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PDBsum entry 2wlw

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Isomerase PDB id
2wlw
Jmol
Contents
Protein chain
164 a.a.
Waters ×207
HEADER    ISOMERASE                               26-JUN-09   2WLW
TITLE     STRUCTURE OF THE N-TERMINAL CAPSID DOMAIN OF HIV-2
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: PEPTIDYL-PROLYL CIS-TRANS ISOMERASE;
COMPND   3 CHAIN: A;
COMPND   4 FRAGMENT: CYPA DOMAIN, RESIDUES 46-210;
COMPND   5 SYNONYM: TRIM-CYP;
COMPND   6 EC: 5.2.1.8;
COMPND   7 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: MACACA MULATTA;
SOURCE   3 ORGANISM_TAXID: 9544;
SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS    ROTAMASE, ISOMERASE, RHESUS MACAQUE TRIM-CYP
EXPDTA    X-RAY DIFFRACTION
AUTHOR    A.J.PRICE,F.MARZETTA,M.LAMMERS,L.M.J.YLINEN,T.SCHALLER,
AUTHOR   2 S.J.WILSON,G.J.TOWERS,L.C.JAMES
REVDAT   3   06-JUL-11 2WLW    1       JRNL   REMARK
REVDAT   2   29-SEP-09 2WLW    1       JRNL
REVDAT   1   22-SEP-09 2WLW    0
JRNL        AUTH   A.J.PRICE,F.MARZETTA,M.LAMMERS,L.M.J.YLINEN,
JRNL        AUTH 2 T.SCHALLER,S.J.WILSON,G.J.TOWERS,L.C.JAMES
JRNL        TITL   ACTIVE SITE REMODELLING SWITCHES HIV SPECIFICITY
JRNL        TITL 2 OF ANTIRETROVIRAL TRIMCYP
JRNL        REF    NAT.STRUCT.MOL.BIOL.          V.  16  1036 2009
JRNL        REFN                   ISSN 1545-9993
JRNL        PMID   19767750
JRNL        DOI    10.1038/NSMB.1667
REMARK   2
REMARK   2 RESOLUTION.     1.50 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.5.0088
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON
REMARK   3
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.5
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 88.570
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 2
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.791
REMARK   3   NUMBER OF REFLECTIONS             : 23059
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.156
REMARK   3   R VALUE            (WORKING SET) : 0.1540
REMARK   3   FREE R VALUE                     : 0.1858
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.03
REMARK   3   FREE R VALUE TEST SET COUNT      : 5669
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED           : 20
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.50
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.64
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 7816
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.47
REMARK   3   BIN R VALUE           (WORKING SET) : 0.244
REMARK   3   BIN FREE R VALUE SET COUNT          : 435
REMARK   3   BIN FREE R VALUE                    : 0.286
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 1319
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 0
REMARK   3   SOLVENT ATOMS            : 207
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 16.659
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 0.329
REMARK   3    B22 (A**2) : -0.585
REMARK   3    B33 (A**2) : 0.256
REMARK   3    B12 (A**2) : 0.000
REMARK   3    B13 (A**2) : 0.000
REMARK   3    B23 (A**2) : 0.000
REMARK   3
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.
REMARK   3   ESU BASED ON R VALUE                            (A): 0.039
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.040
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.026
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.322
REMARK   3
REMARK   3  CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.973
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.965
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2520 ; 0.031 ; 0.022
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3458 ; 2.438 ; 1.943
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   322 ; 6.584 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   128 ;31.658 ;24.219
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   419 ;14.740 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    22 ;21.092 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   362 ; 0.159 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2906 ; 0.014 ; 0.021
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  7930 ; 0.348 ; 0.200
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  1168 ; 0.243 ; 0.200
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):   308 ; 0.359 ; 0.200
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    51 ; 0.267 ; 0.200
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  8182 ; 1.948 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 12714 ; 2.820 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  4478 ; 5.016 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  3872 ; 6.904 ; 4.500
REMARK   3
REMARK   3  ANISOTROPIC THERMAL FACTOR RESTRAINTS.   COUNT   RMS    WEIGHT
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL
REMARK   3
REMARK   3  NCS RESTRAINTS STATISTICS
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK   3
REMARK   3  TLS DETAILS
REMARK   3   NUMBER OF TLS GROUPS  : NULL
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED : BABINET MODEL PLUS MASK
REMARK   3   PARAMETERS FOR MASK CALCULATION
REMARK   3   VDW PROBE RADIUS   : 1.400
REMARK   3   ION PROBE RADIUS   : 0.800
REMARK   3   SHRINKAGE RADIUS   : NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE
REMARK   3   RIDING POSITIONS.
REMARK   4
REMARK   4 2WLW COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 26-JUN-09.
REMARK 100 THE PDBE ID CODE IS EBI-40256.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : NULL
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : NULL
REMARK 200  NUMBER OF CRYSTALS USED        : NULL
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : N
REMARK 200  RADIATION SOURCE               : ROTATING ANODE
REMARK 200  BEAMLINE                       : NULL
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : NULL
REMARK 200  DETECTOR MANUFACTURER          : NULL
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200  DATA SCALING SOFTWARE          : NULL
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 23059
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.50
REMARK 200  RESOLUTION RANGE LOW       (A) : 41.00
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.0
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.5
REMARK 200  DATA REDUNDANCY                : 3.6
REMARK 200  R MERGE                    (I) : 0.07
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 11.20
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL
REMARK 200  R MERGE FOR SHELL          (I) : NULL
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: OTHER
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NONE
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 23.18
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.61
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X+1/2,-Y,Z+1/2
REMARK 290       3555   -X,Y+1/2,-Z+1/2
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       17.94000
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       37.59000
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       25.56000
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       37.59000
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       17.94000
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       25.56000
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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
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     1
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   O    HOH A  2112     O    HOH A  2121              1.12
REMARK 500   CE   MET A    61     O    HOH A  2090              1.89
REMARK 500   O    HOH A  2084     O    HOH A  2193              1.99
REMARK 500   O    HOH A  2036     O    HOH A  2083              2.00
REMARK 500   O    HOH A  2174     O    HOH A  2175              2.15
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION
REMARK 500    PHE A   7   CG    PHE A   7   CD1     0.095
REMARK 500    GLU A  43   CD    GLU A  43   OE2    -0.070
REMARK 500    MET A  61   SD    MET A  61   CE     -0.408
REMARK 500    GLU A  84   CD    GLU A  84   OE1     0.067
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3
REMARK 500    MET A  61   CG  -  SD  -  CE  ANGL. DEV. = -18.6 DEGREES
REMARK 500    ARG A 144   NE  -  CZ  -  NH1 ANGL. DEV. =   4.0 DEGREES
REMARK 500    ARG A 144   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.2 DEGREES
REMARK 500    ARG A 148   NE  -  CZ  -  NH1 ANGL. DEV. =   3.6 DEGREES
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    PHE A  60      -72.83   -127.04
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2WLV   RELATED DB: PDB
REMARK 900  STRUCTURE OF THE N-TERMINAL CAPSID DOMAIN OF HIV-2
DBREF  2WLW A    1   165  UNP    B1P761   B1P761_MACMU    46    210
SEQRES   1 A  165  MET VAL ASN PRO THR VAL PHE PHE ASP ILE ALA VAL ASP
SEQRES   2 A  165  GLY GLU PRO LEU GLY ARG VAL SER PHE GLU LEU PHE ALA
SEQRES   3 A  165  ASP LYS VAL PRO LYS THR ALA GLU ASN PHE ARG ALA LEU
SEQRES   4 A  165  SER THR GLY GLU LYS GLY PHE GLY TYR LYS GLY SER CYS
SEQRES   5 A  165  PHE HIS ARG ILE ILE PRO GLY PHE MET CYS GLN GLY GLY
SEQRES   6 A  165  ASN PHE THR HIS HIS ASN GLY THR GLY GLY LYS SER ILE
SEQRES   7 A  165  TYR GLY GLU LYS PHE GLU ASP GLU ASN PHE ILE LEU LYS
SEQRES   8 A  165  HIS THR GLY PRO GLY ILE LEU SER MET ALA ASN ALA GLY
SEQRES   9 A  165  PRO ASN THR ASN GLY SER GLN PHE PHE ILE CYS THR ALA
SEQRES  10 A  165  LYS THR GLU TRP LEU ASP GLY LYS HIS VAL VAL PHE GLY
SEQRES  11 A  165  LYS VAL LYS GLU GLY MET ASN ILE VAL GLU ALA MET GLU
SEQRES  12 A  165  ARG PHE GLY SER ARG ASN GLY LYS THR SER LYS LYS ILE
SEQRES  13 A  165  THR ILE ALA ASP CYS GLY GLN LEU GLU
FORMUL   2  HOH   *207(H2 O)
HELIX    1   1 VAL A   29  GLY A   42  1                                  14
HELIX    2   2 THR A  119  ASP A  123  5                                   5
HELIX    3   3 GLY A  135  ARG A  144  1                                  10
SHEET    1  AA 8 PHE A  53  ILE A  57  0
SHEET    2  AA 8 MET A  61  GLY A  64 -1  O  MET A  61   N  ILE A  57
SHEET    3  AA 8 PHE A 112  CYS A 115 -1  O  PHE A 112   N  GLY A  64
SHEET    4  AA 8 ILE A  97  MET A 100 -1  O  ILE A  97   N  CYS A 115
SHEET    5  AA 8 VAL A 128  GLU A 134 -1  N  PHE A 129   O  LEU A  98
SHEET    6  AA 8 GLU A  15  LEU A  24 -1  O  SER A  21   N  LYS A 133
SHEET    7  AA 8 THR A   5  VAL A  12 -1  O  VAL A   6   N  PHE A  22
SHEET    8  AA 8 ILE A 156  GLU A 165 -1  O  THR A 157   N  ALA A  11
CRYST1   35.880   51.120   75.180  90.00  90.00  90.00 P 21 21 21    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      0.027871  0.000000  0.000000        0.00000
SCALE2      0.000000  0.019562  0.000000        0.00000
SCALE3      0.000000  0.000000  0.013301        0.00000
      
PROCHECK
Go to PROCHECK summary
 References