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PDBsum entry 2pv2

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Top Page protein Protein-protein interface(s) links
Isomerase PDB id
2pv2
Jmol
Contents
Protein chains
103 a.a.
12 a.a.
Waters ×398
HEADER    ISOMERASE                               09-MAY-07   2PV2
TITLE     CRYSTALLOGRAPHIC STRUCTURE OF SURA FIRST PEPTIDYL-PROLYL
TITLE    2 ISOMERASE DOMAIN COMPLEXED WITH PEPTIDE NFTLKFWDIFRK
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: CHAPERONE SURA;
COMPND   3 CHAIN: A, B, C, D;
COMPND   4 FRAGMENT: PPIC 1;
COMPND   5 SYNONYM: PEPTIDYL-PROLYL CIS-TRANS ISOMERASE SURA, PPIASE
COMPND   6 SURA, ROTAMASE SURA, SURVIVAL PROTEIN A;
COMPND   7 EC: 5.2.1.8;
COMPND   8 ENGINEERED: YES;
COMPND   9 MOL_ID: 2;
COMPND  10 MOLECULE: C-PEPTIDE;
COMPND  11 CHAIN: E, F;
COMPND  12 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE   3 ORGANISM_TAXID: 562;
SOURCE   4 STRAIN: K-12 EMG2;
SOURCE   5 GENE: SURA;
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3);
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PTYB1;
SOURCE  11 MOL_ID: 2;
SOURCE  12 SYNTHETIC: YES
KEYWDS    SURVIVAL PROTEIN A, PEPTIDYL-PROLYL CIS-TRANS ISOMERASE
KEYWDS   2 DOMAIN, PEPTIDE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    X.XU,D.B.MCKAY
REVDAT   3   24-FEB-09 2PV2    1       VERSN
REVDAT   2   30-OCT-07 2PV2    1       JRNL
REVDAT   1   02-OCT-07 2PV2    0
JRNL        AUTH   X.XU,S.WANG,Y.X.HU,D.B.MCKAY
JRNL        TITL   THE PERIPLASMIC BACTERIAL MOLECULAR CHAPERONE SURA
JRNL        TITL 2 ADAPTS ITS STRUCTURE TO BIND PEPTIDES IN DIFFERENT
JRNL        TITL 3 CONFORMATIONS TO ASSERT A SEQUENCE PREFERENCE FOR
JRNL        TITL 4 AROMATIC RESIDUES.
JRNL        REF    J.MOL.BIOL.                   V. 373   367 2007
JRNL        REFN                   ISSN 0022-2836
JRNL        PMID   17825319
JRNL        DOI    10.1016/J.JMB.2007.07.069
REMARK   1
REMARK   1 REFERENCE 1
REMARK   1  AUTH   E.BITTO,D.B.MCKAY
REMARK   1  TITL   CRYSTALLOGRAPHIC STRUCTURE OF SURA, A MOLECULAR
REMARK   1  TITL 2 CHAPERONE THAT FACILITATES FOLDING OF OUTER
REMARK   1  TITL 3 MEMBRANE PORINS
REMARK   1  REF    STRUCTURE                     V.  10  1489 2002
REMARK   1  REFN                   ISSN 0969-2126
REMARK   1  PMID   12429090
REMARK   1  DOI    10.1016/S0969-2126(02)00877-8
REMARK   2
REMARK   2 RESOLUTION.    1.30 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : CNS 1.1
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,
REMARK   3               : READ,RICE,SIMONSON,WARREN
REMARK   3
REMARK   3  REFINEMENT TARGET : NULL
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.30
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 28.20
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 94.4
REMARK   3   NUMBER OF REFLECTIONS             : 90278
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM
REMARK   3   R VALUE            (WORKING SET) : 0.208
REMARK   3   FREE R VALUE                     : 0.227
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 9.500
REMARK   3   FREE R VALUE TEST SET COUNT      : 9046
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.30
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.38
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 89.20
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2560
REMARK   3   BIN FREE R VALUE                    : 0.2810
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 1357
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.008
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 3324
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 0
REMARK   3   SOLVENT ATOMS            : 398
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 17.97
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 1.96600
REMARK   3    B22 (A**2) : -5.33500
REMARK   3    B33 (A**2) : 3.36900
REMARK   3    B12 (A**2) : 0.00000
REMARK   3    B13 (A**2) : 2.72300
REMARK   3    B23 (A**2) : 0.00000
REMARK   3
REMARK   3  ESTIMATED COORDINATE ERROR.
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.16
REMARK   3   ESD FROM SIGMAA              (A) : 0.11
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00
REMARK   3
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.17
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.13
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.
REMARK   3   BOND LENGTHS                 (A) : 0.006
REMARK   3   BOND ANGLES            (DEGREES) : NULL
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 23.40
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.86
REMARK   3
REMARK   3  ISOTROPIC THERMAL MODEL : NULL
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL
REMARK   3
REMARK   3  BULK SOLVENT MODELING.
REMARK   3   METHOD USED : NULL
REMARK   3   KSOL        : NULL
REMARK   3   BSOL        : 48.34
REMARK   3
REMARK   3  NCS MODEL : NULL
REMARK   3
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL
REMARK   3
REMARK   3  PARAMETER FILE  1  : CNS_TOPPAR:PROTEIN_REP.PARAM
REMARK   3  PARAMETER FILE  2  : CNS_TOPPAR:WATER_REP.PARAM
REMARK   3  PARAMETER FILE  3  : NULL
REMARK   3  TOPOLOGY FILE  1   : NULL
REMARK   3  TOPOLOGY FILE  2   : NULL
REMARK   3  TOPOLOGY FILE  3   : NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: NULL
REMARK   4
REMARK   4 2PV2 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-MAY-07.
REMARK 100 THE RCSB ID CODE IS RCSB042804.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 20-DEC-06
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 8.0
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : SSRL
REMARK 200  BEAMLINE                       : BL11-1
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 325 MM CCD
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200  DATA SCALING SOFTWARE          : HKL
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 93257
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.300
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.2
REMARK 200  DATA REDUNDANCY                : 2.500
REMARK 200  R MERGE                    (I) : NULL
REMARK 200  R SYM                      (I) : 0.04500
REMARK 200   FOR THE DATA SET  : 26.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.30
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.35
REMARK 200  COMPLETENESS FOR SHELL     (%) : 90.2
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.20
REMARK 200  R MERGE FOR SHELL          (I) : NULL
REMARK 200  R SYM FOR SHELL            (I) : 0.25000
REMARK 200   FOR SHELL         : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 1M5Y
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 41.08
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.09
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 24% PLOYETHYLENE GLYCOL 8000, 0.1 M
REMARK 280  IMDIDAZOLE, PH 8.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE
REMARK 280  298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,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       25.31500
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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 APPLY THE FOLLOWING TO CHAINS: A, B, E
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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D, F
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 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    ASN B 227       36.65    -99.22
REMARK 500    ASN D 186       78.60   -118.09
REMARK 500
REMARK 500 REMARK: NULL
DBREF  2PV2 A  172   274  UNP    P0ABZ6   SURA_ECOLI     172    274
DBREF  2PV2 B  172   274  UNP    P0ABZ6   SURA_ECOLI     172    274
DBREF  2PV2 C  172   274  UNP    P0ABZ6   SURA_ECOLI     172    274
DBREF  2PV2 D  172   274  UNP    P0ABZ6   SURA_ECOLI     172    274
DBREF  2PV2 E    1    12  PDB    2PV2     2PV2             1     12
DBREF  2PV2 F    1    12  PDB    2PV2     2PV2             1     12
SEQRES   1 A  103  THR GLU LEU ASN LEU SER HIS ILE LEU ILE PRO LEU PRO
SEQRES   2 A  103  GLU ASN PRO THR SER ASP GLN VAL ASN GLU ALA GLU SER
SEQRES   3 A  103  GLN ALA ARG ALA ILE VAL ASP GLN ALA ARG ASN GLY ALA
SEQRES   4 A  103  ASP PHE GLY LYS LEU ALA ILE ALA HIS SER ALA ASP GLN
SEQRES   5 A  103  GLN ALA LEU ASN GLY GLY GLN MET GLY TRP GLY ARG ILE
SEQRES   6 A  103  GLN GLU LEU PRO GLY ILE PHE ALA GLN ALA LEU SER THR
SEQRES   7 A  103  ALA LYS LYS GLY ASP ILE VAL GLY PRO ILE ARG SER GLY
SEQRES   8 A  103  VAL GLY PHE HIS ILE LEU LYS VAL ASN ASP LEU ARG
SEQRES   1 B  103  THR GLU LEU ASN LEU SER HIS ILE LEU ILE PRO LEU PRO
SEQRES   2 B  103  GLU ASN PRO THR SER ASP GLN VAL ASN GLU ALA GLU SER
SEQRES   3 B  103  GLN ALA ARG ALA ILE VAL ASP GLN ALA ARG ASN GLY ALA
SEQRES   4 B  103  ASP PHE GLY LYS LEU ALA ILE ALA HIS SER ALA ASP GLN
SEQRES   5 B  103  GLN ALA LEU ASN GLY GLY GLN MET GLY TRP GLY ARG ILE
SEQRES   6 B  103  GLN GLU LEU PRO GLY ILE PHE ALA GLN ALA LEU SER THR
SEQRES   7 B  103  ALA LYS LYS GLY ASP ILE VAL GLY PRO ILE ARG SER GLY
SEQRES   8 B  103  VAL GLY PHE HIS ILE LEU LYS VAL ASN ASP LEU ARG
SEQRES   1 C  103  THR GLU LEU ASN LEU SER HIS ILE LEU ILE PRO LEU PRO
SEQRES   2 C  103  GLU ASN PRO THR SER ASP GLN VAL ASN GLU ALA GLU SER
SEQRES   3 C  103  GLN ALA ARG ALA ILE VAL ASP GLN ALA ARG ASN GLY ALA
SEQRES   4 C  103  ASP PHE GLY LYS LEU ALA ILE ALA HIS SER ALA ASP GLN
SEQRES   5 C  103  GLN ALA LEU ASN GLY GLY GLN MET GLY TRP GLY ARG ILE
SEQRES   6 C  103  GLN GLU LEU PRO GLY ILE PHE ALA GLN ALA LEU SER THR
SEQRES   7 C  103  ALA LYS LYS GLY ASP ILE VAL GLY PRO ILE ARG SER GLY
SEQRES   8 C  103  VAL GLY PHE HIS ILE LEU LYS VAL ASN ASP LEU ARG
SEQRES   1 D  103  THR GLU LEU ASN LEU SER HIS ILE LEU ILE PRO LEU PRO
SEQRES   2 D  103  GLU ASN PRO THR SER ASP GLN VAL ASN GLU ALA GLU SER
SEQRES   3 D  103  GLN ALA ARG ALA ILE VAL ASP GLN ALA ARG ASN GLY ALA
SEQRES   4 D  103  ASP PHE GLY LYS LEU ALA ILE ALA HIS SER ALA ASP GLN
SEQRES   5 D  103  GLN ALA LEU ASN GLY GLY GLN MET GLY TRP GLY ARG ILE
SEQRES   6 D  103  GLN GLU LEU PRO GLY ILE PHE ALA GLN ALA LEU SER THR
SEQRES   7 D  103  ALA LYS LYS GLY ASP ILE VAL GLY PRO ILE ARG SER GLY
SEQRES   8 D  103  VAL GLY PHE HIS ILE LEU LYS VAL ASN ASP LEU ARG
SEQRES   1 E   12  ASN PHE THR LEU LYS PHE TRP ASP ILE PHE ARG LYS
SEQRES   1 F   12  ASN PHE THR LEU LYS PHE TRP ASP ILE PHE ARG LYS
FORMUL   7  HOH   *398(H2 O)
HELIX    1   1 THR A  188  ASN A  208  1                                  21
HELIX    2   2 ASP A  211  SER A  220  1                                  10
HELIX    3   3 GLN A  224  GLY A  228  5                                   5
HELIX    4   4 GLN A  237  LEU A  239  5                                   3
HELIX    5   5 PRO A  240  THR A  249  1                                  10
HELIX    6   6 THR B  188  ASN B  208  1                                  21
HELIX    7   7 ASP B  211  SER B  220  1                                  10
HELIX    8   8 GLN B  224  GLY B  228  5                                   5
HELIX    9   9 GLN B  237  LEU B  239  5                                   3
HELIX   10  10 PRO B  240  LEU B  247  1                                   8
HELIX   11  11 THR C  188  ASN C  208  1                                  21
HELIX   12  12 ASP C  211  SER C  220  1                                  10
HELIX   13  13 GLN C  224  GLY C  228  5                                   5
HELIX   14  14 GLN C  237  LEU C  239  5                                   3
HELIX   15  15 PRO C  240  SER C  248  1                                   9
HELIX   16  16 THR D  188  ASN D  208  1                                  21
HELIX   17  17 ASP D  211  SER D  220  1                                  10
HELIX   18  18 GLN D  224  GLY D  228  5                                   5
HELIX   19  19 GLN D  237  LEU D  239  5                                   3
HELIX   20  20 PRO D  240  LEU D  247  1                                   8
HELIX   21  21 PHE E    2  ARG E   11  1                                  10
HELIX   22  22 PHE F    2  ARG F   11  1                                  10
SHEET    1   A 4 GLN A 230  ARG A 235  0
SHEET    2   A 4 GLU A 173  PRO A 182 -1  N  LEU A 176   O  MET A 231
SHEET    3   A 4 GLY A 264  ARG A 274 -1  O  PHE A 265   N  ILE A 181
SHEET    4   A 4 ILE A 255  SER A 261 -1  N  VAL A 256   O  LEU A 268
SHEET    1   B 4 GLN B 230  ARG B 235  0
SHEET    2   B 4 GLU B 173  PRO B 182 -1  N  LEU B 176   O  MET B 231
SHEET    3   B 4 GLY B 264  LEU B 273 -1  O  PHE B 265   N  ILE B 181
SHEET    4   B 4 ILE B 255  SER B 261 -1  N  VAL B 256   O  LEU B 268
SHEET    1   C 4 GLN C 230  ARG C 235  0
SHEET    2   C 4 GLU C 173  PRO C 182 -1  N  LEU C 176   O  MET C 231
SHEET    3   C 4 GLY C 264  LEU C 273 -1  O  PHE C 265   N  ILE C 181
SHEET    4   C 4 ILE C 255  SER C 261 -1  N  VAL C 256   O  LEU C 268
SHEET    1   D 4 GLN D 230  ARG D 235  0
SHEET    2   D 4 GLU D 173  PRO D 182 -1  N  LEU D 176   O  MET D 231
SHEET    3   D 4 GLY D 264  ARG D 274 -1  O  PHE D 265   N  ILE D 181
SHEET    4   D 4 ILE D 255  SER D 261 -1  N  VAL D 256   O  LEU D 268
CISPEP   1 GLY A  257    PRO A  258          0         0.05
CISPEP   2 GLY B  257    PRO B  258          0         0.09
CISPEP   3 GLY C  257    PRO C  258          0         0.10
CISPEP   4 GLY D  257    PRO D  258          0        -0.08
CRYST1   56.460   50.630   74.060  90.00 111.54  90.00 P 1 21 1      8
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      0.017712  0.000000  0.006991        0.00000
SCALE2      0.000000  0.019751  0.000000        0.00000
SCALE3      0.000000  0.000000  0.014516        0.00000
      
PROCHECK
Go to PROCHECK summary
 References