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PDBsum entry 2dg9

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Isomerase PDB id
2dg9
Jmol
Contents
Protein chain
107 a.a.
Ligands
RAP
GOL
Waters ×140
HEADER    ISOMERASE                               09-MAR-06   2DG9
TITLE     FK506-BINDING PROTEIN MUTANT WL59 COMPLEXED WITH RAPAMYCIN
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: FK506-BINDING PROTEIN 1A;
COMPND   3 CHAIN: A;
COMPND   4 SYNONYM: PEPTIDYL-PROLYL CIS-TRANS ISOMERASE, PPIASE, ROTAMASE, 12
COMPND   5 KDA FKBP, FKBP-12, IMMUNOPHILIN FKBP12;
COMPND   6 EC: 5.2.1.8;
COMPND   7 ENGINEERED: YES;
COMPND   8 MUTATION: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE   3 ORGANISM_COMMON: HUMAN;
SOURCE   4 ORGANISM_TAXID: 9606;
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: PTRCGST
KEYWDS    IMMUNOPHILIN, ISOMERASE, ROTAMASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    K.F.FULTON,S.E.JACKSON,A.M.BUCKLE
REVDAT   4   13-JUL-11 2DG9    1       VERSN
REVDAT   3   24-FEB-09 2DG9    1       VERSN
REVDAT   2   20-MAR-07 2DG9    1       DBREF  SEQADV
REVDAT   1   25-APR-06 2DG9    0
JRNL        AUTH   K.F.FULTON,S.E.JACKSON,A.M.BUCKLE
JRNL        TITL   ENERGETIC AND STRUCTURAL ANALYSIS OF THE ROLE OF TRYPTOPHAN
JRNL        TITL 2 59 IN FKBP12
JRNL        REF    BIOCHEMISTRY                  V.  42  2364 2003
JRNL        REFN                   ISSN 0006-2960
JRNL        PMID   12600203
JRNL        DOI    10.1021/BI020564A
REMARK   2
REMARK   2 RESOLUTION.    1.70 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.2.0019
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) : 1.70
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 35.58
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000
REMARK   3   COMPLETENESS FOR RANGE        (%) : 88.5
REMARK   3   NUMBER OF REFLECTIONS             : 10805
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 + TEST SET) : 0.209
REMARK   3   R VALUE            (WORKING SET) : 0.208
REMARK   3   FREE R VALUE                     : 0.239
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000
REMARK   3   FREE R VALUE TEST SET COUNT      : 567
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) : 1.70
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.75
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 795
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 90.32
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2990
REMARK   3   BIN FREE R VALUE SET COUNT          : 35
REMARK   3   BIN FREE R VALUE                    : 0.3710
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 795
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 71
REMARK   3   SOLVENT ATOMS            : 140
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 33.68
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 1.75000
REMARK   3    B22 (A**2) : -0.95000
REMARK   3    B33 (A**2) : -0.80000
REMARK   3    B12 (A**2) : 0.00000
REMARK   3    B13 (A**2) : 0.00000
REMARK   3    B23 (A**2) : 0.00000
REMARK   3
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.
REMARK   3   ESU BASED ON R VALUE                            (A): 0.146
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.132
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.098
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.727
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.955
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.933
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):   896 ; 0.006 ; 0.022
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  1214 ; 1.072 ; 2.064
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   106 ; 5.726 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    33 ;28.543 ;24.242
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   137 ;12.096 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):     4 ; 8.678 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   139 ; 0.063 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):   663 ; 0.002 ; 0.020
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):   381 ; 0.165 ; 0.200
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):   593 ; 0.311 ; 0.200
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   116 ; 0.079 ; 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):    29 ; 0.142 ; 0.200
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    16 ; 0.108 ; 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):   555 ; 0.244 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):   852 ; 0.400 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   383 ; 0.513 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   362 ; 0.738 ; 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 WITH MASK
REMARK   3   PARAMETERS FOR MASK CALCULATION
REMARK   3   VDW PROBE RADIUS   : 1.40
REMARK   3   ION PROBE RADIUS   : 0.80
REMARK   3   SHRINKAGE RADIUS   : 0.80
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK   3  POSITIONS
REMARK   4
REMARK   4 2DG9 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 14-MAR-06.
REMARK 100 THE RCSB ID CODE IS RCSB025382.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 29-AUG-03
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 4.6
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          : ELLIOTT GX-13
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418
REMARK 200  MONOCHROMATOR                  : GRAPHITE
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200  DATA SCALING SOFTWARE          : NULL
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 10805
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.700
REMARK 200  RESOLUTION RANGE LOW       (A) : 35.600
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 88.5
REMARK 200  DATA REDUNDANCY                : 3.700
REMARK 200  R MERGE                    (I) : 0.05200
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 20.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.70
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 35.60
REMARK 200  COMPLETENESS FOR SHELL     (%) : 91.2
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.30
REMARK 200  R MERGE FOR SHELL          (I) : 0.27200
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : 2.600
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 48.47
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.39
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% PEG MME 2000, 0.2M AMMONIUM
REMARK 280  SULPHATE, PH 4.6, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K
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       22.05950
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       25.80250
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       24.67950
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       25.80250
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       22.05950
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       24.67950
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 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     GLN A   3    CG   CD   OE1  NE2
REMARK 470     ARG A  13    CD   NE   CZ   NH1  NH2
REMARK 470     LYS A  17    CG   CD   CE   NZ
REMARK 470     ARG A  18    CG   CD   NE   CZ   NH1  NH2
REMARK 470     ASP A  32    CG   OD1  OD2
REMARK 470     LYS A  44    CD   CE   NZ
REMARK 470     LEU A  50    CD1  CD2
REMARK 470     LYS A  52    CD   CE   NZ
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    ARG A  13      -35.65   -133.55
REMARK 500    ALA A  81     -114.71   -124.38
REMARK 500    ILE A  90      -51.52   -125.53
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE RAP A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 1001
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2DG3   RELATED DB: PDB
REMARK 900 THE WILDTYPE FBP12
REMARK 900 RELATED ID: 2DG4   RELATED DB: PDB
DBREF  2DG9 A    1   107  UNP    P62942   FKB1A_HUMAN      2    108
SEQADV 2DG9 LEU A   59  UNP  P62942    TRP    60 ENGINEERED
SEQRES   1 A  107  GLY VAL GLN VAL GLU THR ILE SER PRO GLY ASP GLY ARG
SEQRES   2 A  107  THR PHE PRO LYS ARG GLY GLN THR CYS VAL VAL HIS TYR
SEQRES   3 A  107  THR GLY MET LEU GLU ASP GLY LYS LYS PHE ASP SER SER
SEQRES   4 A  107  ARG ASP ARG ASN LYS PRO PHE LYS PHE MET LEU GLY LYS
SEQRES   5 A  107  GLN GLU VAL ILE ARG GLY LEU GLU GLU GLY VAL ALA GLN
SEQRES   6 A  107  MET SER VAL GLY GLN ARG ALA LYS LEU THR ILE SER PRO
SEQRES   7 A  107  ASP TYR ALA TYR GLY ALA THR GLY HIS PRO GLY ILE ILE
SEQRES   8 A  107  PRO PRO HIS ALA THR LEU VAL PHE ASP VAL GLU LEU LEU
SEQRES   9 A  107  LYS LEU GLU
HET    RAP  A 501      65
HET    GOL  A1001       6
HETNAM     RAP RAPAMYCIN IMMUNOSUPPRESSANT DRUG
HETNAM     GOL GLYCEROL
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL   2  RAP    C51 H79 N O13
FORMUL   3  GOL    C3 H8 O3
FORMUL   4  HOH   *140(H2 O)
HELIX    1   1 ILE A   56  GLN A   65  1                                  10
HELIX    2   2 PRO A   78  ALA A   81  5                                   4
SHEET    1   A 5 VAL A   2  SER A   8  0
SHEET    2   A 5 ARG A  71  ILE A  76 -1  O  LYS A  73   N  GLU A   5
SHEET    3   A 5 LEU A  97  GLU A 107 -1  O  PHE A  99   N  LEU A  74
SHEET    4   A 5 THR A  21  LEU A  30 -1  N  MET A  29   O  VAL A  98
SHEET    5   A 5 LYS A  35  SER A  38 -1  O  ASP A  37   N  GLY A  28
SHEET    1   B 5 VAL A   2  SER A   8  0
SHEET    2   B 5 ARG A  71  ILE A  76 -1  O  LYS A  73   N  GLU A   5
SHEET    3   B 5 LEU A  97  GLU A 107 -1  O  PHE A  99   N  LEU A  74
SHEET    4   B 5 THR A  21  LEU A  30 -1  N  MET A  29   O  VAL A  98
SHEET    5   B 5 PHE A  46  MET A  49 -1  O  PHE A  46   N  VAL A  24
SITE     1 AC1 23 THR A   6  TYR A  26  THR A  27  MET A  29
SITE     2 AC1 23 LYS A  35  PHE A  36  ASP A  37  PHE A  46
SITE     3 AC1 23 GLN A  53  GLU A  54  VAL A  55  ILE A  56
SITE     4 AC1 23 LEU A  59  LYS A  73  TYR A  82  HIS A  87
SITE     5 AC1 23 PHE A  99  ASP A 100  HOH A1009  HOH A1044
SITE     6 AC1 23 HOH A1069  HOH A1072  HOH A1108
SITE     1 AC2  5 TYR A  82  GLY A  83  ALA A  84  THR A  85
SITE     2 AC2  5 HOH A1062
CRYST1   44.119   49.359   51.605  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      0.022666  0.000000  0.000000        0.00000
SCALE2      0.000000  0.020260  0.000000        0.00000
SCALE3      0.000000  0.000000  0.019378        0.00000
      
PROCHECK
Go to PROCHECK summary
 References