH2 ARG A 15 18586 27583 29498 4965 2122 2936 N
ATOM 122 N GLY A 16 22.487 69.190 59.860 1.00202.01 N
ANISOU 122 N GLY A 16 18340 29011 29405 6654 1500 2863 N
ATOM 123 CA GLY A 16 21.281 69.491 59.084 1.00205.53 C
ANISOU 123 CA GLY A 16 18771 29664 29656 7105 1194 2637 C
ATOM 124 C GLY A 16 20.182 70.137 59.934 1.00207.85 C
ANISOU 124 C GLY A 16 19191 29982 29801 7532 786 2324 C
ATOM 125 O GLY A 16 18.997 69.905 59.701 1.00209.69 O
ANISOU 125 O GLY A 16 19264 30431 29978 7668 653 1990 O
ATOM 126 N ASP A 17 20.557 70.899 60.966 1.00236.51 N
ANISOU 126 N ASP A 17 23091 33383 33388 7692 612 2439 N
ATOM 127 CA ASP A 17 19.598 71.558 61.852 1.00238.71 C
ANISOU 127 CA ASP A 17 23507 33651 33541 8049 242 2179 C
ATOM 128 C ASP A 17 19.027 72.814 61.182 1.00243.39 C
ANISOU 128 C ASP A 17 24546 34198 33734 8726 -273 2250 C
ATOM 129 O ASP A 17 19.558 73.919 61.303 1.00244.91 O
ANISOU 129 O ASP A 17 25258 34092 33705 9054 -588 2510 O
ATOM 130 CB ASP A 17 20.233 71.849 63.215 1.00236.69 C
ANISOU 130 CB ASP A 17 23386 33161 33386 7922 254 2252 C
ATOM 131 CG ASP A 17 19.230 72.432 64.222 1.00238.77 C
ANISOU 131 CG ASP A 17 23733 33420 33567 8211 -74 1988 C
ATOM 132 OD1 ASP A 17 19.616 72.500 65.406 1.00236.87 O
ANISOU 132 OD1 ASP A 17 23526 33026 33448 8051 -35 1977 O
ATOM 133 OD2 ASP A 17 18.111 72.846 63.831 1.00242.30 O1-
ANISOU 133 OD2 ASP A 17 24234 34025 33806 8588 -355 1823 O1-
ATOM 134 N VAL A 18 17.921 72.631 60.457 1.00229.27 N
ANISOU 134 N VAL A 18 22619 32681 31810 8913 -386 1998 N
ATOM 135 CA VAL A 18 17.241 73.696 59.706 1.00233.88 C
ANISOU 135 CA VAL A 18 23649 33273 31944 9530 -886 1969 C
ATOM 136 C VAL A 18 16.864 74.880 60.593 1.00236.55 C
ANISOU 136 C VAL A 18 24446 33424 32008 9931 -1329 1913 C
ATOM 137 O VAL A 18 17.004 76.023 60.158 1.00239.61 O
ANISOU 137 O VAL A 18 25465 33566 32008 10363 -1781 2040 O
ATOM 138 CB VAL A 18 15.984 73.146 59.002 1.00235.73 C
ANISOU 138 CB VAL A 18 23572 33893 32100 9592 -873 1644 C
ATOM 139 CG1 VAL A 18 15.289 74.219 58.152 1.00240.56 C
ANISOU 139 CG1 VAL A 18 24683 34523 32195 10220 -1401 1564 C
ATOM 140 CG2 VAL A 18 16.332 71.982 58.071 1.00233.27 C
ANISOU 140 CG2 VAL A 18 22840 33746 32047 9169 -448 1685 C
ATOM 141 N LYS A 19 16.412 74.635 61.830 1.00259.42 N
ANISOU 141 N LYS A 19 27089 36396 35082 9765 -1224 1729 N
ATOM 142 CA LYS A 19 15.952 75.701 62.729 1.00262.04 C
ANISOU 142 CA LYS A 19 27797 36609 35157 10119 -1602 1655 C
ATOM 143 C LYS A 19 17.133 76.577 63.134 1.00261.43 C
ANISOU 143 C LYS A 19 28233 36071 35029 10179 -1782 1979 C
ATOM 144 O LYS A 19 17.137 77.769 62.836 1.00264.83 O
ANISOU 144 O LYS A 19 29309 36259 35053 10593 -2250 2060 O
ATOM 145 CB LYS A 19 15.231 75.094 63.945 1.00260.77 C
ANISOU 145 CB LYS A 19 27195 36655 35229 9871 -1389 1418 C
ATOM 146 CG LYS A 19 14.688 76.196 64.867 1.00263.72 C
ANISOU 146 CG LYS A 19 27927 36965 35309 10249 -1756 1336 C
ATOM 147 CD LYS A 19 14.208 75.640 66.211 1.00262.02 C
ANISOU 147 CD LYS A 19 27319 36885 35352 9971 -1533 1181 C
ATOM 148 CE LYS A 19 13.947 76.842 67.124 1.00264.70 C
ANISOU 148 CE LYS A 19 28070 37106 35398 10339 -1888 1164 C
ATOM 149 NZ LYS A 19 13.970 76.495 68.562 1.00262.32 N
ANISOU 149 NZ LYS A 19 27507 36772 35388 10043 -1691 1132 N
ATOM 150 N SER A 20 18.152 75.969 63.735 1.00269.97 N
ANISOU 150 N SER A 20 29075 37012 36489 9736 -1422 2157 N
ATOM 151 CA SER A 20 19.318 76.696 64.242 1.00268.98 C
ANISOU 151 CA SER A 20 29394 36460 36348 9724 -1538 2484 C
ATOM 152 C SER A 20 20.070 77.402 63.110 1.00270.69 C
ANISOU 152 C SER A 20 30191 36384 36276 9939 -1789 2831 C
ATOM 153 O SER A 20 20.472 78.555 63.249 1.00272.81 O
ANISOU 153 O SER A 20 31145 36254 36256 10167 -2198 3024 O
ATOM 154 CB SER A 20 20.246 75.730 64.982 1.00263.96 C
ANISOU 154 CB SER A 20 28339 35807 36146 9169 -1038 2575 C
ATOM 155 OG SER A 20 19.542 75.083 66.025 1.00262.52 O
ANISOU 155 OG SER A 20 27721 35829 36194 8942 -865 2242 O
ATOM 156 N VAL A 21 20.213 76.759 61.946 1.00275.12 N
ANISOU 156 N VAL A 21 30542 37114 36876 9851 -1581 2912 N
ATOM 157 CA VAL A 21 20.918 77.355 60.798 1.00276.75 C
ANISOU 157 CA VAL A 21 31316 37037 36799 10022 -1809 3276 C
ATOM 158 C VAL A 21 20.129 78.507 60.172 1.00281.91 C
ANISOU 158 C VAL A 21 32661 37540 36910 10542 -2461 3122 C
ATOM 159 O VAL A 21 20.742 79.506 59.783 1.00283.99 O
ANISOU 159 O VAL A 21 33735 37340 36829 10677 -2867 3398 O
ATOM 160 CB VAL A 21 21.284 76.268 59.771 1.00274.54 C
ANISOU 160 CB VAL A 21 30545 37018 36751 9737 -1342 3422 C
ATOM 161 CG1 VAL A 21 21.939 76.792 58.486 1.00276.33 C
ANISOU 161 CG1 VAL A 21 31329 36983 36683 9892 -1553 3833 C
ATOM 162 CG2 VAL A 21 22.304 75.319 60.419 1.00269.68 C
ANISOU 162 CG2 VAL A 21 29419 36433 36617 9149 -723 3641 C
ATOM 163 N SER A 22 18.796 78.414 60.100 1.00239.58 N
ANISOU 163 N SER A 22 27060 32531 31438 10780 -2575 2691 N
ATOM 164 CA SER A 22 17.948 79.515 59.625 1.00244.66 C
ANISOU 164 CA SER A 22 28337 33074 31551 11262 -3167 2484 C
ATOM 165 C SER A 22 17.953 80.693 60.602 1.00246.81 C
ANISOU 165 C SER A 22 29181 33011 31583 11432 -3551 2479 C
ATOM 166 O SER A 22 18.020 81.838 60.159 1.00250.42 O
ANISOU 166 O SER A 22 30463 33098 31588 11677 -4065 2532 O
ATOM 167 CB SER A 22 16.514 79.026 59.396 1.00246.32 C
ANISOU 167 CB SER A 22 28069 33805 31717 11439 -3111 2039 C
ATOM 168 OG SER A 22 15.705 80.069 58.874 1.00251.34 O
ANISOU 168 OG SER A 22 29313 34367 31817 11910 -3660 1822 O
ATOM 169 N GLU A 23 17.901 80.440 61.912 1.00275.43 N
ANISOU 169 N GLU A 23 32415 36740 35495 11264 -3314 2412 N
ATOM 170 CA GLU A 23 17.946 81.488 62.943 1.00277.10 C
ANISOU 170 CA GLU A 23 33091 36668 35526 11389 -3616 2418 C
ATOM 171 C GLU A 23 19.285 82.236 62.931 1.00276.67 C
ANISOU 171 C GLU A 23 33717 36021 35383 11234 -3812 2845 C
ATOM 172 O GLU A 23 19.295 83.468 62.944 1.00280.20 O
ANISOU 172 O GLU A 23 34932 36113 35418 11431 -4290 2868 O
ATOM 173 CB GLU A 23 17.674 80.877 64.329 1.00274.35 C
ANISOU 173 CB GLU A 23 32111 36572 35559 11175 -3260 2281 C
ATOM 174 CG GLU A 23 16.184 80.542 64.520 1.00276.26 C
ANISOU 174 CG GLU A 23 31925 37321 35719 11374 -3222 1854 C
ATOM 175 CD GLU A 23 15.865 79.815 65.841 1.00273.51 C
ANISOU 175 CD GLU A 23 30960 37217 35744 11094 -2860 1726 C
ATOM 176 OE1 GLU A 23 14.668 79.503 66.055 1.00275.03 O
ANISOU 176 OE1 GLU A 23 30822 37817 35861 11208 -2816 1415 O
ATOM 177 OE2 GLU A 23 16.790 79.533 66.632 1.00269.93 O1-
ANISOU 177 OE2 GLU A 23 30374 36546 35640 10747 -2629 1930 O1-
ATOM 178 N ILE A 24 20.408 81.515 62.810 1.00298.73 N
ANISOU 178 N ILE A 24 36280 38707 38515 10859 -3450 3182 N
ATOM 179 CA ILE A 24 21.730 82.143 62.678 1.00298.31 C
ANISOU 179 CA ILE A 24 36893 38099 38350 10652 -3605 3638 C
ATOM 180 C ILE A 24 21.786 83.005 61.415 1.00302.26 C
ANISOU 180 C ILE A 24 38242 38271 38333 10819 -4096 3748 C
ATOM 181 O ILE A 24 22.235 84.144 61.495 1.00304.74 O
ANISOU 181 O ILE A 24 39378 38100 38310 10784 -4510 3912 O
ATOM 182 CB ILE A 24 22.865 81.093 62.697 1.00293.37 C
ANISOU 182 CB ILE A 24 35801 37507 38159 10225 -3048 3980 C
ATOM 183 CG1 ILE A 24 22.956 80.385 64.067 1.00289.54 C
ANISOU 183 CG1 ILE A 24 34632 37235 38145 9974 -2617 3860 C
ATOM 184 CG2 ILE A 24 24.224 81.755 62.388 1.00293.38 C
ANISOU 184 CG2 ILE A 24 36569 36936 37968 9978 -3207 4507 C
ATOM 185 CD1 ILE A 24 23.747 79.068 64.009 1.00284.72 C
ANISOU 185 CD1 ILE A 24 33345 36849 37985 9541 -1947 4049 C
ATOM 186 N TYR A 25 21.301 82.504 60.271 1.00262.77 N
ANISOU 186 N TYR A 25 33069 33522 33251 10961 -4066 3634 N
ATOM 187 CA TYR A 25 21.329 83.246 59.004 1.00266.45 C
ANISOU 187 CA TYR A 25 34346 33672 33223 11080 -4534 3713 C
ATOM 188 C TYR A 25 20.531 84.558 59.062 1.00271.65 C
ANISOU 188 C TYR A 25 35702 34129 33386 11403 -5126 3423 C
ATOM 189 O TYR A 25 21.025 85.592 58.616 1.00274.51 O
ANISOU 189 O TYR A 25 36981 33976 33344 11308 -5559 3600 O
ATOM 190 CB TYR A 25 20.806 82.351 57.876 1.00266.10 C
ANISOU 190 CB TYR A 25 33842 34028 33237 11201 -4343 3579 C
ATOM 191 CG TYR A 25 20.890 82.983 56.497 1.00269.50 C
ANISOU 191 CG TYR A 25 35084 34130 33183 11273 -4797 3673 C
ATOM 192 CD1 TYR A 25 19.719 83.363 55.812 1.00273.41 C
ANISOU 192 CD1 TYR A 25 35751 34784 33348 11654 -5151 3271 C
ATOM 193 CD2 TYR A 25 22.149 83.217 55.911 1.00268.89 C
ANISOU 193 CD2 TYR A 25 35640 33570 32956 10908 -4864 4170 C
ATOM 194 CE1 TYR A 25 19.804 83.944 54.532 1.00276.55 C
ANISOU 194 CE1 TYR A 25 36922 34853 33301 11675 -5577 3343 C
ATOM 195 CE2 TYR A 25 22.239 83.785 54.626 1.00272.06 C
ANISOU 195 CE2 TYR A 25 36802 33642 32928 10730 -5231 4217 C
ATOM 196 CZ TYR A 25 21.065 84.140 53.930 1.00275.83 C
ANISOU 196 CZ TYR A 25 37463 34267 33072 11260 -5651 3834 C
ATOM 197 OH TYR A 25 21.152 84.661 52.678 1.00278.84 O
ANISOU 197 OH TYR A 25 38590 34324 33031 11135 -6026 3892 O
ATOM 198 N GLN A 26 19.331 84.534 59.657 1.00275.73 N
ANISOU 198 N GLN A 26 35800 35047 33917 11735 -5121 2987 N
ATOM 199 CA GLN A 26 18.486 85.725 59.833 1.00280.70 C
ANISOU 199 CA GLN A 26 36999 35571 34083 12093 -5614 2673 C
ATOM 200 C GLN A 26 19.093 86.742 60.821 1.00281.55 C
ANISOU 200 C GLN A 26 37645 35252 34078 11970 -5820 2831 C
ATOM 201 O GLN A 26 18.810 87.935 60.739 1.00285.95 O
ANISOU 201 O GLN A 26 38937 35529 34183 12163 -6288 2695 O
ATOM 202 CB GLN A 26 17.081 85.286 60.286 1.00281.50 C
ANISOU 202 CB GLN A 26 36434 36273 34250 12435 -5470 2198 C
ATOM 203 CG GLN A 26 16.308 84.493 59.213 1.00281.82 C
ANISOU 203 CG GLN A 26 36055 36731 34293 12591 -5356 1978 C
ATOM 204 CD GLN A 26 15.899 85.319 57.996 1.00286.51 C
ANISOU 204 CD GLN A 26 37394 37110 34357 12874 -5870 1838 C
ATOM 205 OE1 GLN A 26 15.785 86.528 58.031 1.00290.46 O
ANISOU 205 OE1 GLN A 26 38666 37262 34434 13054 -6335 1753 O
ATOM 206 NE2 GLN A 26 15.647 84.703 56.860 1.00286.38 N
ANISOU 206 NE2 GLN A 26 37182 37289 34341 12910 -5805 1789 N
ATOM 207 N GLY A 27 19.962 86.289 61.733 1.00304.02 N
ANISOU 207 N GLY A 27 40145 38036 37332 11633 -5469 3115 N
ATOM 208 CA GLY A 27 20.694 87.144 62.668 1.00304.19 C
ANISOU 208 CA GLY A 27 40620 37654 37305 11442 -5606 3320 C
ATOM 209 C GLY A 27 21.930 87.851 62.089 1.00304.96 C
ANISOU 209 C GLY A 27 41558 37143 37169 11070 -5848 3745 C
ATOM 210 O GLY A 27 22.465 88.740 62.751 1.00306.02 O
ANISOU 210 O GLY A 27 42173 36926 37173 10914 -6028 3882 O
ATOM 211 N LEU A 28 22.400 87.495 60.884 1.00307.17 N
ANISOU 211 N LEU A 28 42039 37299 37374 10888 -5849 3960 N
ATOM 212 CA LEU A 28 23.610 88.089 60.291 1.00307.85 C
ANISOU 212 CA LEU A 28 42923 36823 37221 10428 -6041 4390 C
ATOM 213 C LEU A 28 23.348 89.508 59.775 1.00313.55 C
ANISOU 213 C LEU A 28 44619 37166 37350 10512 -6632 4251 C
ATOM 214 O LEU A 28 22.453 89.741 58.950 1.00316.87 O
ANISOU 214 O LEU A 28 45238 37684 37473 10845 -6910 3943 O
ATOM 215 CB LEU A 28 24.192 87.205 59.174 1.00305.61 C
ANISOU 215 CB LEU A 28 42541 36547 37029 10175 -5825 4673 C
ATOM 216 CG LEU A 28 24.536 85.774 59.602 1.00300.05 C
ANISOU 216 CG LEU A 28 40880 36220 36904 10082 -5194 4815 C
ATOM 217 CD1 LEU A 28 25.096 84.986 58.423 1.00298.37 C
ANISOU 217 CD1 LEU A 28 40634 36024 36711 9872 -4974 5102 C
ATOM 218 CD2 LEU A 28 25.540 85.697 60.752 1.00296.74 C
ANISOU 218 CD2 LEU A 28 40320 35631 36797 9725 -4913 5118 C
ATOM 219 N GLN A 29 24.166 90.456 60.239 1.00324.64 N
ANISOU 219 N GLN A 29 46631 38133 38582 10185 -6810 4472 N
ATOM 220 CA GLN A 29 23.927 91.888 60.048 1.00330.10 C
ANISOU 220 CA GLN A 29 48198 38474 38752 10271 -7337 4293 C
ATOM 221 C GLN A 29 24.641 92.457 58.817 1.00332.64 C
ANISOU 221 C GLN A 29 49357 38345 38685 9849 -7622 4529 C
ATOM 222 O GLN A 29 24.165 93.443 58.255 1.00337.58 O
ANISOU 222 O GLN A 29 50655 38750 38860 10011 -8076 4286 O
ATOM 223 CB GLN A 29 24.335 92.655 61.316 1.00330.35 C
ANISOU 223 CB GLN A 29 48387 38322 38808 10174 -7367 4344 C
ATOM 224 CG GLN A 29 23.510 92.234 62.544 1.00328.58 C
ANISOU 224 CG GLN A 29 47412 38532 38900 10592 -7141 4060 C
ATOM 225 CD GLN A 29 23.793 93.066 63.791 1.00329.26 C
ANISOU 225 CD GLN A 29 47687 38446 38970 10548 -7211 4067 C
ATOM 226 OE1 GLN A 29 24.553 94.024 63.803 1.00331.31 O
ANISOU 226 OE1 GLN A 29 48633 38273 38975 10245 -7440 4249 O
ATOM 227 NE2 GLN A 29 23.170 92.732 64.902 1.00327.67 N
ANISOU 227 NE2 GLN A 29 46873 38594 39035 10834 -7008 3855 N
ATOM 228 N SER A 30 25.753 91.857 58.386 1.00309.47 N
ANISOU 228 N SER A 30 46401 35278 35907 9299 -7359 4981 N
ATOM 229 CA SER A 30 26.527 92.323 57.226 1.00311.62 C
ANISOU 229 CA SER A 30 47435 35147 35819 8783 -7574 5241 C
ATOM 230 C SER A 30 26.572 91.313 56.079 1.00309.73 C
ANISOU 230 C SER A 30 46980 35053 35651 8668 -7401 5381 C
ATOM 231 O SER A 30 26.533 90.099 56.283 1.00305.40 O
ANISOU 231 O SER A 30 45665 34851 35522 8775 -6982 5462 O
ATOM 232 CB SER A 30 27.935 92.732 57.660 1.00310.50 C
ANISOU 232 CB SER A 30 47626 34666 35685 8111 -7455 5668 C
ATOM 233 OG SER A 30 28.681 91.616 58.087 1.00305.06 O
ANISOU 233 OG SER A 30 46310 34149 35451 7829 -6936 6014 O
ATOM 234 N ASP A 31 26.709 91.816 54.850 1.00292.29 N
ANISOU 234 N ASP A 31 45463 32566 33028 8414 -7714 5418 N
ATOM 235 CA ASP A 31 26.830 90.968 53.658 1.00290.93 C
ANISOU 235 CA ASP A 31 45206 32479 32857 8230 -7589 5577 C
ATOM 236 C ASP A 31 28.131 90.148 53.660 1.00286.54 C
ANISOU 236 C ASP A 31 44445 31870 32557 7579 -7139 6103 C
ATOM 237 O ASP A 31 28.144 89.009 53.202 1.00283.40 O
ANISOU 237 O ASP A 31 43577 31712 32390 7591 -6828 6225 O
ATOM 238 CB ASP A 31 26.685 91.826 52.392 1.00295.87 C
ANISOU 238 CB ASP A 31 46678 32787 32952 8066 -8055 5480 C
ATOM 239 CG ASP A 31 25.265 92.384 52.217 1.00299.90 C
ANISOU 239 CG ASP A 31 47298 33414 33236 8778 -8449 4932 C
ATOM 240 OD1 ASP A 31 25.144 93.465 51.602 1.00304.74 O
ANISOU 240 OD1 ASP A 31 48703 33682 33401 8701 -8894 4790 O
ATOM 241 OD2 ASP A 31 24.300 91.751 52.729 1.00298.31 O1-
ANISOU 241 OD2 ASP A 31 46381 33654 33307 9386 -8292 4638 O1-
ATOM 242 N ALA A 32 29.197 90.659 54.281 1.00308.78 N
ANISOU 242 N ALA A 32 47533 34419 35370 7052 -7057 6394 N
ATOM 243 CA ALA A 32 30.436 89.910 54.488 1.00304.55 C
ANISOU 243 CA ALA A 32 46751 33861 35104 6435 -6588 6870 C
ATOM 244 C ALA A 32 30.242 88.695 55.421 1.00299.37 C
ANISOU 244 C ALA A 32 45147 33584 35018 6798 -6106 6885 C
ATOM 245 O ALA A 32 30.722 87.598 55.116 1.00295.75 O
ANISOU 245 O ALA A 32 44195 33323 34855 6482 -5614 7088 O
ATOM 246 CB ALA A 32 31.491 90.889 55.012 1.00305.89 C
ANISOU 246 CB ALA A 32 47409 33704 35112 5865 -6644 7087 C
ATOM 247 N GLU A 33 29.478 88.849 56.512 1.00309.85 N
ANISOU 247 N GLU A 33 46059 35117 36555 7373 -6133 6572 N
ATOM 248 CA GLU A 33 29.115 87.740 57.404 1.00305.42 C
ANISOU 248 CA GLU A 33 44532 34978 36533 7780 -5686 6488 C
ATOM 249 C GLU A 33 28.247 86.714 56.662 1.00304.33 C
ANISOU 249 C GLU A 33 43846 35257 36528 8241 -5525 6278 C
ATOM 250 O GLU A 33 28.514 85.513 56.732 1.00300.16 O
ANISOU 250 O GLU A 33 42370 35150 36528 7880 -4810 6274 O
ATOM 251 CB GLU A 33 28.366 88.264 58.642 1.00306.25 C
ANISOU 251 CB GLU A 33 44372 35226 36764 8244 -5809 6140 C
ATOM 252 CG GLU A 33 29.283 88.967 59.665 1.00305.84 C
ANISOU 252 CG GLU A 33 44576 34886 36742 7849 -5789 6371 C
ATOM 253 CD GLU A 33 28.553 89.908 60.640 1.00308.45 C
ANISOU 253 CD GLU A 33 44983 35231 36983 8247 -6070 6022 C
ATOM 254 OE1 GLU A 33 29.193 90.333 61.632 1.00307.53 O
ANISOU 254 OE1 GLU A 33 44910 34967 36972 8015 -5991 6175 O
ATOM 255 OE2 GLU A 33 27.426 90.357 60.296 1.00311.99 O1-
ANISOU 255 OE2 GLU A 33 45580 35784 37176 8730 -6407 5617 O1-
ATOM 256 N ARG A 34 27.253 87.178 55.889 1.00299.63 N
ANISOU 256 N ARG A 34 43527 34706 35613 8601 -5937 5929 N
ATOM 257 CA ARG A 34 26.391 86.306 55.068 1.00299.16 C
ANISOU 257 CA ARG A 34 42902 35091 35675 8906 -5762 5654 C
ATOM 258 C ARG A 34 27.181 85.543 54.015 1.00297.23 C
ANISOU 258 C ARG A 34 42398 34933 35602 8033 -5248 5835 C
ATOM 259 O ARG A 34 26.951 84.350 53.848 1.00294.09 O
ANISOU 259 O ARG A 34 41044 35040 35659 7914 -4658 5682 O
ATOM 260 CB ARG A 34 25.288 87.120 54.385 1.00304.16 C
ANISOU 260 CB ARG A 34 44048 35665 35852 9400 -6364 5281 C
ATOM 261 CG ARG A 34 24.267 87.662 55.388 1.00305.98 C
ANISOU 261 CG ARG A 34 44041 36098 36118 9914 -6525 4835 C
ATOM 262 CD ARG A 34 23.327 88.615 54.658 1.00311.42 C
ANISOU 262 CD ARG A 34 45325 36679 36322 10225 -7063 4465 C
ATOM 263 NE ARG A 34 22.484 89.349 55.606 1.00313.87 N
ANISOU 263 NE ARG A 34 45610 37088 36559 10645 -7259 4080 N
ATOM 264 CZ ARG A 34 21.761 90.408 55.308 1.00318.94 C
ANISOU 264 CZ ARG A 34 46847 37571 36763 10919 -7733 3754 C
ATOM 265 NH1 ARG A 34 21.831 91.012 54.148 1.00322.39 N
ANISOU 265 NH1 ARG A 34 48027 37681 36783 10779 -8102 3766 N
ATOM 266 NH2 ARG A 34 20.950 90.879 56.211 1.00320.68 N
ANISOU 266 NH2 ARG A 34 46923 37962 36957 11333 -7831 3400 N
ATOM 267 N LEU A 35 28.144 86.184 53.352 1.00275.49 N
ANISOU 267 N LEU A 35 40459 31716 32498 7403 -5447 6166 N
ATOM 268 CA LEU A 35 29.012 85.531 52.373 1.00273.85 C
ANISOU 268 CA LEU A 35 40055 31582 32414 6533 -4977 6367 C
ATOM 269 C LEU A 35 29.832 84.412 53.020 1.00268.58 C
ANISOU 269 C LEU A 35 38466 31232 32349 6030 -4177 6531 C
ATOM 270 O LEU A 35 29.875 83.293 52.505 1.00265.91 O
ANISOU 270 O LEU A 35 37357 31302 32376 5719 -3609 6446 O
ATOM 271 CB LEU A 35 29.928 86.587 51.729 1.00277.09 C
ANISOU 271 CB LEU A 35 41594 31412 32277 5973 -5412 6717 C
ATOM 272 CG LEU A 35 30.908 86.015 50.690 1.00275.83 C
ANISOU 272 CG LEU A 35 41304 31322 32177 5036 -4966 6948 C
ATOM 273 CD1 LEU A 35 30.193 85.326 49.527 1.00276.10 C
ANISOU 273 CD1 LEU A 35 40923 31702 32281 5093 -4801 6662 C
ATOM 274 CD2 LEU A 35 31.775 87.134 50.116 1.00279.42 C
ANISOU 274 CD2 LEU A 35 42910 31213 32042 4492 -5446 7296 C
ATOM 275 N GLN A 36 30.460 84.699 54.164 1.00301.73 N
ANISOU 275 N GLN A 36 42745 35246 36654 5976 -4140 6754 N
ATOM 276 CA GLN A 36 31.234 83.711 54.913 1.00296.83 C
ANISOU 276 CA GLN A 36 41294 34895 36593 5557 -3424 6906 C
ATOM 277 C GLN A 36 30.352 82.535 55.361 1.00293.67 C
ANISOU 277 C GLN A 36 39771 35081 36730 5993 -2960 6562 C
ATOM 278 O GLN A 36 30.759 81.371 55.255 1.00290.03 O
ANISOU 278 O GLN A 36 38505 34975 36718 5564 -2298 6578 O
ATOM 279 CB GLN A 36 31.903 84.409 56.106 1.00296.43 C
ANISOU 279 CB GLN A 36 41642 34496 36493 5550 -3590 7177 C
ATOM 280 CG GLN A 36 32.899 83.477 56.811 1.00291.57 C
ANISOU 280 CG GLN A 36 40285 34093 36405 5011 -2867 7387 C
ATOM 281 CD GLN A 36 33.609 84.124 57.994 1.00290.96 C
ANISOU 281 CD GLN A 36 40570 33680 36301 4967 -2995 7667 C
ATOM 282 OE1 GLN A 36 33.202 85.125 58.560 1.00293.51 O
ANISOU 282 OE1 GLN A 36 41518 33683 36318 5477 -3568 7655 O
ATOM 283 NE2 GLN A 36 34.709 83.556 58.439 1.00287.51 N
ANISOU 283 NE2 GLN A 36 39741 33312 36190 4366 -2459 7927 N
ATOM 284 N TYR A 37 29.133 82.827 55.813 1.00315.63 N
ANISOU 284 N TYR A 37 42505 37980 39438 6837 -3320 6243 N
ATOM 285 CA TYR A 37 28.160 81.823 56.222 1.00313.33 C
ANISOU 285 CA TYR A 37 41214 38260 39578 7302 -2970 5894 C
ATOM 286 C TYR A 37 27.658 80.967 55.057 1.00313.13 C
ANISOU 286 C TYR A 37 40710 38606 39658 7169 -2699 5674 C
ATOM 287 O TYR A 37 27.595 79.747 55.180 1.00309.63 O
ANISOU 287 O TYR A 37 39334 38612 39700 7009 -2097 5573 O
ATOM 288 CB TYR A 37 26.987 82.520 56.904 1.00315.91 C
ANISOU 288 CB TYR A 37 41734 38608 39691 8244 -3515 5611 C
ATOM 289 CG TYR A 37 26.082 81.554 57.628 1.00313.39 C
ANISOU 289 CG TYR A 37 40374 38882 39819 8715 -3153 5294 C
ATOM 290 CD1 TYR A 37 24.873 81.128 57.048 1.00314.67 C
ANISOU 290 CD1 TYR A 37 40126 39468 39965 9166 -3201 4907 C
ATOM 291 CD2 TYR A 37 26.458 81.095 58.900 1.00309.86 C
ANISOU 291 CD2 TYR A 37 39379 38564 39789 8685 -2777 5392 C
ATOM 292 CE1 TYR A 37 23.999 80.296 57.774 1.00312.68 C
ANISOU 292 CE1 TYR A 37 38941 39782 40083 9608 -2909 4615 C
ATOM 293 CE2 TYR A 37 25.589 80.266 59.623 1.00307.84 C
ANISOU 293 CE2 TYR A 37 38203 38853 39909 9129 -2489 5099 C
ATOM 294 CZ TYR A 37 24.356 79.884 59.074 1.00309.34 C
ANISOU 294 CZ TYR A 37 38002 39478 40055 9590 -2565 4714 C
ATOM 295 OH TYR A 37 23.512 79.152 59.836 1.00307.68 O
ANISOU 295 OH TYR A 37 36944 39794 40168 9967 -2318 4420 O
ATOM 296 N LEU A 38 27.350 81.566 53.902 1.00264.29 N
ANISOU 296 N LEU A 38 35166 32226 33025 7194 -3126 5612 N
ATOM 297 CA LEU A 38 26.881 80.839 52.719 1.00264.40 C
ANISOU 297 CA LEU A 38 34808 32554 33098 7065 -2913 5412 C
ATOM 298 C LEU A 38 27.965 79.942 52.127 1.00261.39 C
ANISOU 298 C LEU A 38 34048 32265 33002 6187 -2294 5646 C
ATOM 299 O LEU A 38 27.655 78.826 51.716 1.00259.23 O
ANISOU 299 O LEU A 38 32998 32426 33069 6082 -1829 5475 O
ATOM 300 CB LEU A 38 26.350 81.818 51.662 1.00269.30 C
ANISOU 300 CB LEU A 38 36306 32883 33131 7303 -3572 5309 C
ATOM 301 CG LEU A 38 24.967 82.408 51.992 1.00272.35 C
ANISOU 301 CG LEU A 38 36850 33359 33271 8272 -4123 4944 C
ATOM 302 CD1 LEU A 38 24.600 83.399 50.903 1.00277.21 C
ANISOU 302 CD1 LEU A 38 38413 33627 33288 8430 -4776 4878 C
ATOM 303 CD2 LEU A 38 23.846 81.370 52.046 1.00270.77 C
ANISOU 303 CD2 LEU A 38 35657 33803 33422 8709 -3799 4555 C
ATOM 304 N LYS A 39 29.238 80.358 52.144 1.00237.65 N
ANISOU 304 N LYS A 39 31527 28892 29878 5560 -2258 6029 N
ATOM 305 CA LYS A 39 30.360 79.471 51.791 1.00234.50 C
ANISOU 305 CA LYS A 39 30694 28625 29779 4743 -1631 6257 C
ATOM 306 C LYS A 39 30.405 78.241 52.707 1.00229.80 C
ANISOU 306 C LYS A 39 29038 28460 29813 4744 -980 6182 C
ATOM 307 O LYS A 39 30.485 77.113 52.217 1.00227.42 O
ANISOU 307 O LYS A 39 28047 28520 29841 4443 -463 6100 O
ATOM 308 CB LYS A 39 31.688 80.240 51.845 1.00235.25 C
ANISOU 308 CB LYS A 39 31511 28268 29605 4133 -1754 6680 C
ATOM 309 CG LYS A 39 31.888 81.205 50.667 1.00239.53 C
ANISOU 309 CG LYS A 39 33027 28431 29551 3872 -2261 6802 C
ATOM 310 CD LYS A 39 33.274 81.854 50.769 1.00240.02 C
ANISOU 310 CD LYS A 39 33719 28108 29370 3185 -2318 7239 C
ATOM 311 CE LYS A 39 33.622 82.654 49.509 1.00243.99 C
ANISOU 311 CE LYS A 39 35117 28286 29303 2766 -2731 7392 C
ATOM 312 NZ LYS A 39 35.087 82.897 49.438 1.00243.71 N
ANISOU 312 NZ LYS A 39 35425 28050 29124 1923 -2578 7812 N
ATOM 313 N LEU A 40 30.290 78.448 54.024 1.00263.66 N
ANISOU 313 N LEU A 40 33204 32716 34259 5114 -1026 6189 N
ATOM 314 CA LEU A 40 30.256 77.360 55.006 1.00259.42 C
ANISOU 314 CA LEU A 40 31706 32565 34298 5172 -466 6107 C
ATOM 315 C LEU A 40 29.047 76.435 54.784 1.00258.69 C
ANISOU 315 C LEU A 40 30846 32985 34460 5595 -274 5716 C
ATOM 316 O LEU A 40 29.211 75.218 54.734 1.00255.48 O
ANISOU 316 O LEU A 40 29651 32939 34482 5304 306 5664 O
ATOM 317 CB LEU A 40 30.269 77.962 56.427 1.00258.99 C
ANISOU 317 CB LEU A 40 31798 32330 34277 5553 -667 6182 C
ATOM 318 CG LEU A 40 30.208 76.919 57.557 1.00254.75 C
ANISOU 318 CG LEU A 40 30309 32166 34318 5645 -130 6100 C
ATOM 319 CD1 LEU A 40 31.458 76.043 57.594 1.00251.05 C
ANISOU 319 CD1 LEU A 40 29416 31762 34209 4887 503 6347 C
ATOM 320 CD2 LEU A 40 30.060 77.613 58.910 1.00254.82 C
ANISOU 320 CD2 LEU A 40 30509 31999 34311 6112 -404 6139 C
ATOM 321 N LEU A 41 27.855 77.005 54.602 1.00267.98 N
ANISOU 321 N LEU A 41 32271 34198 35351 6262 -768 5443 N
ATOM 322 CA LEU A 41 26.621 76.267 54.337 1.00267.96 C
ANISOU 322 CA LEU A 41 31620 34684 35507 6700 -668 5061 C
ATOM 323 C LEU A 41 26.722 75.445 53.045 1.00267.43 C
ANISOU 323 C LEU A 41 31272 34817 35521 6246 -342 5015 C
ATOM 324 O LEU A 41 26.338 74.277 53.024 1.00265.01 O
ANISOU 324 O LEU A 41 30134 34961 35598 6216 111 4839 O
ATOM 325 CB LEU A 41 25.460 77.279 54.285 1.00272.18 C
ANISOU 325 CB LEU A 41 32670 35142 35603 7477 -1358 4812 C
ATOM 326 CG LEU A 41 24.067 76.646 54.124 1.00272.64 C
ANISOU 326 CG LEU A 41 32082 35737 35770 8026 -1326 4393 C
ATOM 327 CD1 LEU A 41 23.691 75.822 55.349 1.00269.53 C
ANISOU 327 CD1 LEU A 41 30803 35772 35833 8270 -948 4263 C
ATOM 328 CD2 LEU A 41 23.010 77.733 53.962 1.00277.22 C
ANISOU 328 CD2 LEU A 41 33259 36217 35854 8775 -2046 4152 C
ATOM 329 N CYS A 42 27.294 76.026 51.987 1.00277.70 N
ANISOU 329 N CYS A 42 33265 35783 36466 5855 -560 5187 N
ATOM 330 CA CYS A 42 27.436 75.396 50.679 1.00277.66 C
ANISOU 330 CA CYS A 42 33110 35917 36470 5420 -317 5160 C
ATOM 331 C CYS A 42 28.222 74.082 50.760 1.00273.38 C
ANISOU 331 C CYS A 42 31787 35655 36428 4839 418 5266 C
ATOM 332 O CYS A 42 27.798 73.071 50.192 1.00272.12 O
ANISOU 332 O CYS A 42 31018 35871 36506 4778 753 5078 O
ATOM 333 CB CYS A 42 28.125 76.396 49.740 1.00280.73 C
ANISOU 333 CB CYS A 42 34464 35835 36365 5042 -700 5395 C
ATOM 334 SG CYS A 42 28.224 75.700 48.074 1.00281.06 S
ANISOU 334 SG CYS A 42 34363 36052 36376 4552 -452 5343 S
ATOM 335 N VAL A 43 29.345 74.094 51.485 1.00224.04 N
ANISOU 335 N VAL A 43 25562 29231 30333 4436 653 5557 N
ATOM 336 CA VAL A 43 30.265 72.954 51.589 1.00220.18 C
ANISOU 336 CA VAL A 43 24433 28952 30273 3852 1318 5690 C
ATOM 337 C VAL A 43 29.883 71.999 52.718 1.00216.77 C
ANISOU 337 C VAL A 43 23138 28877 30347 4104 1714 5541 C
ATOM 338 O VAL A 43 29.991 70.787 52.542 1.00214.11 O
ANISOU 338 O VAL A 43 22098 28874 30379 3847 2224 5465 O
ATOM 339 CB VAL A 43 31.716 73.457 51.747 1.00219.76 C
ANISOU 339 CB VAL A 43 24854 28546 30100 3259 1371 6081 C
ATOM 340 CG1 VAL A 43 32.704 72.307 51.974 1.00215.80 C
ANISOU 340 CG1 VAL A 43 23688 28270 30036 2699 2047 6210 C
ATOM 341 CG2 VAL A 43 32.152 74.231 50.497 1.00223.04 C
ANISOU 341 CG2 VAL A 43 26051 28669 30025 2895 1046 6232 C
ATOM 342 N MET A 44 29.437 72.498 53.874 1.00244.93 N
ANISOU 342 N MET A 44 26744 32385 33934 4599 1485 5494 N
ATOM 343 CA MET A 44 29.266 71.670 55.075 1.00241.58 C
ANISOU 343 CA MET A 44 25555 32253 33980 4762 1865 5410 C
ATOM 344 C MET A 44 27.848 71.130 55.277 1.00241.75 C
ANISOU 344 C MET A 44 24995 32711 34147 5344 1848 5036 C
ATOM 345 O MET A 44 27.695 70.175 56.040 1.00238.80 O
ANISOU 345 O MET A 44 23880 32660 34195 5369 2249 4946 O
ATOM 346 CB MET A 44 29.764 72.410 56.327 1.00241.03 C
ANISOU 346 CB MET A 44 25785 31894 33902 4880 1711 5608 C
ATOM 347 CG MET A 44 31.255 72.750 56.265 1.00240.27 C
ANISOU 347 CG MET A 44 26122 31437 33731 4233 1832 5991 C
ATOM 348 SD MET A 44 32.387 71.355 56.028 1.00236.21 S
ANISOU 348 SD MET A 44 24931 31157 33662 3474 2600 6126 S
ATOM 349 CE MET A 44 32.189 70.460 57.585 1.00232.22 C
ANISOU 349 CE MET A 44 23584 30931 33717 3712 3009 6029 C
ATOM 350 N TRP A 45 26.823 71.672 54.603 1.00264.64 N
ANISOU 350 N TRP A 45 28195 35650 36706 5790 1405 4815 N
ATOM 351 CA TRP A 45 25.480 71.088 54.682 1.00264.94 C
ANISOU 351 CA TRP A 45 27640 36163 36863 6297 1415 4451 C
ATOM 352 C TRP A 45 25.483 69.680 54.056 1.00262.56 C
ANISOU 352 C TRP A 45 26615 36237 36908 5908 1960 4358 C
ATOM 353 O TRP A 45 26.028 69.519 52.956 1.00262.87 O
ANISOU 353 O TRP A 45 26859 36161 36858 5458 2064 4459 O
ATOM 354 CB TRP A 45 24.425 71.985 54.021 1.00269.26 C
ANISOU 354 CB TRP A 45 28689 36673 36944 6846 817 4231 C
ATOM 355 CG TRP A 45 23.005 71.606 54.315 1.00270.03 C
ANISOU 355 CG TRP A 45 28238 37261 37100 7464 740 3857 C
ATOM 356 CD1 TRP A 45 22.250 70.694 53.656 1.00269.82 C
ANISOU 356 CD1 TRP A 45 27649 37668 37203 7485 957 3613 C
ATOM 357 CD2 TRP A 45 22.152 72.085 55.401 1.00271.13 C
ANISOU 357 CD2 TRP A 45 28288 37557 37173 8150 439 3676 C
ATOM 358 NE1 TRP A 45 21.007 70.587 54.242 1.00270.79 N
ANISOU 358 NE1 TRP A 45 27365 38198 37325 8087 808 3291 N
ATOM 359 CE2 TRP A 45 20.889 71.431 55.309 1.00271.69 C
ANISOU 359 CE2 TRP A 45 27831 38111 37290 8404 470 3250 C
ATOM 360 CE3 TRP A 45 22.323 72.974 56.483 1.00271.69 C
ANISOU 360 CE3 TRP A 45 28722 37377 37131 8471 140 3775 C
ATOM 361 CZ2 TRP A 45 19.849 71.654 56.212 1.00272.89 C
ANISOU 361 CZ2 TRP A 45 28015 38340 37331 8627 193 2818 C
ATOM 362 CZ3 TRP A 45 21.273 73.219 57.385 1.00272.88 C
ANISOU 362 CZ3 TRP A 45 28798 37697 37188 8886 -131 3386 C
ATOM 363 CH2 TRP A 45 20.042 72.565 57.253 1.00273.52 C
ANISOU 363 CH2 TRP A 45 28487 38147 37292 8873 -102 2888 C
ATOM 364 N PRO A 46 24.893 68.659 54.698 1.00256.22 N
ANISOU 364 N PRO A 46 24993 35880 36480 6058 2297 4168 N
ATOM 365 CA PRO A 46 24.837 67.294 54.173 1.00254.06 C
ANISOU 365 CA PRO A 46 24347 35817 36366 5496 2678 3899 C
ATOM 366 C PRO A 46 24.264 67.253 52.750 1.00256.44 C
ANISOU 366 C PRO A 46 24532 36338 36567 5696 2623 3888 C
ATOM 367 O PRO A 46 23.194 67.794 52.484 1.00259.36 O
ANISOU 367 O PRO A 46 25030 36838 36676 6243 2232 3686 O
ATOM 368 CB PRO A 46 23.968 66.514 55.167 1.00252.48 C
ANISOU 368 CB PRO A 46 24061 35733 36135 5355 2615 3309 C
ATOM 369 CG PRO A 46 24.137 67.286 56.470 1.00252.27 C
ANISOU 369 CG PRO A 46 24240 35528 36083 5602 2429 3392 C
ATOM 370 CD PRO A 46 24.313 68.724 56.028 1.00255.56 C
ANISOU 370 CD PRO A 46 24931 35814 36357 6234 2126 3852 C
ATOM 371 N GLU A 47 24.998 66.684 51.802 1.00273.33 N
ANISOU 371 N GLU A 47 26613 38440 38800 5167 2932 4030 N
ATOM 372 CA GLU A 47 24.662 66.665 50.373 1.00275.43 C
ANISOU 372 CA GLU A 47 27083 38734 38834 5082 2812 3929 C
ATOM 373 C GLU A 47 23.360 65.932 50.064 1.00275.98 C
ANISOU 373 C GLU A 47 26598 39278 38983 5416 2851 3589 C
ATOM 374 O GLU A 47 22.695 66.272 49.091 1.00278.68 O
ANISOU 374 O GLU A 47 27197 39649 39039 5613 2565 3442 O
ATOM 375 CB GLU A 47 25.780 65.986 49.571 1.00273.64 C
ANISOU 375 CB GLU A 47 26803 38422 38747 4382 3216 4123 C
ATOM 376 CG GLU A 47 27.104 66.756 49.546 1.00273.74 C
ANISOU 376 CG GLU A 47 27439 37979 38589 3969 3151 4462 C
ATOM 377 CD GLU A 47 28.232 66.031 48.802 1.00271.98 C
ANISOU 377 CD GLU A 47 27099 37739 38503 3280 3575 4639 C
ATOM 378 OE1 GLU A 47 28.039 64.844 48.468 1.00270.23 O
ANISOU 378 OE1 GLU A 47 26264 37845 38566 3132 3957 4505 O
ATOM 379 OE2 GLU A 47 29.279 66.642 48.479 1.00272.60 O1-
ANISOU 379 OE2 GLU A 47 27706 37495 38376 2887 3509 4902 O1-
ATOM 380 N LEU A 48 23.014 64.926 50.868 1.00262.75 N
ANISOU 380 N LEU A 48 24847 37612 37375 5036 2937 3126 N
ATOM 381 CA LEU A 48 21.850 64.071 50.631 1.00262.97 C
ANISOU 381 CA LEU A 48 24708 37856 37352 4989 2868 2608 C
ATOM 382 C LEU A 48 20.573 64.597 51.283 1.00265.13 C
ANISOU 382 C LEU A 48 24991 38263 37484 5530 2495 2314 C
ATOM 383 O LEU A 48 19.513 64.010 51.083 1.00265.82 O
ANISOU 383 O LEU A 48 24924 38523 37554 5532 2420 1920 O
ATOM 384 CB LEU A 48 22.173 62.639 51.089 1.00259.31 C
ANISOU 384 CB LEU A 48 24204 37306 37018 4301 3110 2267 C
ATOM 385 CG LEU A 48 23.372 62.015 50.355 1.00257.37 C
ANISOU 385 CG LEU A 48 24009 36930 36848 3754 3425 2466 C
ATOM 386 CD1 LEU A 48 23.598 60.597 50.864 1.00253.99 C
ANISOU 386 CD1 LEU A 48 23631 36436 36438 3201 3541 2053 C
ATOM 387 CD2 LEU A 48 23.161 61.931 48.840 1.00259.20 C
ANISOU 387 CD2 LEU A 48 24120 37313 37050 3778 3494 2554 C
ATOM 388 N ASP A 49 20.665 65.663 52.077 1.00287.64 N
ANISOU 388 N ASP A 49 28040 41009 40240 5959 2257 2492 N
ATOM 389 CA ASP A 49 19.488 66.288 52.665 1.00290.10 C
ANISOU 389 CA ASP A 49 28429 41422 40372 6496 1856 2219 C
ATOM 390 C ASP A 49 18.635 67.011 51.607 1.00294.08 C
ANISOU 390 C ASP A 49 29029 42127 40580 7107 1519 2206 C
ATOM 391 O ASP A 49 19.135 67.427 50.559 1.00295.27 O
ANISOU 391 O ASP A 49 29283 42284 40623 7279 1512 2530 O
ATOM 392 CB ASP A 49 19.909 67.201 53.820 1.00290.06 C
ANISOU 392 CB ASP A 49 28682 41207 40321 6753 1673 2393 C
ATOM 393 CG ASP A 49 18.708 67.627 54.658 1.00292.03 C
ANISOU 393 CG ASP A 49 28992 41530 40435 7144 1310 2038 C
ATOM 394 OD1 ASP A 49 18.710 68.774 55.144 1.00293.95 O
ANISOU 394 OD1 ASP A 49 29564 41647 40477 7637 968 2172 O
ATOM 395 OD2 ASP A 49 17.752 66.826 54.779 1.00291.87 O1-
ANISOU 395 OD2 ASP A 49 28723 41667 40507 6952 1356 1648 O1-
ATOM 396 N ALA A 50 17.336 67.153 51.875 1.00258.69 N
ANISOU 396 N ALA A 50 24535 37802 35952 7426 1227 1835 N
ATOM 397 CA ALA A 50 16.389 67.702 50.909 1.00262.44 C
ANISOU 397 CA ALA A 50 25124 38489 36103 7962 886 1716 C
ATOM 398 C ALA A 50 16.766 69.147 50.517 1.00265.35 C
ANISOU 398 C ALA A 50 26011 38718 36090 8636 447 2005 C
ATOM 399 O ALA A 50 16.959 69.981 51.407 1.00265.97 O
ANISOU 399 O ALA A 50 26417 38585 36055 8910 187 2086 O
ATOM 400 CB ALA A 50 14.971 67.626 51.485 1.00264.21 C
ANISOU 400 CB ALA A 50 25266 38875 36248 8128 674 1305 C
ATOM 401 N PRO A 51 16.813 69.504 49.216 1.00257.60 N
ANISOU 401 N PRO A 51 25240 37769 34867 8885 283 2123 N
ATOM 402 CA PRO A 51 17.180 70.857 48.786 1.00260.54 C
ANISOU 402 CA PRO A 51 26601 37595 34797 9010 -245 2245 C
ATOM 403 C PRO A 51 16.283 71.947 49.394 1.00263.97 C
ANISOU 403 C PRO A 51 27390 38048 34860 9814 -845 2035 C
ATOM 404 O PRO A 51 16.747 73.040 49.713 1.00265.50 O
ANISOU 404 O PRO A 51 28306 37783 34788 9947 -1231 2189 O
ATOM 405 CB PRO A 51 17.081 70.832 47.257 1.00262.24 C
ANISOU 405 CB PRO A 51 27114 37718 34808 8798 -327 2200 C
ATOM 406 CG PRO A 51 17.291 69.367 46.894 1.00258.91 C
ANISOU 406 CG PRO A 51 25922 37630 34824 8274 310 2214 C
ATOM 407 CD PRO A 51 16.658 68.624 48.064 1.00257.07 C
ANISOU 407 CD PRO A 51 24870 37901 34904 8541 563 2050 C
ATOM 408 N THR A 52 15.008 71.639 49.630 1.00282.07 N
ANISOU 408 N THR A 52 29243 40804 37127 10206 -915 1659 N
ATOM 409 CA THR A 52 14.043 72.525 50.298 1.00285.28 C
ANISOU 409 CA THR A 52 30014 41166 37212 10657 -1399 1370 C
ATOM 410 C THR A 52 14.441 72.934 51.718 1.00284.12 C
ANISOU 410 C THR A 52 30000 40786 37169 10600 -1418 1466 C
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