spacer
spacer

PDBsum entry 1ist

Go to PDB code: 
Top Page protein Protein-protein interface(s) links
Isomerase PDB id
1ist
Jmol
Contents
Protein chains
161 a.a. *
Waters ×126
* Residue conservation analysis
HEADER    ISOMERASE                               25-DEC-01   1IST
TITLE     CRYSTAL STRUCTURE OF YEAST CYCLOPHILIN A, CPR1
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: CYCLOPHILIN A;
COMPND   3 CHAIN: A, B;
COMPND   4 SYNONYM: PEPTIDYL-PROLYL CIS-TRANS ISOMERASE;
COMPND   5 EC: 5.2.1.8
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE   3 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE   4 ORGANISM_TAXID: 4932;
SOURCE   5 STRAIN: AH22
KEYWDS    BARREL, CYCLOSPORIN, ISOMERASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    M.KONNO,A.KASHIMA,S.YOSHIKAWA-FUJIOKA
REVDAT   2   24-FEB-09 1IST    1       VERSN
REVDAT   1   18-NOV-03 1IST    0
JRNL        AUTH   A.KASHIMA,S.YOSHIKAWA-FUJIOKA,T.HAYANO,N.TAKAHASHI,
JRNL        AUTH 2 M.KONNO
JRNL        TITL   TURNS ARE ESSENTIAL IN THE FOLDING OF THE GLOBULAR
JRNL        TITL 2 BETA-BARREL STRUCTURE OF YEAST CYCLOPHILIN A, CPR1
JRNL        REF    TO BE PUBLISHED
JRNL        REFN
REMARK   1
REMARK   2
REMARK   2 RESOLUTION.    1.90 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : X-PLOR
REMARK   3   AUTHORS     : BRUNGER
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 10.00
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)   (%) : NULL
REMARK   3   NUMBER OF REFLECTIONS             : 18779
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   CROSS-VALIDATION METHOD          : NULL
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDAM
REMARK   3   R VALUE            (WORKING SET) : 0.199
REMARK   3   FREE R VALUE                     : 0.216
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.000
REMARK   3   FREE R VALUE TEST SET COUNT      : 1851
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           : 8
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.90
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.99
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 60.00
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 1485
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2751
REMARK   3   BIN FREE R VALUE                    : 0.2812
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 10.00
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 161
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 2440
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 0
REMARK   3   SOLVENT ATOMS            : 126
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 22.60
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  ESTIMATED COORDINATE ERROR.
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL
REMARK   3   ESD FROM SIGMAA              (A) : NULL
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL
REMARK   3
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.
REMARK   3   BOND LENGTHS                 (A) : 0.015
REMARK   3   BOND ANGLES            (DEGREES) : 2.66
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 28.74
REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.39
REMARK   3
REMARK   3  ISOTROPIC THERMAL MODEL : ISOTROPIC
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  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  : NULL
REMARK   3  TOPOLOGY FILE  1   : NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: NULL
REMARK   4
REMARK   4 1IST COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 28-DEC-01.
REMARK 100 THE RCSB ID CODE IS RCSB005243.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 01-JAN-94; 01-JAN-93
REMARK 200  TEMPERATURE           (KELVIN) : 293; 293
REMARK 200  PH                             : 8.0
REMARK 200  NUMBER OF CRYSTALS USED        : 4
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y; Y
REMARK 200  RADIATION SOURCE               : PHOTON FACTORY; PHOTON FACTORY
REMARK 200  BEAMLINE                       : BL-6A; BL-6A
REMARK 200  X-RAY GENERATOR MODEL          : NULL; NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M; NULL
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.00; 1.00
REMARK 200  MONOCHROMATOR                  : NULL; NULL
REMARK 200  OPTICS                         : NULL; NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE; IMAGE PLATE
REMARK 200  DETECTOR MANUFACTURER          : FUJI; FUJI
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : WEIS
REMARK 200  DATA SCALING SOFTWARE          : PURDUE DATA PROCESSING PACKAGE
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 19288
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.900
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 85.8
REMARK 200  DATA REDUNDANCY                : NULL
REMARK 200  R MERGE                    (I) : 0.04740
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.00
REMARK 200  COMPLETENESS FOR SHELL     (%) : 59.9
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; NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: X-PLOR
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 38.16
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.00
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 6000, EDTA, ETHANOL, TRIS-HCL,
REMARK 280  PH 8.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,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
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: MONOMERIC
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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
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 465     MET B     1
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    HIS A  89   NE2   HIS A  89   CD2    -0.083
REMARK 500    HIS A  90   NE2   HIS A  90   CD2    -0.066
REMARK 500    HIS A 124   NE2   HIS A 124   CD2    -0.083
REMARK 500    GLU A 141   CD    GLU A 141   OE2    -0.066
REMARK 500    HIS B  52   NE2   HIS B  52   CD2    -0.075
REMARK 500    HIS B  90   NE2   HIS B  90   CD2    -0.071
REMARK 500    HIS B 124   NE2   HIS B 124   CD2    -0.074
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    TYR A  23   CB  -  CG  -  CD1 ANGL. DEV. =  -3.6 DEGREES
REMARK 500    ARG A  53   NE  -  CZ  -  NH1 ANGL. DEV. =   3.4 DEGREES
REMARK 500    VAL A  54   C   -  N   -  CA  ANGL. DEV. =  15.0 DEGREES
REMARK 500    TRP A 119   CD1 -  CG  -  CD2 ANGL. DEV. =   6.2 DEGREES
REMARK 500    TRP A 119   CE2 -  CD2 -  CG  ANGL. DEV. =  -5.9 DEGREES
REMARK 500    TYR B  23   CB  -  CG  -  CD2 ANGL. DEV. =  -4.8 DEGREES
REMARK 500    ARG B  92   NE  -  CZ  -  NH2 ANGL. DEV. =   4.0 DEGREES
REMARK 500    TRP B 119   CD1 -  CG  -  CD2 ANGL. DEV. =   7.8 DEGREES
REMARK 500    TRP B 119   CG  -  CD1 -  NE1 ANGL. DEV. =  -7.1 DEGREES
REMARK 500    TRP B 119   CE2 -  CD2 -  CG  ANGL. DEV. =  -4.9 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    ASP A  11       58.57     37.10
REMARK 500    PHE A  58      -76.03   -142.72
REMARK 500    PHE B  58      -83.70   -152.66
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525  M RES CSSEQI
REMARK 525    HOH A 173        DISTANCE =  5.08 ANGSTROMS
REMARK 525    HOH B 195        DISTANCE =  5.22 ANGSTROMS
REMARK 525    HOH B 197        DISTANCE =  5.79 ANGSTROMS
REMARK 525    HOH A 204        DISTANCE =  6.22 ANGSTROMS
DBREF  1IST A    1   162  UNP    P14832   CYPH_YEAST       0    161
DBREF  1IST B    1   162  UNP    P14832   CYPH_YEAST       0    161
SEQRES   1 A  162  MET SER GLN VAL TYR PHE ASP VAL GLU ALA ASP GLY GLN
SEQRES   2 A  162  PRO ILE GLY ARG VAL VAL PHE LYS LEU TYR ASN ASP ILE
SEQRES   3 A  162  VAL PRO LYS THR ALA GLU ASN PHE ARG ALA LEU CYS THR
SEQRES   4 A  162  GLY GLU LYS GLY PHE GLY TYR ALA GLY SER PRO PHE HIS
SEQRES   5 A  162  ARG VAL ILE PRO ASP PHE MET LEU GLN GLY GLY ASP PHE
SEQRES   6 A  162  THR ALA GLY ASN GLY THR GLY GLY LYS SER ILE TYR GLY
SEQRES   7 A  162  GLY LYS PHE PRO ASP GLU ASN PHE LYS LYS HIS HIS ASP
SEQRES   8 A  162  ARG PRO GLY LEU LEU SER MET ALA ASN ALA GLY PRO ASN
SEQRES   9 A  162  THR ASN GLY SER GLN PHE PHE ILE THR THR VAL PRO CYS
SEQRES  10 A  162  PRO TRP LEU ASP GLY LYS HIS VAL VAL PHE GLY GLU VAL
SEQRES  11 A  162  VAL ASP GLY TYR ASP ILE VAL LYS LYS VAL GLU SER LEU
SEQRES  12 A  162  GLY SER PRO SER GLY ALA THR LYS ALA ARG ILE VAL VAL
SEQRES  13 A  162  ALA LYS SER GLY GLU LEU
SEQRES   1 B  162  MET SER GLN VAL TYR PHE ASP VAL GLU ALA ASP GLY GLN
SEQRES   2 B  162  PRO ILE GLY ARG VAL VAL PHE LYS LEU TYR ASN ASP ILE
SEQRES   3 B  162  VAL PRO LYS THR ALA GLU ASN PHE ARG ALA LEU CYS THR
SEQRES   4 B  162  GLY GLU LYS GLY PHE GLY TYR ALA GLY SER PRO PHE HIS
SEQRES   5 B  162  ARG VAL ILE PRO ASP PHE MET LEU GLN GLY GLY ASP PHE
SEQRES   6 B  162  THR ALA GLY ASN GLY THR GLY GLY LYS SER ILE TYR GLY
SEQRES   7 B  162  GLY LYS PHE PRO ASP GLU ASN PHE LYS LYS HIS HIS ASP
SEQRES   8 B  162  ARG PRO GLY LEU LEU SER MET ALA ASN ALA GLY PRO ASN
SEQRES   9 B  162  THR ASN GLY SER GLN PHE PHE ILE THR THR VAL PRO CYS
SEQRES  10 B  162  PRO TRP LEU ASP GLY LYS HIS VAL VAL PHE GLY GLU VAL
SEQRES  11 B  162  VAL ASP GLY TYR ASP ILE VAL LYS LYS VAL GLU SER LEU
SEQRES  12 B  162  GLY SER PRO SER GLY ALA THR LYS ALA ARG ILE VAL VAL
SEQRES  13 B  162  ALA LYS SER GLY GLU LEU
FORMUL   3  HOH   *126(H2 O)
HELIX    1   1 TYR A   23  VAL A   27  5                                   5
HELIX    2   2 PRO A   28  THR A   39  1                                  12
HELIX    3   3 CYS A  117  ASP A  121  5                                   5
HELIX    4   4 GLY A  133  VAL A  140  1                                   8
HELIX    5   5 GLU A  141  GLY A  144  5                                   4
HELIX    6   6 TYR B   23  VAL B   27  5                                   5
HELIX    7   7 PRO B   28  THR B   39  1                                  12
HELIX    8   8 CYS B  117  ASP B  121  5                                   5
HELIX    9   9 GLY B  133  VAL B  140  1                                   8
HELIX   10  10 GLU B  141  GLY B  144  5                                   4
SHEET    1   A 9 SER A   2  GLU A   9  0
SHEET    2   A 9 PRO A  14  LEU A  22 -1
SHEET    3   A 9 VAL A 125  ASP A 132 -1
SHEET    4   A 9 GLY A  94  ALA A  99 -1
SHEET    5   A 9 GLN A 109  THR A 114 -1
SHEET    6   A 9 MET A  59  GLY A  62 -1
SHEET    7   A 9 GLY A  48  VAL A  54 -1
SHEET    8   A 9 ARG A 153  LEU A 162 -1
SHEET    9   A 9 SER A   2  GLU A   9 -1
SHEET    1   B 9 SER B   2  GLU B   9  0
SHEET    2   B 9 PRO B  14  LEU B  22 -1  O  PHE B  20   N  VAL B   4
SHEET    3   B 9 VAL B 125  ASP B 132 -1  O  VAL B 131   N  VAL B  19
SHEET    4   B 9 GLY B  94  ALA B  99 -1  N  LEU B  96   O  PHE B 127
SHEET    5   B 9 GLN B 109  THR B 114 -1  O  PHE B 111   N  SER B  97
SHEET    6   B 9 MET B  59  GLY B  62 -1  N  LEU B  60   O  ILE B 112
SHEET    7   B 9 GLY B  48  VAL B  54 -1  N  ILE B  55   O  MET B  59
SHEET    8   B 9 ARG B 153  LEU B 162 -1  O  VAL B 156   N  SER B  49
SHEET    9   B 9 SER B   2  GLU B   9 -1  N  ASP B   7   O  LYS B 158
CRYST1   44.950   53.110   32.018  84.91  95.22 108.56 P 1           2
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      0.022247  0.007469  0.001562        0.00000
SCALE2      0.000000  0.019862 -0.001261        0.00000
SCALE3      0.000000  0.000000  0.031426        0.00000
      
PROCHECK
Go to PROCHECK summary
 References