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PDBsum entry 4dh0

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Isomerase/immunosuppressant PDB id
4dh0
Jmol
Contents
Protein chain
107 a.a.
Ligands
MR8
Waters ×76
HEADER    ISOMERASE/IMMUNOSUPPRESSANT             27-JAN-12   4DH0
TITLE     X-RAY CRYSTAL STRUCTURE OF 28-O-METHYLRAPAMYCIN COMPLEXED WITH FKBP12:
TITLE    2 IS THE CYCLOHEXYL MOIETY PART OF THE EFFECTOR DOMAIN OF RAPAMYCIN?
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: PEPTIDYL-PROLYL CIS-TRANS ISOMERASE FKBP1A;
COMPND   3 CHAIN: A;
COMPND   4 SYNONYM: PPIASE FKBP1A, 12 KDA FK506-BINDING PROTEIN, 12 KDA FKBP,
COMPND   5 FKBP-12, FK506-BINDING PROTEIN 1A, FKBP-1A, IMMUNOPHILIN FKBP12,
COMPND   6 ROTAMASE;
COMPND   7 EC: 5.2.1.8;
COMPND   8 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE   3 ORGANISM_COMMON: HUMAN;
SOURCE   4 ORGANISM_TAXID: 9606;
SOURCE   5 GENE: FKBP1A, FKBP1, FKBP12;
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS    PEPTIDYL-PROLYL CIS-TRANS ISOMERASE, ISOMERASE-IMMUNOSUPPRESSANT
KEYWDS   2 COMPLEX
EXPDTA    X-RAY DIFFRACTION
AUTHOR    J.KALLEN
REVDAT   1   15-FEB-12 4DH0    0
JRNL        AUTH   J.KALLEN,R.SEDRANI,S.COTTENS
JRNL        TITL   X-RAY CRYSTAL STRUCTURE OF 28-O-METHYLRAPAMYCIN COMPLEXED
JRNL        TITL 2 WITH FKBP12: IS THE CYCLOHEXYL MOIETY PART OF THE EFFECTOR
JRNL        TITL 3 DOMAIN OF RAPAMYCIN?
JRNL        REF    J.AM.CHEM.SOC.                V. 118  5857 1996
JRNL        REFN                   ISSN 0002-7863
JRNL        DOI    10.1021/JA954328H
REMARK   2
REMARK   2 RESOLUTION.    2.10 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.5.0063
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) : 2.10
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 36.96
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000
REMARK   3   COMPLETENESS FOR RANGE        (%) : 89.6
REMARK   3   NUMBER OF REFLECTIONS             : 6604
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) : 0.219
REMARK   3   R VALUE            (WORKING SET) : 0.217
REMARK   3   FREE R VALUE                     : 0.257
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.600
REMARK   3   FREE R VALUE TEST SET COUNT      : 316
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) : 2.10
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.15
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 409
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 77.70
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3150
REMARK   3   BIN FREE R VALUE SET COUNT          : 23
REMARK   3   BIN FREE R VALUE                    : 0.3360
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 832
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 66
REMARK   3   SOLVENT ATOMS            : 76
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 25.55
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 0.45000
REMARK   3    B22 (A**2) : 0.40000
REMARK   3    B33 (A**2) : -0.85000
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): 0.288
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.219
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.142
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.534
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.933
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.897
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):   920 ; 0.006 ; 0.022
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  1245 ; 0.966 ; 2.051
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   106 ; 5.585 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    37 ;31.498 ;23.514
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   148 ;14.395 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):     6 ; 8.727 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   137 ; 0.061 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):   689 ; 0.003 ; 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):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL
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):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL
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):   529 ; 0.370 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):   853 ; 0.704 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   391 ; 0.858 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   392 ; 1.537 ; 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 : MASK
REMARK   3   PARAMETERS FOR MASK CALCULATION
REMARK   3   VDW PROBE RADIUS   : 1.20
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 4DH0 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-FEB-12.
REMARK 100 THE RCSB ID CODE IS RCSB070317.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 29-NOV-93
REMARK 200  TEMPERATURE           (KELVIN) : 293.0
REMARK 200  PH                             : 7.7
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          : ENRAF-NONIUS FR571
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                  : AREA DETECTOR
REMARK 200  DETECTOR MANUFACTURER          : ENRAF-NONIUS FAST
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MADNES
REMARK 200  DATA SCALING SOFTWARE          : ROTAVATA
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 6946
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.100
REMARK 200  RESOLUTION RANGE LOW       (A) : 15.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 90.0
REMARK 200  DATA REDUNDANCY                : 2.300
REMARK 200  R MERGE                    (I) : NULL
REMARK 200  R SYM                      (I) : 0.09100
REMARK 200   FOR THE DATA SET  : 6.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.15
REMARK 200  COMPLETENESS FOR SHELL     (%) : 84.0
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL
REMARK 200  R MERGE FOR SHELL          (I) : 0.29000
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: X-PLOR
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 53.43
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.64
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 35% AMMONIUM SULPHATE, 0.1M NA/K
REMARK 280  PHOSPHATE, PH 7.7, 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       22.75000
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       27.65000
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       24.85000
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       27.65000
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       22.75000
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       24.85000
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 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      -38.31   -144.85
REMARK 500    ALA A  81     -112.35   -121.05
REMARK 500    ILE A  90      -56.61   -129.79
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 357        DISTANCE =  5.95 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MR8 A 201
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1FKL   RELATED DB: PDB
REMARK 900 THE SAME PROTEIN COMPLEXED WITH RAPAMYCIN.
DBREF  4DH0 A    1   107  UNP    P62942   FKB1A_HUMAN      2    108
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 TRP 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    MR8  A 201      66
HETNAM     MR8 28-O-METHYLRAPAMYCIN
HETSYN     MR8 (3S,6R,7E,9R,10R,12R,14S,15E,17E,19E,21S,23S,26R,27R,
HETSYN   2 MR8  34AS)-27-HYDROXY-3-{(2R)-1-[(1S,3R,4R)-4-HYDROXY-3-
HETSYN   3 MR8  METHOXYCYCLOHEXYL]PROPAN-2-YL}-9,10,21-TRIMETHOXY-6,8,
HETSYN   4 MR8  12,14,20,26-HEXAMETHYL-9,10,12,13,14,21,22,23,24,25,
HETSYN   5 MR8  26,27,32,33,34,34A-HEXADECAHYDRO-3H-23,27-
HETSYN   6 MR8  EPOXYPYRIDO[2,1-C][1,4]OXAZACYCLOHENTRIACONTINE-1,5,
HETSYN   7 MR8  11,28,29(4H,6H,31H)-PENTONE 28-O-METHYLRAPAMYCIN
FORMUL   2  MR8    C52 H81 N O13
FORMUL   3  HOH   *76(H2 O)
HELIX    1   1 ILE A   56  ALA A   64  1                                   9
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  LEU A  97   N  ILE A  76
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  LEU A  97   N  ILE A  76
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 17 GLU A   5  THR A   6  TYR A  26  THR A  27
SITE     2 AC1 17 PHE A  36  ASP A  37  PHE A  46  GLU A  54
SITE     3 AC1 17 VAL A  55  ILE A  56  TRP A  59  ARG A  71
SITE     4 AC1 17 LYS A  73  ALA A  81  TYR A  82  ASP A 100
SITE     5 AC1 17 HOH A 321
CRYST1   45.500   49.700   55.300  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      0.021978  0.000000  0.000000        0.00000
SCALE2      0.000000  0.020121  0.000000        0.00000
SCALE3      0.000000  0.000000  0.018083        0.00000
      
PROCHECK
Go to PROCHECK summary
 References