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PDBsum entry 1ihg

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Isomerase PDB id
1ihg
Jmol
Contents
Protein chain
364 a.a. *
Ligands
GOL
Waters ×489
* Residue conservation analysis
HEADER    ISOMERASE                               19-APR-01   1IHG
TITLE     BOVINE CYCLOPHILIN 40, MONOCLINIC FORM
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: CYCLOPHILIN 40;
COMPND   3 CHAIN: A;
COMPND   4 SYNONYM: 40 KDA PEPTIDYL-PROLYL CIS-TRANS ISOMERASE;
COMPND   5 EC: 5.2.1.8;
COMPND   6 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: BOS TAURUS;
SOURCE   3 ORGANISM_COMMON: CATTLE;
SOURCE   4 ORGANISM_TAXID: 9913;
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PET11
KEYWDS    PPIASE IMMUNOPHILIN TETRATRICOPEPTIDE, ISOMERASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    P.TAYLOR,J.DORNAN,A.CARRELLO,R.F.MINCHIN,T.RATAJCZAK,M.D.WALKINSHAW
REVDAT   3   13-JUL-11 1IHG    1       VERSN
REVDAT   2   24-FEB-09 1IHG    1       VERSN
REVDAT   1   16-MAY-01 1IHG    0
JRNL        AUTH   P.TAYLOR,J.DORNAN,A.CARRELLO,R.F.MINCHIN,T.RATAJCZAK,
JRNL        AUTH 2 M.D.WALKINSHAW
JRNL        TITL   TWO STRUCTURES OF CYCLOPHILIN 40: FOLDING AND FIDELITY IN
JRNL        TITL 2 THE TPR DOMAINS.
JRNL        REF    STRUCTURE                     V.   9   431 2001
JRNL        REFN                   ISSN 0969-2126
JRNL        PMID   11377203
JRNL        DOI    10.1016/S0969-2126(01)00603-7
REMARK   2
REMARK   2 RESOLUTION.    1.80 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : SHELXL-97
REMARK   3   AUTHORS     : G.M.SHELDRICK
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 24.00
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000
REMARK   3   COMPLETENESS FOR RANGE        (%) : 93.5
REMARK   3   CROSS-VALIDATION METHOD           : FREE R
REMARK   3   FREE R VALUE TEST SET SELECTION   : RANDOM
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT (NO CUTOFF).
REMARK   3   R VALUE   (WORKING + TEST SET, NO CUTOFF) : 0.178
REMARK   3   R VALUE          (WORKING SET, NO CUTOFF) : 0.178
REMARK   3   FREE R VALUE                  (NO CUTOFF) : 0.256
REMARK   3   FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : 5.000
REMARK   3   FREE R VALUE TEST SET COUNT   (NO CUTOFF) : 2035
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (NO CUTOFF) : 38413
REMARK   3
REMARK   3  FIT/AGREEMENT OF MODEL FOR DATA WITH F>4SIG(F).
REMARK   3   R VALUE   (WORKING + TEST SET, F>4SIG(F)) : 0.176
REMARK   3   R VALUE          (WORKING SET, F>4SIG(F)) : NULL
REMARK   3   FREE R VALUE                  (F>4SIG(F)) : 0.250
REMARK   3   FREE R VALUE TEST SET SIZE (%, F>4SIG(F)) : 5.000
REMARK   3   FREE R VALUE TEST SET COUNT   (F>4SIG(F)) : NULL
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (F>4SIG(F)) : 37387
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS      : 2810
REMARK   3   NUCLEIC ACID ATOMS : 0
REMARK   3   HETEROGEN ATOMS    : 6
REMARK   3   SOLVENT ATOMS      : 489
REMARK   3
REMARK   3  MODEL REFINEMENT.
REMARK   3   OCCUPANCY SUM OF NON-HYDROGEN ATOMS      : 3305.00
REMARK   3   OCCUPANCY SUM OF HYDROGEN ATOMS          : 0.00
REMARK   3   NUMBER OF DISCRETELY DISORDERED RESIDUES : NULL
REMARK   3   NUMBER OF LEAST-SQUARES PARAMETERS       : 13223
REMARK   3   NUMBER OF RESTRAINTS                     : 11467
REMARK   3
REMARK   3  RMS DEVIATIONS FROM RESTRAINT TARGET VALUES.
REMARK   3   BOND LENGTHS                         (A) : 0.000
REMARK   3   ANGLE DISTANCES                      (A) : 0.020
REMARK   3   SIMILAR DISTANCES (NO TARGET VALUES) (A) : 0.000
REMARK   3   DISTANCES FROM RESTRAINT PLANES      (A) : 0.025
REMARK   3   ZERO CHIRAL VOLUMES               (A**3) : 0.030
REMARK   3   NON-ZERO CHIRAL VOLUMES           (A**3) : 0.040
REMARK   3   ANTI-BUMPING DISTANCE RESTRAINTS     (A) : 0.000
REMARK   3   RIGID-BOND ADP COMPONENTS         (A**2) : 0.000
REMARK   3   SIMILAR ADP COMPONENTS            (A**2) : 0.070
REMARK   3   APPROXIMATELY ISOTROPIC ADPS      (A**2) : 0.000
REMARK   3
REMARK   3  BULK SOLVENT MODELING.
REMARK   3   METHOD USED: NULL
REMARK   3
REMARK   3  STEREOCHEMISTRY TARGET VALUES : ENGH AND HUBER
REMARK   3   SPECIAL CASE: NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: NULL
REMARK   4
REMARK   4 1IHG COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-APR-01.
REMARK 100 THE RCSB ID CODE IS RCSB013270.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 10-JUN-99
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 6.1
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : SRS
REMARK 200  BEAMLINE                       : PX9.6
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.87
REMARK 200  MONOCHROMATOR                  : SINGLE CRYSTAL SI
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 41259
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.800
REMARK 200  RESOLUTION RANGE LOW       (A) : 28.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.3
REMARK 200  DATA REDUNDANCY                : 3.700
REMARK 200  R MERGE                    (I) : 0.05000
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 20.6700
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.83
REMARK 200  COMPLETENESS FOR SHELL     (%) : 87.3
REMARK 200  DATA REDUNDANCY IN SHELL       : 1.87
REMARK 200  R MERGE FOR SHELL          (I) : 0.09600
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : 9.030
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: CYCLOPHILIN A
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 54.99
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.00
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 4000, MES GLYCEROL SODIUM
REMARK 280  CHLORIDE, PH 6.1, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277K
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       63.06250
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       23.66400
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       63.06250
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       23.66400
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 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 465     ALA A   366
REMARK 465     LYS A   367
REMARK 465     MET A   368
REMARK 465     PHE A   369
REMARK 465     ALA A   370
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    ARG A  49   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.0 DEGREES
REMARK 500    PHE A 132   CB  -  CG  -  CD2 ANGL. DEV. =   4.8 DEGREES
REMARK 500    PHE A 132   CB  -  CG  -  CD1 ANGL. DEV. =  -5.0 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  80      -75.27   -144.42
REMARK 500    ASN A  91       13.61   -145.47
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 667        DISTANCE =  5.06 ANGSTROMS
REMARK 525    HOH A 834        DISTANCE =  5.71 ANGSTROMS
REMARK 525    HOH A 842        DISTANCE =  5.12 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 371
DBREF  1IHG A    1   370  UNP    P26882   PPID_BOVIN       1    370
SEQRES   1 A  370  MET SER HIS PRO SER PRO GLN ALA LYS PRO SER ASN PRO
SEQRES   2 A  370  SER ASN PRO ARG VAL PHE PHE ASP VAL ASP ILE GLY GLY
SEQRES   3 A  370  GLU ARG VAL GLY ARG ILE VAL LEU GLU LEU PHE ALA ASP
SEQRES   4 A  370  ILE VAL PRO LYS THR ALA GLU ASN PHE ARG ALA LEU CYS
SEQRES   5 A  370  THR GLY GLU LYS GLY ILE GLY PRO THR THR GLY LYS PRO
SEQRES   6 A  370  LEU HIS PHE LYS GLY CYS PRO PHE HIS ARG ILE ILE LYS
SEQRES   7 A  370  LYS PHE MET ILE GLN GLY GLY ASP PHE SER ASN GLN ASN
SEQRES   8 A  370  GLY THR GLY GLY GLU SER ILE TYR GLY GLU LYS PHE GLU
SEQRES   9 A  370  ASP GLU ASN PHE HIS TYR LYS HIS ASP LYS GLU GLY LEU
SEQRES  10 A  370  LEU SER MET ALA ASN ALA GLY SER ASN THR ASN GLY SER
SEQRES  11 A  370  GLN PHE PHE ILE THR THR VAL PRO THR PRO HIS LEU ASP
SEQRES  12 A  370  GLY LYS HIS VAL VAL PHE GLY GLN VAL ILE LYS GLY MET
SEQRES  13 A  370  GLY VAL ALA LYS ILE LEU GLU ASN VAL GLU VAL LYS GLY
SEQRES  14 A  370  GLU LYS PRO ALA LYS LEU CYS VAL ILE ALA GLU CYS GLY
SEQRES  15 A  370  GLU LEU LYS GLU GLY ASP ASP TRP GLY ILE PHE PRO LYS
SEQRES  16 A  370  ASP GLY SER GLY ASP SER HIS PRO ASP PHE PRO GLU ASP
SEQRES  17 A  370  ALA ASP VAL ASP LEU LYS ASP VAL ASP LYS ILE LEU LEU
SEQRES  18 A  370  ILE SER GLU ASP LEU LYS ASN ILE GLY ASN THR PHE PHE
SEQRES  19 A  370  LYS SER GLN ASN TRP GLU MET ALA ILE LYS LYS TYR THR
SEQRES  20 A  370  LYS VAL LEU ARG TYR VAL GLU GLY SER ARG ALA ALA ALA
SEQRES  21 A  370  GLU ASP ALA ASP GLY ALA LYS LEU GLN PRO VAL ALA LEU
SEQRES  22 A  370  SER CYS VAL LEU ASN ILE GLY ALA CYS LYS LEU LYS MET
SEQRES  23 A  370  SER ASP TRP GLN GLY ALA VAL ASP SER CYS LEU GLU ALA
SEQRES  24 A  370  LEU GLU ILE ASP PRO SER ASN THR LYS ALA LEU TYR ARG
SEQRES  25 A  370  ARG ALA GLN GLY TRP GLN GLY LEU LYS GLU TYR ASP GLN
SEQRES  26 A  370  ALA LEU ALA ASP LEU LYS LYS ALA GLN GLU ILE ALA PRO
SEQRES  27 A  370  GLU ASP LYS ALA ILE GLN ALA GLU LEU LEU LYS VAL LYS
SEQRES  28 A  370  GLN LYS ILE LYS ALA GLN LYS ASP LYS GLU LYS ALA ALA
SEQRES  29 A  370  TYR ALA LYS MET PHE ALA
HET    GOL  A 371       6
HETNAM     GOL GLYCEROL
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL   2  GOL    C3 H8 O3
FORMUL   3  HOH   *489(H2 O)
HELIX    1   1 VAL A   41  GLY A   54  1                                  14
HELIX    2   2 THR A  139  ASP A  143  5                                   5
HELIX    3   3 GLY A  155  ASN A  164  1                                  10
HELIX    4   4 PHE A  205  ALA A  209  5                                   5
HELIX    5   5 ASP A  215  SER A  236  1                                  22
HELIX    6   6 ASN A  238  ALA A  260  1                                  23
HELIX    7   7 GLU A  261  ALA A  266  1                                   6
HELIX    8   8 LEU A  268  MET A  286  1                                  19
HELIX    9   9 ASP A  288  GLU A  301  1                                  14
HELIX   10  10 ASN A  306  LEU A  320  1                                  15
HELIX   11  11 GLU A  322  ALA A  337  1                                  16
HELIX   12  12 ASP A  340  ALA A  363  1                                  24
SHEET    1   A 8 PHE A  73  ILE A  77  0
SHEET    2   A 8 MET A  81  GLY A  84 -1  O  MET A  81   N  ILE A  77
SHEET    3   A 8 PHE A 132  THR A 135 -1  O  PHE A 132   N  GLY A  84
SHEET    4   A 8 LEU A 117  MET A 120 -1  O  LEU A 117   N  THR A 135
SHEET    5   A 8 VAL A 148  LYS A 154 -1  N  PHE A 149   O  LEU A 118
SHEET    6   A 8 GLU A  27  LEU A  36 -1  O  VAL A  33   N  ILE A 153
SHEET    7   A 8 ARG A  17  ILE A  24 -1  O  VAL A  18   N  LEU A  34
SHEET    8   A 8 CYS A 176  LEU A 184 -1  N  VAL A 177   O  ASP A  23
SHEET    1   B 2 VAL A 167  LYS A 168  0
SHEET    2   B 2 LYS A 171  PRO A 172 -1  O  LYS A 171   N  LYS A 168
CISPEP   1 LYS A    9    PRO A   10          0         3.36
SITE     1 AC1  8 PHE A 205  PRO A 206  GLU A 207  ARG A 251
SITE     2 AC1  8 HOH A 411  HOH A 420  HOH A 745  HOH A 884
CRYST1  126.125   47.328   85.563  90.00 119.42  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      0.007929  0.000000  0.004471        0.00000
SCALE2      0.000000  0.021129  0.000000        0.00000
SCALE3      0.000000  0.000000  0.013418        0.00000
      
PROCHECK
Go to PROCHECK summary
 References