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PDBsum entry 3bt8

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Isomerase PDB id
3bt8
Jmol
Contents
Protein chain
166 a.a.
Waters ×38
HEADER    ISOMERASE                               28-DEC-07   3BT8
TITLE     CRYSTAL STRUCTURE OF MUTANT CYCLOPHILIN (R147A) FROM
TITLE    2 LEISHMANIA DONOVANI
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: PEPTIDYL-PROLYL CIS-TRANS ISOMERASE;
COMPND   3 CHAIN: A;
COMPND   4 FRAGMENT: UNP RESIDUES 22-187;
COMPND   5 SYNONYM: CYCLOPHILIN;
COMPND   6 EC: 5.2.1.8;
COMPND   7 ENGINEERED: YES;
COMPND   8 MUTATION: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: LEISHMANIA DONOVANI;
SOURCE   3 ORGANISM_TAXID: 5661;
SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE   6 EXPRESSION_SYSTEM_STRAIN: M15;
SOURCE   7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PQE32
KEYWDS    CYCLOPHILIN, ROTAMASE, PROLINE, ISOMERASE, CIS-TRANS,
KEYWDS   2 PROTOZOA, LEISHMANIA, DONOVANI, KALA-AZAR
EXPDTA    X-RAY DIFFRACTION
AUTHOR    V.VENUGOPAL,B.SEN,A.K.DATTA,R.BANERJEE
REVDAT   2   24-FEB-09 3BT8    1       VERSN
REVDAT   1   15-JAN-08 3BT8    0
JRNL        AUTH   V.VENUGOPAL,B.SEN,A.K.DATTA,R.BANERJEE
JRNL        TITL   CRYSTAL STRUCTURE OF MUTANT CYCLOPHILIN FROM
JRNL        TITL 2 LEISHMANIA DONOVANI
JRNL        REF    TO BE PUBLISHED
JRNL        REFN
REMARK   1
REMARK   1 REFERENCE 1
REMARK   1  AUTH   V.VENUGOPAL,B.SEN,A.K.DATTA,R.BANERJEE
REMARK   1  TITL   STRUCTURE OF CYCLOPHILIN FROM LEISHMANIA DONOVANI
REMARK   1  TITL 2 AT 1.97 A RESOLUTION
REMARK   1  REF    ACTA CRYSTALLOGR.,SECT.F      V.  63    60 2007
REMARK   1  REFN                   ESSN 1744-3091
REMARK   1  PMID   17277440
REMARK   1  DOI    10.1107/S1744309106056351
REMARK   1 REFERENCE 2
REMARK   1  AUTH   B.SEN,V.VENUGOPAL,A.CHAKRABORTY,R.DATTA,S.DOLAI,
REMARK   1  AUTH 2 R.BANERJEE,A.K.DATTA
REMARK   1  TITL   AMINO ACID RESIDUES OF LEISHMANIA DONOVANI
REMARK   1  TITL 2 CYCLOPHILIN KEY TO INTERACTION WITH ITS ADENOSINE
REMARK   1  TITL 3 KINASE: BIOLOGICAL IMPLICATIONS
REMARK   1  REF    BIOCHEMISTRY                  V.  46  7832 2007
REMARK   1  REFN                   ISSN 0006-2960
REMARK   1  PMID   17552497
REMARK   1  DOI    10.1021/BI602625H
REMARK   2
REMARK   2 RESOLUTION.    2.70 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) : 2.70
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 17.30
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 2.000
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 98.7
REMARK   3   NUMBER OF REFLECTIONS             : 5369
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) : 0.158
REMARK   3   FREE R VALUE                     : 0.226
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 6.400
REMARK   3   FREE R VALUE TEST SET COUNT      : 341
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.012
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED           : 6
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.70
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.87
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 98.30
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 831
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2000
REMARK   3   BIN FREE R VALUE                    : 0.2110
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 5.40
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 47
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.031
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 1269
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 0
REMARK   3   SOLVENT ATOMS            : 38
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : 4.70
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 29.30
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : -0.09000
REMARK   3    B22 (A**2) : -0.09000
REMARK   3    B33 (A**2) : 0.18000
REMARK   3    B12 (A**2) : 5.69000
REMARK   3    B13 (A**2) : 0.00000
REMARK   3    B23 (A**2) : 0.00000
REMARK   3
REMARK   3  ESTIMATED COORDINATE ERROR.
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.23
REMARK   3   ESD FROM SIGMAA              (A) : 0.24
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) : 0.35
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.35
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.
REMARK   3   BOND LENGTHS                 (A) : 0.008
REMARK   3   BOND ANGLES            (DEGREES) : 1.30
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 25.20
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.84
REMARK   3
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED
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        : NULL
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  : PROTEIN_REP.PARAM
REMARK   3  PARAMETER FILE  2  : WATER_REP.PARAM
REMARK   3  PARAMETER FILE  3  : NULL
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP
REMARK   3  TOPOLOGY FILE  2   : WATER.TOP
REMARK   3  TOPOLOGY FILE  3   : NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: NULL
REMARK   4
REMARK   4 3BT8 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 04-JAN-08.
REMARK 100 THE RCSB ID CODE IS RCSB045939.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 01-SEP-07
REMARK 200  TEMPERATURE           (KELVIN) : 293
REMARK 200  PH                             : 8.5
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : N
REMARK 200  RADIATION SOURCE               : ROTATING ANODE
REMARK 200  BEAMLINE                       : NULL
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU RU200
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : OSMIC MAXFLUX CONFOCAL
REMARK 200                                   MULTILAYER MIRRORS
REMARK 200
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : AUTOMAR
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 5450
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.700
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.5
REMARK 200  DATA REDUNDANCY                : 6.150
REMARK 200  R MERGE                    (I) : 0.05000
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 11.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.75
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.3
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.17
REMARK 200  R MERGE FOR SHELL          (I) : 0.15200
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : 4.200
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: PDB ENTRY 2HAQ
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 53.02
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.62
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.01M TRIS, 10.0% PEG 3350, 0.02%
REMARK 280  AZIDE, PH 8.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 292K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 65
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -Y,X-Y,Z+2/3
REMARK 290       3555   -X+Y,-X,Z+1/3
REMARK 290       4555   -X,-Y,Z+1/2
REMARK 290       5555   Y,-X+Y,Z+1/6
REMARK 290       6555   X-Y,X,Z+5/6
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 -0.500000 -0.866025  0.000000        0.00000
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       40.88200
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       20.44100
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       30.66150
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       10.22050
REMARK 290   SMTRY1   6  0.500000 -0.866025  0.000000        0.00000
REMARK 290   SMTRY2   6  0.866025  0.500000  0.000000        0.00000
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       51.10250
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     HIS A    16
REMARK 465     HIS A    17
REMARK 465     HIS A    18
REMARK 465     HIS A    19
REMARK 465     HIS A    20
REMARK 465     HIS A    21
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     GLU A  22    CG   CD   OE1  OE2
REMARK 470     GLN A  81    CG   CD   OE1  NE2
REMARK 470     ASN A 170    CG   OD1  ND2
REMARK 470     SER A 171    OG
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    PRO A  23      170.10    -57.40
REMARK 500    ASP A  36      105.55     77.50
REMARK 500    SER A  37        8.77     56.23
REMARK 500    ALA A  52       72.60   -151.03
REMARK 500    GLU A  66       10.99    -66.78
REMARK 500    GLN A  81      108.54    -40.02
REMARK 500    ASN A  82       20.69     83.08
REMARK 500    PHE A  83      -63.01   -133.06
REMARK 500    PHE A  93       18.75     53.20
REMARK 500    ASN A 170     -135.07    -89.40
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2HAQ   RELATED DB: PDB
REMARK 900 THE CRYSTAL STRUCTURE OF WILD TYPE CYCLOPHILIN FROM
REMARK 900 LEISHMANIA DONOVANI
DBREF  3BT8 A   22   187  UNP    Q9U9R3   Q9U9R3_LEIDO    22    187
SEQADV 3BT8 HIS A   16  UNP  Q9U9R3              EXPRESSION TAG
SEQADV 3BT8 HIS A   17  UNP  Q9U9R3              EXPRESSION TAG
SEQADV 3BT8 HIS A   18  UNP  Q9U9R3              EXPRESSION TAG
SEQADV 3BT8 HIS A   19  UNP  Q9U9R3              EXPRESSION TAG
SEQADV 3BT8 HIS A   20  UNP  Q9U9R3              EXPRESSION TAG
SEQADV 3BT8 HIS A   21  UNP  Q9U9R3              EXPRESSION TAG
SEQADV 3BT8 ALA A  147  UNP  Q9U9R3    ARG   147 ENGINEERED
SEQRES   1 A  172  HIS HIS HIS HIS HIS HIS GLU PRO GLU VAL THR ALA LYS
SEQRES   2 A  172  VAL TYR PHE ASP VAL MET ILE ASP SER GLU PRO LEU GLY
SEQRES   3 A  172  ARG ILE THR ILE GLY LEU PHE GLY LYS ASP ALA PRO LEU
SEQRES   4 A  172  THR THR GLU ASN PHE ARG GLN LEU CYS THR GLY GLU HIS
SEQRES   5 A  172  GLY PHE GLY TYR LYS ASP SER ILE PHE HIS ARG VAL ILE
SEQRES   6 A  172  GLN ASN PHE MET ILE GLN GLY GLY ASP PHE THR ASN PHE
SEQRES   7 A  172  ASP GLY THR GLY GLY LYS SER ILE TYR GLY GLU LYS PHE
SEQRES   8 A  172  ALA ASP GLU ASN LEU ASN VAL LYS HIS PHE VAL GLY ALA
SEQRES   9 A  172  LEU SER MET ALA ASN ALA GLY PRO ASN THR ASN GLY SER
SEQRES  10 A  172  GLN PHE PHE ILE THR THR ALA PRO THR PRO TRP LEU ASP
SEQRES  11 A  172  GLY ALA HIS VAL VAL PHE GLY LYS VAL LEU ASP GLY MET
SEQRES  12 A  172  ASP VAL VAL LEU ARG ILE GLU LYS THR LYS THR ASN SER
SEQRES  13 A  172  HIS ASP ARG PRO VAL LYS PRO VAL LYS ILE VAL ALA SER
SEQRES  14 A  172  GLY GLU LEU
FORMUL   2  HOH   *38(H2 O)
HELIX    1   1 ALA A   52  GLY A   65  1                                  14
HELIX    2   2 THR A  141  ASP A  145  5                                   5
HELIX    3   3 GLY A  157  GLU A  165  1                                   9
HELIX    4   4 ASN A  170  ARG A  174  5                                   5
SHEET    1   A 8 ARG A  78  ILE A  80  0
SHEET    2   A 8 MET A  84  GLY A  87 -1  O  GLN A  86   N  ARG A  78
SHEET    3   A 8 PHE A 134  THR A 137 -1  O  ILE A 136   N  ILE A  85
SHEET    4   A 8 ALA A 119  MET A 122 -1  N  SER A 121   O  PHE A 135
SHEET    5   A 8 VAL A 150  ASP A 156 -1  O  PHE A 151   N  LEU A 120
SHEET    6   A 8 GLY A  41  LEU A  47 -1  N  GLY A  46   O  LYS A 153
SHEET    7   A 8 VAL A  29  MET A  34 -1  N  VAL A  29   O  ILE A  45
SHEET    8   A 8 LYS A 180  GLU A 186 -1  O  ALA A 183   N  ASP A  32
CRYST1   74.973   74.973   61.323  90.00  90.00 120.00 P 65          6
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      0.013338  0.007701  0.000000        0.00000
SCALE2      0.000000  0.015402  0.000000        0.00000
SCALE3      0.000000  0.000000  0.016307        0.00000
      
PROCHECK
Go to PROCHECK summary
 References