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PDBsum entry 1mf8

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Hydrolase/isomerase/immunosuppressant PDB id
1mf8
Jmol
Contents
Protein chains
352 a.a. *
164 a.a. *
164 a.a. *
11 a.a. *
Ligands
PO4
Metals
_CA ×4
* Residue conservation analysis
HEADER    HYDROLASE/ISOMERASE/IMMUNOSUPPRESSANT   09-AUG-02   1MF8
TITLE     CRYSTAL STRUCTURE OF HUMAN CALCINEURIN COMPLEXED WITH CYCLOSPORIN A
TITLE    2 AND HUMAN CYCLOPHILIN
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: CALMODULIN-DEPENDENT CALCINEURIN A SUBUNIT, ALPHA ISOFORM;
COMPND   3 CHAIN: A;
COMPND   4 FRAGMENT: TRUNCATED FORM (RESIDUES 20-392);
COMPND   5 SYNONYM: SERINE/THREONINE PROTEIN PHOSPHATASE 2B CATALYTIC SUBUNIT
COMPND   6 ALPHA ISOFORM, CAM-PRP CATALYTIC SUBUNIT;
COMPND   7 EC: 3.1.3.16;
COMPND   8 ENGINEERED: YES;
COMPND   9 MOL_ID: 2;
COMPND  10 MOLECULE: CALCINEURIN B SUBUNIT ISOFORM 1;
COMPND  11 CHAIN: B;
COMPND  12 SYNONYM: PROTEIN PHOSPHATASE 2B REGULATORY SUBUNIT 1, PROTEIN
COMPND  13 PHOSPHATASE 3 REGULATORY SUBUNIT B ALPHA ISOFORM 1;
COMPND  14 EC: 3.1.3.16;
COMPND  15 ENGINEERED: YES;
COMPND  16 MOL_ID: 3;
COMPND  17 MOLECULE: PEPTIDYL-PROLYL CIS-TRANS ISOMERASE A;
COMPND  18 CHAIN: C;
COMPND  19 SYNONYM: PPIASE, ROTAMASE, CYCLOPHILIN A;
COMPND  20 EC: 5.2.1.8;
COMPND  21 ENGINEERED: YES;
COMPND  22 MOL_ID: 4;
COMPND  23 MOLECULE: CYCLOSPORIN A;
COMPND  24 CHAIN: D;
COMPND  25 SYNONYM: CYCLOSPORINE, CICLOSPORIN, CICLOSPORINE;
COMPND  26 ENGINEERED: 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;
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3) PLYSS;
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PETCN ALPHA;
SOURCE  10 MOL_ID: 2;
SOURCE  11 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE  12 ORGANISM_COMMON: HUMAN;
SOURCE  13 ORGANISM_TAXID: 9606;
SOURCE  14 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE  15 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE  16 EXPRESSION_SYSTEM_STRAIN: BL21(DE3) PLYSS;
SOURCE  17 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE  18 EXPRESSION_SYSTEM_PLASMID: PETCN ALPHA;
SOURCE  19 MOL_ID: 3;
SOURCE  20 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE  21 ORGANISM_COMMON: HUMAN;
SOURCE  22 ORGANISM_TAXID: 9606;
SOURCE  23 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE  24 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE  25 EXPRESSION_SYSTEM_STRAIN: BL21(DE3) CODONPLUS RIL;
SOURCE  26 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE  27 EXPRESSION_SYSTEM_PLASMID: PET3A.CYPA;
SOURCE  28 MOL_ID: 4;
SOURCE  29 SYNTHETIC: YES;
SOURCE  30 ORGANISM_SCIENTIFIC: TOLYPOCLADIUM INFLATUM;
SOURCE  31 ORGANISM_TAXID: 29910
KEYWDS    HYDROLASE-ISOMERASE-IMMUNOSUPPRESSANT COMPLEX, CALCINEURIN-
KEYWDS   2 CYCLOPHILIN-CYCLOSPORIN COMPLEX, CYCLOSPORIN A, IMMUNOSUPPRESSANT,
KEYWDS   3 HYDROLASE, ISOMERASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    L.JIN,S.C.HARRISON
REVDAT   5   27-JUL-11 1MF8    1       REMARK
REVDAT   4   13-JUL-11 1MF8    1       VERSN
REVDAT   3   24-FEB-09 1MF8    1       VERSN
REVDAT   2   23-OCT-02 1MF8    1       JRNL
REVDAT   1   16-OCT-02 1MF8    0
JRNL        AUTH   L.JIN,S.C.HARRISON
JRNL        TITL   CRYSTAL STRUCTURE OF HUMAN CALCINEURIN COMPLEXED WITH
JRNL        TITL 2 CYCLOSPORIN A AND HUMAN CYCLOPHILIN
JRNL        REF    PROC.NATL.ACAD.SCI.USA        V.  99 13522 2002
JRNL        REFN                   ISSN 0027-8424
JRNL        PMID   12357034
JRNL        DOI    10.1073/PNAS.212504399
REMARK   2
REMARK   2 RESOLUTION.    3.10 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : CNS 1.0
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 : ENGH & HUBER
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.10
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 15.00
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 95.6
REMARK   3   NUMBER OF REFLECTIONS             : 14195
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) : 0.250
REMARK   3   FREE R VALUE                     : 0.300
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL
REMARK   3   FREE R VALUE TEST SET COUNT      : 1052
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           : NULL
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL
REMARK   3   BIN R VALUE           (WORKING SET) : NULL
REMARK   3   BIN FREE R VALUE                    : NULL
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL
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            : 5513
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 9
REMARK   3   SOLVENT ATOMS            : 0
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL
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) : 0.010
REMARK   3   BOND ANGLES            (DEGREES) : 1.50
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL
REMARK   3
REMARK   3  ISOTROPIC THERMAL MODEL : NULL
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  : NULL
REMARK   3  TOPOLOGY FILE  1   : NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: NULL
REMARK   4
REMARK   4 1MF8 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 21-AUG-02.
REMARK 100 THE RCSB ID CODE IS RCSB016869.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 12-MAR-02
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 4.6
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : CHESS
REMARK 200  BEAMLINE                       : F1
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.91611
REMARK 200  MONOCHROMATOR                  : SI 111 CHANNEL
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   : 14195
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.100
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     (%) : 95.6
REMARK 200  DATA REDUNDANCY                : 5.300
REMARK 200  R MERGE                    (I) : NULL
REMARK 200  R SYM                      (I) : 0.07700
REMARK 200   FOR THE DATA SET  : 19.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.10
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.21
REMARK 200  COMPLETENESS FOR SHELL     (%) : 81.7
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL
REMARK 200  R MERGE FOR SHELL          (I) : NULL
REMARK 200  R SYM FOR SHELL            (I) : 0.37000
REMARK 200   FOR SHELL         : 3.300
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: PDB ENTRY 1AUI AND 2RMA
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 46.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.60
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 12% PEG 4000, 5MM POTASSIUM PHOSPHATE,
REMARK 280  75MM SODIUM CITRATE, 15% GLYCEROL, 5MM TRIS, PH 4.6, MICROBATCH,
REMARK 280  TEMPERATURE 292K
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       32.47450
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       56.42050
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       54.16700
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       56.42050
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       32.47450
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       54.16700
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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 7390 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 28770 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -91.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D
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 400
REMARK 400 COMPOUND
REMARK 400 CYCLOSPORIN IS A CYCLIC UNDECAPEPTIDE.
REMARK 400 HERE, CYCLOSPORIN A  IS REPRESENTED BY THE SEQUENCE (SEQRES)
REMARK 400
REMARK 400  GROUP: 1
REMARK 400   NAME: CYCLOSPORIN A
REMARK 400   CHAIN: D
REMARK 400   COMPONENT_1: PEPTIDE LIKE SEQUENCE RESIDUES 1 TO 11
REMARK 400   DESCRIPTION: CYCLOSPORIN IS A CYCLIC UNDECAPEPTIDE.
REMARK 400                CYCLIZATION IS ACHIEVED BY LINKING THE N- AND
REMARK 400                THE C- TERMINI.
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     CYS A   372
REMARK 465     SER A   373
REMARK 465     ASP A   374
REMARK 465     ASP A   375
REMARK 465     GLU A   376
REMARK 465     LEU A   377
REMARK 465     GLY A   378
REMARK 465     SER A   379
REMARK 465     GLU A   380
REMARK 465     GLU A   381
REMARK 465     ASP A   382
REMARK 465     GLY A   383
REMARK 465     PHE A   384
REMARK 465     ASP A   385
REMARK 465     GLY A   386
REMARK 465     ALA A   387
REMARK 465     THR A   388
REMARK 465     ALA A   389
REMARK 465     ALA A   390
REMARK 465     ALA A   391
REMARK 465     ARG A   392
REMARK 465     MET B     0
REMARK 465     GLY B     1
REMARK 465     ASN B     2
REMARK 465     GLU B     3
REMARK 465     ALA B     4
REMARK 465     VAL B   169
REMARK 465     GLU C   165
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480   M RES C SSEQI ATOMS
REMARK 480     SER A   26   OG
REMARK 480     LYS A   32   CE   NZ
REMARK 480     LYS A   76   CE   NZ
REMARK 480     ASN A  110   OD1  ND2
REMARK 480     GLU A  158   CG   CD   OE1  OE2
REMARK 480     SER A  233   OG
REMARK 480     GLU A  237   CD   OE1  OE2
REMARK 480     LYS A  243   CG   CD   CE   NZ
REMARK 480     GLN A  245   CG   CD   OE1  NE2
REMARK 480     THR A  252   OG1
REMARK 480     GLN A  295   CG   CD   OE1  NE2
REMARK 480     ASN A  316   CG   OD1  ND2
REMARK 480     LYS B   20   CD   CE   NZ
REMARK 480     LYS B   27   NZ
REMARK 480     LYS B   28   CD   CE   NZ
REMARK 480     SER B   36   OG
REMARK 480     GLU B   40   CG   CD   OE1  OE2
REMARK 480     MET B   43   CE
REMARK 480     GLU B   47   CG   CD   OE1  OE2
REMARK 480     GLN B   49   CG   CD   OE1  NE2
REMARK 480     LYS B   84   NZ
REMARK 480     LYS B  124   CD   CE   NZ
REMARK 480     LYS B  141   CG   CD   CE   NZ
REMARK 480     GLU B  150   CG   CD   OE1  OE2
REMARK 480     LYS B  163   NZ
REMARK 480     LYS B  164   CG   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    LEU A  29      147.14    -38.89
REMARK 500    LEU A  46      -74.61    -36.40
REMARK 500    LYS A  47      -37.64    -36.00
REMARK 500    GLU A  53        4.28     84.25
REMARK 500    HIS A  92       55.05     38.46
REMARK 500    LEU A 114      110.58   -170.70
REMARK 500    ASP A 118       67.96     71.38
REMARK 500    ASP A 121      160.20     68.27
REMARK 500    ARG A 122      -70.37     79.63
REMARK 500    THR A 143      -59.75   -123.46
REMARK 500    CYS A 153      145.38   -170.13
REMARK 500    TYR A 170     -104.07   -125.02
REMARK 500    ALA A 188     -167.79   -165.66
REMARK 500    ASN A 192       46.22     36.36
REMARK 500    GLN A 193       17.37     43.47
REMARK 500    GLN A 245       38.11    -93.54
REMARK 500    HIS A 247      -77.01    -82.86
REMARK 500    SER A 257     -148.54     59.60
REMARK 500    ALA A 280     -126.71   -110.65
REMARK 500    HIS A 281      -49.50     80.04
REMARK 500    TYR A 288      169.20    173.70
REMARK 500    ARG A 292      139.87    -35.98
REMARK 500    ASP A 313       -0.51     72.44
REMARK 500    TYR B   6       98.71     75.25
REMARK 500    GLN B  50       63.62   -115.57
REMARK 500    ASP C  13       10.32     80.63
REMARK 500    GLU C  43       -7.51    -45.79
REMARK 500    PHE C  60      -78.72   -121.84
REMARK 500    GLU C  81      -46.57    -29.79
REMARK 500    GLU C  84      167.56    -49.75
REMARK 500    GLU C  86      -75.59    -50.02
REMARK 500    PRO C  95      162.59    -49.25
REMARK 500    THR C 107       34.43   -143.49
REMARK 500    ARG C 148        3.46    -69.04
REMARK 500    ILE C 158       74.41   -101.67
REMARK 500    MLE D   2       79.60   -112.39
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              CA B 401  CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B  30   OD1
REMARK 620 2 SER B  36   O   102.7
REMARK 620 3 GLU B  41   OE1  93.5 103.7
REMARK 620 4 GLU B  41   OE2 140.1 106.9  53.9
REMARK 620 5 SER B  34   OG   97.8  72.6 168.6 116.1
REMARK 620 6 ASP B  32   OD1 101.0 141.3 104.8  71.0  74.3
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              CA B 402  CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU B  73   OE2
REMARK 620 2 ASP B  64   OD1  72.0
REMARK 620 3 ASN B  66   OD1 164.2  92.4
REMARK 620 4 GLU B  68   O   121.0 163.6  74.7
REMARK 620 5 GLU B  73   OE1  56.7 123.6 136.0  72.6
REMARK 620 6 ASP B  62   OD1  99.0  93.2  83.6  75.5 115.1
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              CA B 403  CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B  99   OD1
REMARK 620 2 ASP B 103   OD1  67.0
REMARK 620 3 GLU B 110   OE2 120.4 155.5
REMARK 620 4 GLU B 110   OE1 101.0 149.7  54.8
REMARK 620 5 TYR B 105   O    54.2  72.6 131.5  77.9
REMARK 620 6 ASP B 101   OD1 106.9  62.0  94.0 146.2 134.4
REMARK 620 7 ASP B 101   OD2 153.2 100.6  61.9 100.5 147.4  47.9
REMARK 620 N                    1     2     3     4     5     6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              CA B 404  CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ARG B 146   O
REMARK 620 2 ASP B 140   OD1 100.9
REMARK 620 3 ASP B 144   OD1  78.5  79.2
REMARK 620 4 ASP B 142   OD1 157.3  75.0  78.9
REMARK 620 5 GLU B 151   OE2 127.4 113.9 143.7  73.0
REMARK 620 6 GLU B 151   OE1  76.4 131.9 143.0 123.3  51.1
REMARK 620 N                    1     2     3     4     5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 393
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN D OF CYCLOSPORIN A
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1AUI   RELATED DB: PDB
REMARK 900 HUMAN CALCINEURIN STRUCTURE
REMARK 900 RELATED ID: 1BCK   RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN CYCLOPHILIN A COMPLEXED WITH
REMARK 900 CYCLOSPORIN C
REMARK 900 RELATED ID: 1C5F   RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE CYCLOPHILIN-LIKE DOMAIN FROM
REMARK 900 BRUGIA MALAYI COMPLEXED WITH CYCLOSPORIN A
REMARK 900 RELATED ID: 1CSA   RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURE OF E.COLI CYCLOPHILIN (F112W) COMPLEXED
REMARK 900 WITH CYCLOSPORIN A
REMARK 900 RELATED ID: 1CWA   RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN CYCLOPHILIN A COMPLEXED WITH
REMARK 900 CYCLOSPORIN A
REMARK 900 RELATED ID: 1CWB   RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN CYCLOPHILIN A COMPLEXED WITH
REMARK 900 MODIFIED CYCLOSPORIN A AT POSITION 5
REMARK 900 RELATED ID: 1CWC   RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN CYCLOPHILIN A COMPLEXED WITH
REMARK 900 MODIFIED CYCLOSPORIN A AT POSITION 8
REMARK 900 RELATED ID: 1CWF   RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN CYCLOPHILIN A COMPLEXED WITH
REMARK 900 CYCLOSPORIN D
REMARK 900 RELATED ID: 1CWH   RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN CYCLOPHILIN A COMPLEXED WITH
REMARK 900 CYCLOSPORIN A MODIFIED AT POSITION 7
REMARK 900 RELATED ID: 1CWI   RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN CYCLOPHILIN A COMPLEXED WITH
REMARK 900 MODIFIED CYCLOSPORIN D AT POSITION 7
REMARK 900 RELATED ID: 1CWJ   RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN CYCLOPHILIN A COMPLEXED WITH
REMARK 900 MODIFIED CYCLOSPORIN D AT POSITIONS 5 AND 7.
REMARK 900 RELATED ID: 1CWK   RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN CYCLOPHILIN A COMPLEXED WITH
REMARK 900 MODIFIED CYCLOSPORIN D AT POSITIONS 5 AND 7.
REMARK 900 RELATED ID: 1CWL   RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN CYCLOPHILIN A COMPLEXED WITH
REMARK 900 MODIFIED CYCLOSPORIN A AT POSITION 8
REMARK 900 RELATED ID: 1CWM   RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN CYCLOPHILIN A COMPLEXED WITH
REMARK 900 MODIFIED CYCLOSPORIN A AT POSITION 8
REMARK 900 RELATED ID: 1CWO   RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN CYCLOPHILIN A COMPLEXED WITH
REMARK 900 NODIFIED CYCLOSPORIN C AT POSITIONS 1, AND 9
REMARK 900 RELATED ID: 1CYA   RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURE OF HUMAN CYCLOPHILIN COMPLEXED WIYH
REMARK 900 CYCLOSPORIN A
REMARK 900 RELATED ID: 1CYB   RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURE OF HUMAN CYCLOPHILIN COMPLEXED WITH
REMARK 900 CYCLOSPORIN A
REMARK 900 RELATED ID: 1CYN   RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN CYCLOPHILIN B COMPLEXED WITH
REMARK 900 MODIFIED CYCLOSPORIN A
REMARK 900 RELATED ID: 1IKF   RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF CTCLOSPORIN-FAB COMPLEX
REMARK 900 RELATED ID: 1M63   RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF CALCINEURIN-CYCLOPHILIN-CYCLOSPORIN
REMARK 900 COMPLEX
REMARK 900 RELATED ID: 1MIK   RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN CYCLOPHILIN A COMPLEXED WITH
REMARK 900 MODIFIED CYCLOSPORIN A AT POSITION 6
REMARK 900 RELATED ID: 1QNG   RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF PLASMODIUM FALCIPARUM CYCLOPHILIN
REMARK 900 COMPLEXED WITH CYCLOSPORIN A
REMARK 900 RELATED ID: 1QNH   RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF PLASMODIUM FALCIPARUM CYCLOPHILIN
REMARK 900 (DOUBLE MUTANT) COMPLEXED WITH CYCLOSPORIN A
REMARK 900 RELATED ID: 1XQ7   RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF TRYPANOSOMA CRUZI CYCLOPHILIN
REMARK 900 COMPLEXED WITH CYCLOSPORIN A
REMARK 900 RELATED ID: 2ESL   RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN CYCLOPHILIN C COMPLEXED WITH
REMARK 900 CYCLOSPORIN A
REMARK 900 RELATED ID: 2OJU   RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN CYCLOPHILIN J COMPLEXED WITH
REMARK 900 CYCLOSPORIN A
REMARK 900 RELATED ID: 2POY   RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF CRYPTOSPORIDIUM PARVUM IOWA II
REMARK 900 CYCLOPHILIN A COMPLEXED WITH CYCLOSPORIN A
REMARK 900 RELATED ID: 2RMA   RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN CYCLOPHILIN A COMPLEXED WITH
REMARK 900 CYCLOSPORIN A
REMARK 900 RELATED ID: 2RMB   RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN CYCLOPHILIN A COMPLEXED WITH
REMARK 900 MODIFIED CYCLOSPORIN A AT POSITION 5
REMARK 900 RELATED ID: 2RMC   RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MURINE CYCLOPHILIN C COMPLEXED WITH
REMARK 900 CYCLOSPORIN A
REMARK 900 RELATED ID: 2WFJ   RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE PPIASE DOMAIN OF HUMAN CYCLOPHILIN
REMARK 900 G COMPLEXED WITH CYCLOSPORIN A
REMARK 900 RELATED ID: 2X2C   RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN ACETYL-CYPA COMPLEXED WITH
REMARK 900 CYCLOSPORINE A
REMARK 900 RELATED ID: 2X7K   RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF PPIL1 COMPLEXED WITH CYCLOSPORINE A
REMARK 900 RELATED ID: 2Z6W   RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN CYCLOPHILIN D IN COMPLEX WITH
REMARK 900 CYCLOSPORIN A
REMARK 900 RELATED ID: 3BO7   RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF CYCLOSPHILIN A FROM TOXOPLASMA GONDII
REMARK 900 COMPLEXED WIT CYCLOSPORIN A
REMARK 900 RELATED ID: 3CYS   RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURE OF THE HUMAN CYCLOSPORIN A COMPLEXED
REMARK 900 WITH CYCLOSPORIN A
REMARK 900 RELATED ID: 3EOV   RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF CYCLOPHILIN FROM LEISHMANIA DONOVANI
REMARK 900 COMPLEXED WITH CYCLOSPORIN A
DBREF  1MF8 A   20   392  UNP    Q08209   P2BA_HUMAN      20    392
DBREF  1MF8 B    0   169  UNP    P63098   CANB1_HUMAN      0    169
DBREF  1MF8 C    1   165  UNP    P62937   PPIA_HUMAN       0    164
DBREF  1MF8 D    1    11  NOR    NOR00033 NOR00033         1     11
SEQRES   1 A  373  ALA VAL PRO PHE PRO PRO SER HIS ARG LEU THR ALA LYS
SEQRES   2 A  373  GLU VAL PHE ASP ASN ASP GLY LYS PRO ARG VAL ASP ILE
SEQRES   3 A  373  LEU LYS ALA HIS LEU MET LYS GLU GLY ARG LEU GLU GLU
SEQRES   4 A  373  SER VAL ALA LEU ARG ILE ILE THR GLU GLY ALA SER ILE
SEQRES   5 A  373  LEU ARG GLN GLU LYS ASN LEU LEU ASP ILE ASP ALA PRO
SEQRES   6 A  373  VAL THR VAL CYS GLY ASP ILE HIS GLY GLN PHE PHE ASP
SEQRES   7 A  373  LEU MET LYS LEU PHE GLU VAL GLY GLY SER PRO ALA ASN
SEQRES   8 A  373  THR ARG TYR LEU PHE LEU GLY ASP TYR VAL ASP ARG GLY
SEQRES   9 A  373  TYR PHE SER ILE GLU CYS VAL LEU TYR LEU TRP ALA LEU
SEQRES  10 A  373  LYS ILE LEU TYR PRO LYS THR LEU PHE LEU LEU ARG GLY
SEQRES  11 A  373  ASN HIS GLU CYS ARG HIS LEU THR GLU TYR PHE THR PHE
SEQRES  12 A  373  LYS GLN GLU CYS LYS ILE LYS TYR SER GLU ARG VAL TYR
SEQRES  13 A  373  ASP ALA CYS MET ASP ALA PHE ASP CYS LEU PRO LEU ALA
SEQRES  14 A  373  ALA LEU MET ASN GLN GLN PHE LEU CYS VAL HIS GLY GLY
SEQRES  15 A  373  LEU SER PRO GLU ILE ASN THR LEU ASP ASP ILE ARG LYS
SEQRES  16 A  373  LEU ASP ARG PHE LYS GLU PRO PRO ALA TYR GLY PRO MET
SEQRES  17 A  373  CYS ASP ILE LEU TRP SER ASP PRO LEU GLU ASP PHE GLY
SEQRES  18 A  373  ASN GLU LYS THR GLN GLU HIS PHE THR HIS ASN THR VAL
SEQRES  19 A  373  ARG GLY CYS SER TYR PHE TYR SER TYR PRO ALA VAL CYS
SEQRES  20 A  373  GLU PHE LEU GLN HIS ASN ASN LEU LEU SER ILE LEU ARG
SEQRES  21 A  373  ALA HIS GLU ALA GLN ASP ALA GLY TYR ARG MET TYR ARG
SEQRES  22 A  373  LYS SER GLN THR THR GLY PHE PRO SER LEU ILE THR ILE
SEQRES  23 A  373  PHE SER ALA PRO ASN TYR LEU ASP VAL TYR ASN ASN LYS
SEQRES  24 A  373  ALA ALA VAL LEU LYS TYR GLU ASN ASN VAL MET ASN ILE
SEQRES  25 A  373  ARG GLN PHE ASN CYS SER PRO HIS PRO TYR TRP LEU PRO
SEQRES  26 A  373  ASN PHE MET ASP VAL PHE THR TRP SER LEU PRO PHE VAL
SEQRES  27 A  373  GLY GLU LYS VAL THR GLU MET LEU VAL ASN VAL LEU ASN
SEQRES  28 A  373  ILE CYS SER ASP ASP GLU LEU GLY SER GLU GLU ASP GLY
SEQRES  29 A  373  PHE ASP GLY ALA THR ALA ALA ALA ARG
SEQRES   1 B  170  MET GLY ASN GLU ALA SER TYR PRO LEU GLU MET CYS SER
SEQRES   2 B  170  HIS PHE ASP ALA ASP GLU ILE LYS ARG LEU GLY LYS ARG
SEQRES   3 B  170  PHE LYS LYS LEU ASP LEU ASP ASN SER GLY SER LEU SER
SEQRES   4 B  170  VAL GLU GLU PHE MET SER LEU PRO GLU LEU GLN GLN ASN
SEQRES   5 B  170  PRO LEU VAL GLN ARG VAL ILE ASP ILE PHE ASP THR ASP
SEQRES   6 B  170  GLY ASN GLY GLU VAL ASP PHE LYS GLU PHE ILE GLU GLY
SEQRES   7 B  170  VAL SER GLN PHE SER VAL LYS GLY ASP LYS GLU GLN LYS
SEQRES   8 B  170  LEU ARG PHE ALA PHE ARG ILE TYR ASP MET ASP LYS ASP
SEQRES   9 B  170  GLY TYR ILE SER ASN GLY GLU LEU PHE GLN VAL LEU LYS
SEQRES  10 B  170  MET MET VAL GLY ASN ASN LEU LYS ASP THR GLN LEU GLN
SEQRES  11 B  170  GLN ILE VAL ASP LYS THR ILE ILE ASN ALA ASP LYS ASP
SEQRES  12 B  170  GLY ASP GLY ARG ILE SER PHE GLU GLU PHE CYS ALA VAL
SEQRES  13 B  170  VAL GLY GLY LEU ASP ILE HIS LYS LYS MET VAL VAL ASP
SEQRES  14 B  170  VAL
SEQRES   1 C  165  MET VAL ASN PRO THR VAL PHE PHE ASP ILE ALA VAL ASP
SEQRES   2 C  165  GLY GLU PRO LEU GLY ARG VAL SER PHE GLU LEU PHE ALA
SEQRES   3 C  165  ASP LYS VAL PRO LYS THR ALA GLU ASN PHE ARG ALA LEU
SEQRES   4 C  165  SER THR GLY GLU LYS GLY PHE GLY TYR LYS GLY SER CYS
SEQRES   5 C  165  PHE HIS ARG ILE ILE PRO GLY PHE MET CYS GLN GLY GLY
SEQRES   6 C  165  ASP PHE THR ARG HIS ASN GLY THR GLY GLY LYS SER ILE
SEQRES   7 C  165  TYR GLY GLU LYS PHE GLU ASP GLU ASN PHE ILE LEU LYS
SEQRES   8 C  165  HIS THR GLY PRO GLY ILE LEU SER MET ALA ASN ALA GLY
SEQRES   9 C  165  PRO ASN THR ASN GLY SER GLN PHE PHE ILE CYS THR ALA
SEQRES  10 C  165  LYS THR GLU TRP LEU ASP GLY LYS HIS VAL VAL PHE GLY
SEQRES  11 C  165  LYS VAL LYS GLU GLY MET ASN ILE VAL GLU ALA MET GLU
SEQRES  12 C  165  ARG PHE GLY SER ARG ASN GLY LYS THR SER LYS LYS ILE
SEQRES  13 C  165  THR ILE ALA ASP CYS GLY GLN LEU GLU
SEQRES   1 D   11  DAL MLE MLE MVA BMT ABA SAR MLE VAL MLE ALA
HET    DAL  D   1       5
HET    MLE  D   2       9
HET    MLE  D   3       9
HET    MVA  D   4       8
HET    BMT  D   5      13
HET    ABA  D   6       6
HET    SAR  D   7       5
HET    MLE  D   8       9
HET    MLE  D  10       9
HET     CA  B 401       1
HET     CA  B 402       1
HET     CA  B 403       1
HET     CA  B 404       1
HET    PO4  A 393       5
HETNAM     DAL D-ALANINE
HETNAM     MLE N-METHYLLEUCINE
HETNAM     MVA N-METHYLVALINE
HETNAM     BMT 4-METHYL-4-[(E)-2-BUTENYL]-4,N-METHYL-THREONINE
HETNAM     ABA ALPHA-AMINOBUTYRIC ACID
HETNAM     SAR SARCOSINE
HETNAM      CA CALCIUM ION
HETNAM     PO4 PHOSPHATE ION
FORMUL   4  DAL    C3 H7 N O2
FORMUL   4  MLE    4(C7 H15 N O2)
FORMUL   4  MVA    C6 H13 N O2
FORMUL   4  BMT    C10 H19 N O3
FORMUL   4  ABA    C4 H9 N O2
FORMUL   4  SAR    C3 H7 N O2
FORMUL   5   CA    4(CA 2+)
FORMUL   9  PO4    O4 P 3-
HELIX    1   1 THR A   30  PHE A   35  1                                   6
HELIX    2   2 ARG A   42  MET A   51  1                                  10
HELIX    3   3 GLU A   57  GLU A   75  1                                  19
HELIX    4   4 GLN A   94  GLY A  106  1                                  13
HELIX    5   5 PHE A  125  TYR A  140  1                                  16
HELIX    6   6 CYS A  153  PHE A  160  1                                   8
HELIX    7   7 THR A  161  TYR A  170  1                                  10
HELIX    8   8 SER A  171  ASP A  183  1                                  13
HELIX    9   9 THR A  208  LEU A  215  1                                   8
HELIX   10  10 GLY A  225  SER A  233  1                                   9
HELIX   11  11 SER A  261  ASN A  272  1                                  12
HELIX   12  12 ASN A  310  VAL A  314  5                                   5
HELIX   13  13 LEU A  343  MET A  347  5                                   5
HELIX   14  14 ASP A  348  ASN A  370  1                                  23
HELIX   15  15 ASP B   15  ASP B   30  1                                  16
HELIX   16  16 SER B   38  MET B   43  1                                   6
HELIX   17  17 SER B   44  GLN B   49  5                                   6
HELIX   18  18 LEU B   53  ASP B   62  1                                  10
HELIX   19  19 PHE B   71  SER B   79  1                                   9
HELIX   20  20 GLN B   80  SER B   82  5                                   3
HELIX   21  21 ASP B   86  ASP B   99  1                                  14
HELIX   22  22 SER B  107  GLY B  120  1                                  14
HELIX   23  23 LYS B  124  ASP B  140  1                                  17
HELIX   24  24 PHE B  149  GLY B  157  1                                   9
HELIX   25  25 GLY B  158  LYS B  164  5                                   7
HELIX   26  26 VAL C   29  GLY C   42  1                                  14
HELIX   27  27 THR C  119  LEU C  122  5                                   4
HELIX   28  28 GLY C  135  ARG C  144  1                                  10
SHEET    1  AA 6 LEU A  78  ILE A  81  0
SHEET    2  AA 6 ALA A 188  MET A 191  1  O  ALA A 188   N  LEU A  79
SHEET    3  AA 6 PHE A 195  CYS A 197 -1  O  PHE A 195   N  MET A 191
SHEET    4  AA 6 SER A 276  ARG A 279  1  O  SER A 276   N  LEU A 196
SHEET    5  AA 6 LEU A 302  ILE A 305  1  O  ILE A 303   N  ARG A 279
SHEET    6  AA 6 TYR A 288  MET A 290 -1  O  ARG A 289   N  THR A 304
SHEET    1  AB 4 ARG A 112  PHE A 115  0
SHEET    2  AB 4 VAL A  85  CYS A  88  1  O  THR A  86   N  LEU A 114
SHEET    3  AB 4 ALA A 319  GLU A 325 -1  O  LEU A 322   N  VAL A  87
SHEET    4  AB 4 VAL A 328  PHE A 334 -1  O  VAL A 328   N  GLU A 325
SHEET    1  AC 3 ASP A 234  PRO A 235  0
SHEET    2  AC 3 TYR A 258  TYR A 260  1  O  TYR A 258   N  ASP A 234
SHEET    3  AC 3 THR A 249  HIS A 250 -1  O  THR A 249   N  PHE A 259
SHEET    1  BA 2 SER B  36  LEU B  37  0
SHEET    2  BA 2 VAL B  69  ASP B  70 -1  O  VAL B  69   N  LEU B  37
SHEET    1  BB 2 TYR B 105  ILE B 106  0
SHEET    2  BB 2 ILE B 147  SER B 148 -1  O  ILE B 147   N  ILE B 106
SHEET    1  CA 8 ARG C  55  ILE C  57  0
SHEET    2  CA 8 MET C  61  GLY C  64 -1  O  MET C  61   N  ILE C  57
SHEET    3  CA 8 PHE C 112  CYS C 115 -1  O  PHE C 112   N  GLY C  64
SHEET    4  CA 8 ILE C  97  MET C 100 -1  O  ILE C  97   N  CYS C 115
SHEET    5  CA 8 VAL C 128  GLU C 134 -1  N  PHE C 129   O  LEU C  98
SHEET    6  CA 8 GLU C  15  LEU C  24 -1  O  SER C  21   N  LYS C 133
SHEET    7  CA 8 THR C   5  VAL C  12 -1  O  VAL C   6   N  PHE C  22
SHEET    8  CA 8 ILE C 156  GLN C 163 -1  O  THR C 157   N  ALA C  11
LINK        CA    CA B 401                 OD1 ASP B  30     1555   1555  2.14
LINK        CA    CA B 401                 O   SER B  36     1555   1555  2.65
LINK        CA    CA B 401                 OE1 GLU B  41     1555   1555  2.40
LINK        CA    CA B 401                 OE2 GLU B  41     1555   1555  2.45
LINK        CA    CA B 401                 OG  SER B  34     1555   1555  3.06
LINK        CA    CA B 401                 OD1 ASP B  32     1555   1555  2.16
LINK        CA    CA B 402                 OE2 GLU B  73     1555   1555  2.33
LINK        CA    CA B 402                 OD1 ASP B  64     1555   1555  2.13
LINK        CA    CA B 402                 OD1 ASN B  66     1555   1555  2.43
LINK        CA    CA B 402                 O   GLU B  68     1555   1555  2.37
LINK        CA    CA B 402                 OE1 GLU B  73     1555   1555  2.31
LINK        CA    CA B 402                 OD1 ASP B  62     1555   1555  2.47
LINK        CA    CA B 403                 OD1 ASP B  99     1555   1555  2.33
LINK        CA    CA B 403                 OD1 ASP B 103     1555   1555  2.34
LINK        CA    CA B 403                 OE2 GLU B 110     1555   1555  2.61
LINK        CA    CA B 403                 OE1 GLU B 110     1555   1555  2.10
LINK        CA    CA B 403                 O   TYR B 105     1555   1555  2.72
LINK        CA    CA B 403                 OD1 ASP B 101     1555   1555  2.65
LINK        CA    CA B 403                 OD2 ASP B 101     1555   1555  2.78
LINK        CA    CA B 404                 O   ARG B 146     1555   1555  2.25
LINK        CA    CA B 404                 OD1 ASP B 140     1555   1555  2.38
LINK        CA    CA B 404                 OD1 ASP B 144     1555   1555  1.96
LINK        CA    CA B 404                 OD1 ASP B 142     1555   1555  1.92
LINK        CA    CA B 404                 OE2 GLU B 151     1555   1555  2.56
LINK        CA    CA B 404                 OE1 GLU B 151     1555   1555  2.50
LINK         C   DAL D   1                 N   MLE D   2     1555   1555  1.35
LINK         N   DAL D   1                 C   ALA D  11     1555   1555  1.33
LINK         C   MLE D   2                 N   MLE D   3     1555   1555  1.35
LINK         C   MLE D   3                 N   MVA D   4     1555   1555  1.36
LINK         C   MVA D   4                 N   BMT D   5     1555   1555  1.34
LINK         C   BMT D   5                 N   ABA D   6     1555   1555  1.34
LINK         C   ABA D   6                 N   SAR D   7     1555   1555  1.34
LINK         C   SAR D   7                 N   MLE D   8     1555   1555  1.34
LINK         C   MLE D   8                 N   VAL D   9     1555   1555  1.33
LINK         C   VAL D   9                 N   MLE D  10     1555   1555  1.35
LINK         C   MLE D  10                 N   ALA D  11     1555   1555  1.33
CISPEP   1 ALA A   83    PRO A   84          0         1.30
SITE     1 AC1  5 ASP B  30  ASP B  32  SER B  34  SER B  36
SITE     2 AC1  5 GLU B  41
SITE     1 AC2  5 ASP B  62  ASP B  64  ASN B  66  GLU B  68
SITE     2 AC2  5 GLU B  73
SITE     1 AC3  5 ASP B  99  ASP B 101  ASP B 103  TYR B 105
SITE     2 AC3  5 GLU B 110
SITE     1 AC4  5 ASP B 140  ASP B 142  ASP B 144  ARG B 146
SITE     2 AC4  5 GLU B 151
SITE     1 AC5  2 ARG A 122  TYR A 311
SITE     1 AC6 20 LEU A 312  VAL A 314  TYR A 341  TRP A 342
SITE     2 AC6 20 LEU A 343  PRO A 344  TRP A 352  PHE A 356
SITE     3 AC6 20 ASN B 122  ARG C  55  PHE C  60  GLN C  63
SITE     4 AC6 20 GLY C  72  ALA C 101  ASN C 102  ALA C 103
SITE     5 AC6 20 GLN C 111  PHE C 113  TRP C 121  HIS C 126
CRYST1   64.949  108.334  112.841  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      0.015397  0.000000  0.000000        0.00000
SCALE2      0.000000  0.009231  0.000000        0.00000
SCALE3      0.000000  0.000000  0.008862        0.00000
      
PROCHECK
Go to PROCHECK summary
 References