HEADER HYDROLASE/HYDROLASE REGULATOR 16-MAR-07 2P6B
TITLE CRYSTAL STRUCTURE OF HUMAN CALCINEURIN IN COMPLEX WITH PVIVIT PEPTIDE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PVIVIT 14-MER PEPTIDE;
COMPND 3 CHAIN: E;
COMPND 4 FRAGMENT: RESIDUES 3-16;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: CALMODULIN-DEPENDENT CALCINEURIN A SUBUNIT ALPHA ISOFORM;
COMPND 8 CHAIN: A, C;
COMPND 9 FRAGMENT: RESIDUES 1-381;
COMPND 10 SYNONYM: SERINE/THREONINE-PROTEIN PHOSPHATASE 2B CATALYTIC SUBUNIT
COMPND 11 ALPHA ISOFORM; CAM-PRP CATALYTIC SUBUNIT;
COMPND 12 ENGINEERED: YES;
COMPND 13 MOL_ID: 3;
COMPND 14 MOLECULE: CALCINEURIN SUBUNIT B ISOFORM 1;
COMPND 15 CHAIN: B, D;
COMPND 16 FRAGMENT: RESIDUES 16-170;
COMPND 17 SYNONYM: PROTEIN PHOSPHATASE 2B REGULATORY SUBUNIT 1; PROTEIN
COMPND 18 PHOSPHATASE 3 REGULATORY SUBUNIT B ALPHA ISOFORM 1;
COMPND 19 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 OTHER_DETAILS: SYNTHETIC PEPTIDE;
SOURCE 4 MOL_ID: 2;
SOURCE 5 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 6 ORGANISM_COMMON: HUMAN;
SOURCE 7 ORGANISM_TAXID: 9606;
SOURCE 8 GENE: PPP3CA, CALNA, CNA;
SOURCE 9 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 10 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 11 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 12 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 13 EXPRESSION_SYSTEM_PLASMID: PET15B;
SOURCE 14 MOL_ID: 3;
SOURCE 15 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 16 ORGANISM_COMMON: HUMAN;
SOURCE 17 ORGANISM_TAXID: 9606;
SOURCE 18 GENE: PPP3R1;
SOURCE 19 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 20 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 21 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 22 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 23 EXPRESSION_SYSTEM_PLASMID: PET15B
KEYWDS BETA-SHEET AUGMENTATION; PROTEIN-PEPTIDE COMPLEX, HYDROLASE-HYDROLASE
KEYWDS 2 REGULATOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR H.LI,L.ZHANG,A.RAO,S.C.HARRISON,P.G.HOGAN
REVDAT 6 30-AUG-23 2P6B 1 REMARK SEQADV LINK
REVDAT 5 24-JUL-19 2P6B 1 REMARK LINK
REVDAT 4 18-OCT-17 2P6B 1 REMARK
REVDAT 3 24-FEB-09 2P6B 1 VERSN
REVDAT 2 20-NOV-07 2P6B 1 JRNL
REVDAT 1 05-JUN-07 2P6B 0
JRNL AUTH H.LI,L.ZHANG,A.RAO,S.C.HARRISON,P.G.HOGAN
JRNL TITL STRUCTURE OF CALCINEURIN IN COMPLEX WITH PVIVIT PEPTIDE:
JRNL TITL 2 PORTRAIT OF A LOW-AFFINITY SIGNALLING INTERACTION
JRNL REF J.MOL.BIOL. V. 369 1296 2007
JRNL REFN ISSN 0022-2836
JRNL PMID 17498738
JRNL DOI 10.1016/J.JMB.2007.04.032
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH C.R.KISSINGER,H.E.PARGE,D.R.KNIGHTON,C.T.LEWIS,
REMARK 1 AUTH 2 L.A.PELLETIER,A.TEMPCZYK,V.J.KALISH,K.D.TUCKER,
REMARK 1 AUTH 3 R.E.SHOWALTER,E.W.MOOMAW,L.N.GASTINEL,N.HABUKA,X.CHEN,
REMARK 1 AUTH 4 F.MALDONADO,J.E.BARKER
REMARK 1 TITL CRYSTAL STRUCTURES OF HUMAN CALCINEURIN AND THE HUMAN
REMARK 1 TITL 2 FKBP12-FK506-CALCINEURIN COMPLEX
REMARK 1 REF NATURE V. 378 641 1995
REMARK 1 REFN ISSN 0028-0836
REMARK 1 REFERENCE 2
REMARK 1 AUTH J.P.GRIFFITH,J.L.KIM,E.E.KIM,M.D.SINTCHAK,J.A.THOMSON,
REMARK 1 AUTH 2 M.J.FITZGIBBON,M.A.FLEMING,P.R.CARON,K.HSIAO,M.A.NAVIA
REMARK 1 TITL X-RAY STRUCTURE OF CALCINEURIN INHIBITED BY THE
REMARK 1 TITL 2 IMMUNOPHILIN-IMMUNOSUPPRESSANT FKBP12-FK506 COMPLEX
REMARK 1 REF CELL(CAMBRIDGE,MASS.) V. 82 507 1995
REMARK 1 REFN ISSN 0092-8674
REMARK 1 REFERENCE 3
REMARK 1 AUTH J.ARAMBURU,M.B.YAFFE,C.LOPEZ-RODRIGUEZ,L.C.CANTLEY,
REMARK 1 AUTH 2 P.G.HOGAN,A.RAO
REMARK 1 TITL AFFINITY-DRIVEN PEPTIDE SELECTION OF AN NFAT INHIBITOR MORE
REMARK 1 TITL 2 SELECTIVE THAN CYCLOSPORIN A
REMARK 1 REF SCIENCE V. 285 2129 1999
REMARK 1 REFN ISSN 0036-8075
REMARK 1 REFERENCE 4
REMARK 1 AUTH H.LI,A.RAO,P.G.HOGAN
REMARK 1 TITL STRUCTURAL DELINEATION OF THE CALCINEURIN-NFAT INTERACTION
REMARK 1 TITL 2 AND ITS PARALLELS TO PP1 TARGETING INTERACTIONS
REMARK 1 REF J.MOL.BIOL. V. 342 1659 2004
REMARK 1 REFN ISSN 0022-2836
REMARK 2
REMARK 2 RESOLUTION. 2.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1
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) : 2.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
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) (%) : 93.5
REMARK 3 NUMBER OF REFLECTIONS : 51123
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) : 0.192
REMARK 3 FREE R VALUE : 0.254
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 9.500
REMARK 3 FREE R VALUE TEST SET COUNT : 5173
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) : 2.30
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) : 0.1924
REMARK 3 BIN FREE R VALUE : 0.2543
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 5173
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 : 8283
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 22
REMARK 3 SOLVENT ATOMS : 564
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 37.88
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 2.98500
REMARK 3 B22 (A**2) : -1.67900
REMARK 3 B33 (A**2) : -1.30600
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 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) : NULL
REMARK 3 BOND ANGLES (DEGREES) : NULL
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) : 1.555 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.616 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 2.228 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 3.387 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : 36.06
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 : CNS_TOPPAR:PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : CNS_TOPPAR:WATER_REP.PARAM
REMARK 3 PARAMETER FILE 3 : CNS_TOPPAR:ION.PARAM
REMARK 3 PARAMETER FILE 4 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 2 : NULL
REMARK 3 TOPOLOGY FILE 3 : NULL
REMARK 3 TOPOLOGY FILE 4 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2P6B COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 04-APR-07.
REMARK 100 THE DEPOSITION ID IS D_1000042020.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 24-FEB-06
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 19-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9789
REMARK 200 MONOCHROMATOR : SI 111
REMARK 200 OPTICS : ROSENBAUM-ROCK HIGH-RESOLUTION
REMARK 200 DOUBLE-CRYSTAL MONOCHROMATOR.
REMARK 200 LN2 COOLED FIRST CRYSTAL,
REMARK 200 SAGITTAL FOCUSING 2ND CRYSTAL,
REMARK 200 ROSENBAUM-ROCK VERTICAL FOCUSING
REMARK 200 MIRROR, BEAM DEFINING SLITS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000, DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 60710
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.200
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.2
REMARK 200 DATA REDUNDANCY : 4.700
REMARK 200 R MERGE (I) : 0.10400
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 8.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.28
REMARK 200 COMPLETENESS FOR SHELL (%) : 73.9
REMARK 200 DATA REDUNDANCY IN SHELL : 1.90
REMARK 200 R MERGE FOR SHELL (I) : 0.52900
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 1AUI
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 49.18
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.42
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 12% PEG 4000, 0.1M CALCIUM CHLORIDE,
REMARK 280 0.1M TES, 0.001M DTT, PH 8.0, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 295K
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 43.05200
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 78.84250
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 44.57750
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 78.84250
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 43.05200
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 44.57750
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 300 REMARK: ALTHOUGH THE ASYMMETRIC UNIT CONTAINS TWO CALCINEURIN AB
REMARK 300 HETERODIMERS, THE FUNCTIONAL UNIT IN SOLUTION IS A SINGLE AB
REMARK 300 HETERODIMER
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: PENTAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, 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 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 GLY E 3
REMARK 465 GLY A -2
REMARK 465 SER A -1
REMARK 465 HIS A 0
REMARK 465 MET A 1
REMARK 465 SER A 2
REMARK 465 GLU A 3
REMARK 465 PRO A 4
REMARK 465 LYS A 5
REMARK 465 ALA A 6
REMARK 465 ILE A 7
REMARK 465 ASP A 8
REMARK 465 PRO A 9
REMARK 465 LYS A 10
REMARK 465 LEU A 11
REMARK 465 SER A 12
REMARK 465 THR A 13
REMARK 465 ILE A 371
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 MET B 14
REMARK 465 ILE B 161
REMARK 465 HIS B 162
REMARK 465 LYS B 163
REMARK 465 LYS B 164
REMARK 465 MET B 165
REMARK 465 VAL B 166
REMARK 465 VAL B 167
REMARK 465 ASP B 168
REMARK 465 VAL B 169
REMARK 465 GLY C -2
REMARK 465 SER C -1
REMARK 465 HIS C 0
REMARK 465 MET C 1
REMARK 465 SER C 2
REMARK 465 GLU C 3
REMARK 465 PRO C 4
REMARK 465 LYS C 5
REMARK 465 ALA C 6
REMARK 465 ILE C 7
REMARK 465 ASP C 8
REMARK 465 PRO C 9
REMARK 465 LYS C 10
REMARK 465 LEU C 11
REMARK 465 SER C 12
REMARK 465 THR C 13
REMARK 465 ILE C 371
REMARK 465 CYS C 372
REMARK 465 SER C 373
REMARK 465 ASP C 374
REMARK 465 ASP C 375
REMARK 465 GLU C 376
REMARK 465 LEU C 377
REMARK 465 GLY C 378
REMARK 465 SER C 379
REMARK 465 GLU C 380
REMARK 465 MET D 14
REMARK 465 ASP D 168
REMARK 465 VAL D 169
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 GLU E 16 CG CD OE1 OE2
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 HIS E 14 95.57 -68.24
REMARK 500 ASN A 37 1.26 -69.28
REMARK 500 ASN A 110 26.29 -142.14
REMARK 500 ASP A 121 149.96 81.52
REMARK 500 ARG A 122 -51.88 74.70
REMARK 500 PHE A 160 -122.92 -83.40
REMARK 500 TYR A 170 -117.01 -128.42
REMARK 500 GLN A 193 19.20 59.15
REMARK 500 GLN A 245 14.89 -68.03
REMARK 500 SER A 257 -150.21 64.25
REMARK 500 ALA A 280 -120.26 -128.77
REMARK 500 HIS A 281 -24.58 69.92
REMARK 500 ARG A 292 133.50 -33.76
REMARK 500 ASN A 310 54.97 39.27
REMARK 500 ASP A 313 16.03 59.57
REMARK 500 ALA B 16 -60.77 -139.77
REMARK 500 LEU B 31 -71.90 -50.18
REMARK 500 ASP B 32 1.50 -59.82
REMARK 500 ASP B 62 72.98 -69.49
REMARK 500 LYS B 102 14.96 57.51
REMARK 500 LEU B 159 -87.64 -119.48
REMARK 500 ARG C 16 111.67 -31.87
REMARK 500 ASN C 110 24.24 -143.27
REMARK 500 ASP C 121 153.57 76.21
REMARK 500 ARG C 122 -53.74 72.57
REMARK 500 PHE C 160 -109.07 -84.89
REMARK 500 TYR C 170 -105.27 -132.55
REMARK 500 GLN C 194 -37.12 -137.16
REMARK 500 SER C 257 -156.48 60.27
REMARK 500 ALA C 280 -121.53 -126.51
REMARK 500 HIS C 281 -23.74 72.85
REMARK 500 ARG C 292 135.70 -39.97
REMARK 500 ASN C 326 109.97 -23.54
REMARK 500 ASN D 33 71.64 53.20
REMARK 500 LEU D 48 44.18 -68.24
REMARK 500 GLN D 49 -12.53 -149.31
REMARK 500 PHE D 81 75.96 -103.52
REMARK 500 GLU D 88 -71.59 -50.07
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 FE A 510 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 90 OD2
REMARK 620 2 HIS A 92 NE2 95.7
REMARK 620 3 ASP A 118 OD2 93.4 85.4
REMARK 620 4 PO4 A 511 O1 178.0 82.4 87.1
REMARK 620 5 HOH A 673 O 90.1 84.4 169.4 89.0
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 509 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 118 OD2
REMARK 620 2 ASN A 150 OD1 95.9
REMARK 620 3 HIS A 199 NE2 89.0 84.7
REMARK 620 4 HIS A 281 ND1 168.6 93.7 85.7
REMARK 620 5 PO4 A 511 O2 97.0 82.6 166.5 90.4
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 501 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 30 OD1
REMARK 620 2 ASP B 32 OD1 55.5
REMARK 620 3 ASP B 32 OD2 87.9 43.0
REMARK 620 4 SER B 34 OG 68.9 55.7 91.4
REMARK 620 5 SER B 36 O 52.8 101.9 140.6 73.3
REMARK 620 6 GLU B 41 OE1 53.9 64.5 58.3 113.3 94.1
REMARK 620 7 GLU B 41 OE2 57.5 100.1 100.1 124.4 63.6 42.6
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 502 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 62 OD1
REMARK 620 2 ASP B 64 OD1 89.1
REMARK 620 3 ASP B 64 OD2 122.4 42.7
REMARK 620 4 ASN B 66 OD1 77.3 79.5 111.6
REMARK 620 5 GLU B 68 O 71.2 142.6 165.9 65.5
REMARK 620 6 GLU B 73 OE1 113.6 132.8 92.2 143.5 84.6
REMARK 620 7 GLU B 73 OE2 98.3 91.4 62.8 169.9 122.1 46.6
REMARK 620 8 HOH B 530 O 170.4 90.8 62.4 93.2 103.6 73.1 91.3
REMARK 620 N 1 2 3 4 5 6 7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 503 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 99 OD1
REMARK 620 2 ASP B 101 OD2 131.7
REMARK 620 3 ASP B 101 OD1 93.2 41.3
REMARK 620 4 ASP B 103 OD1 83.8 95.1 75.1
REMARK 620 5 ASP B 103 OD2 121.8 60.9 63.8 40.2
REMARK 620 6 TYR B 105 O 82.4 144.6 152.5 77.5 95.5
REMARK 620 7 GLU B 110 OE1 92.6 108.9 134.7 150.2 142.4 72.8
REMARK 620 8 GLU B 110 OE2 98.3 70.4 87.4 162.4 130.0 120.1 47.3
REMARK 620 9 HOH B 521 O 167.7 60.6 98.8 96.3 62.0 85.5 81.2 85.3
REMARK 620 N 1 2 3 4 5 6 7 8
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 504 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 140 OD1
REMARK 620 2 ASP B 142 OD2 78.3
REMARK 620 3 ASP B 142 OD1 116.9 44.3
REMARK 620 4 ASP B 144 OD1 86.8 78.6 101.7
REMARK 620 5 ARG B 146 O 89.2 148.4 153.2 71.8
REMARK 620 6 GLU B 151 OE2 92.1 96.1 74.2 174.8 113.3
REMARK 620 7 GLU B 151 OE1 117.1 138.2 98.2 136.8 73.2 47.9
REMARK 620 8 HOH B 532 O 163.0 95.7 65.2 76.4 88.0 104.4 77.9
REMARK 620 N 1 2 3 4 5 6 7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FE C 513 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP C 90 OD2
REMARK 620 2 HIS C 92 NE2 91.6
REMARK 620 3 ASP C 118 OD2 88.5 77.9
REMARK 620 4 PO4 C 514 O1 171.2 83.4 83.3
REMARK 620 5 HOH C 603 O 96.1 80.3 157.8 90.2
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN C 512 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP C 118 OD2
REMARK 620 2 ASN C 150 OD1 93.3
REMARK 620 3 HIS C 199 NE2 90.0 85.9
REMARK 620 4 HIS C 281 ND1 170.2 96.1 88.0
REMARK 620 5 PO4 C 514 O2 89.1 75.1 160.9 96.0
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA D 505 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP D 30 OD1
REMARK 620 2 ASP D 32 OD2 102.3
REMARK 620 3 ASP D 32 OD1 75.5 42.5
REMARK 620 4 SER D 34 OG 94.6 97.6 67.7
REMARK 620 5 SER D 36 O 82.9 174.6 139.5 80.6
REMARK 620 6 GLU D 41 OE1 95.7 99.4 134.2 157.7 81.2
REMARK 620 7 GLU D 41 OE2 80.2 64.1 91.2 158.9 118.7 43.1
REMARK 620 8 HOH D 533 O 156.1 53.8 85.1 90.8 121.0 87.7 86.3
REMARK 620 N 1 2 3 4 5 6 7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA D 506 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP D 62 OD1
REMARK 620 2 ASP D 64 OD2 121.6
REMARK 620 3 ASP D 64 OD1 84.3 43.4
REMARK 620 4 ASN D 66 OD1 76.8 110.9 82.3
REMARK 620 5 GLU D 68 O 67.1 169.8 139.4 64.1
REMARK 620 6 GLU D 73 OE2 101.5 68.2 95.7 177.5 117.1
REMARK 620 7 GLU D 73 OE1 112.4 100.5 140.0 135.7 79.5 46.6
REMARK 620 8 HOH D 528 O 164.2 61.1 90.5 87.7 109.1 93.9 80.9
REMARK 620 N 1 2 3 4 5 6 7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA D 507 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP D 99 OD1
REMARK 620 2 ASP D 101 OD1 85.7
REMARK 620 3 ASP D 103 OD1 90.7 78.6
REMARK 620 4 ASP D 103 OD2 121.6 57.6 42.6
REMARK 620 5 TYR D 105 O 61.9 140.1 79.2 119.0
REMARK 620 6 GLU D 110 OE1 84.5 123.8 156.5 152.8 78.3
REMARK 620 7 GLU D 110 OE2 91.2 80.0 158.3 120.4 120.4 45.1
REMARK 620 8 HOH D 523 O 168.0 99.7 100.8 70.0 116.8 83.6 79.4
REMARK 620 N 1 2 3 4 5 6 7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA D 508 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP D 140 OD1
REMARK 620 2 ASP D 142 OD2 70.5
REMARK 620 3 ASP D 144 OD1 73.3 70.8
REMARK 620 4 ARG D 146 O 76.5 138.5 76.1
REMARK 620 5 GLU D 151 OE1 110.3 140.0 149.1 75.1
REMARK 620 6 GLU D 151 OE2 93.6 92.5 161.3 114.4 47.7
REMARK 620 7 HOH D 530 O 159.5 107.2 86.6 95.0 84.8 106.9
REMARK 620 N 1 2 3 4 5 6
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 509
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FE A 510
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 511
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN C 512
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FE C 513
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 C 514
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA D 505
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA D 506
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA D 507
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA D 508
DBREF 2P6B A 1 380 UNP Q08209 PP2BA_HUMAN 1 380
DBREF 2P6B C 1 380 UNP Q08209 PP2BA_HUMAN 1 380
DBREF 2P6B B 15 169 UNP P63098 CANB1_HUMAN 16 170
DBREF 2P6B D 15 169 UNP P63098 CANB1_HUMAN 16 170
DBREF 2P6B E 3 17 PDB 2P6B 2P6B 3 17
SEQADV 2P6B GLY A -2 UNP Q08209 CLONING ARTIFACT
SEQADV 2P6B SER A -1 UNP Q08209 CLONING ARTIFACT
SEQADV 2P6B HIS A 0 UNP Q08209 CLONING ARTIFACT
SEQADV 2P6B GLY C -2 UNP Q08209 CLONING ARTIFACT
SEQADV 2P6B SER C -1 UNP Q08209 CLONING ARTIFACT
SEQADV 2P6B HIS C 0 UNP Q08209 CLONING ARTIFACT
SEQADV 2P6B MET B 14 UNP P63098 INITIATING METHIONINE
SEQADV 2P6B MET D 14 UNP P63098 INITIATING METHIONINE
SEQRES 1 E 15 GLY PRO HIS PRO VAL ILE VAL ILE THR GLY PRO HIS GLU
SEQRES 2 E 15 GLU NH2
SEQRES 1 A 383 GLY SER HIS MET SER GLU PRO LYS ALA ILE ASP PRO LYS
SEQRES 2 A 383 LEU SER THR THR ASP ARG VAL VAL LYS ALA VAL PRO PHE
SEQRES 3 A 383 PRO PRO SER HIS ARG LEU THR ALA LYS GLU VAL PHE ASP
SEQRES 4 A 383 ASN ASP GLY LYS PRO ARG VAL ASP ILE LEU LYS ALA HIS
SEQRES 5 A 383 LEU MET LYS GLU GLY ARG LEU GLU GLU SER VAL ALA LEU
SEQRES 6 A 383 ARG ILE ILE THR GLU GLY ALA SER ILE LEU ARG GLN GLU
SEQRES 7 A 383 LYS ASN LEU LEU ASP ILE ASP ALA PRO VAL THR VAL CYS
SEQRES 8 A 383 GLY ASP ILE HIS GLY GLN PHE PHE ASP LEU MET LYS LEU
SEQRES 9 A 383 PHE GLU VAL GLY GLY SER PRO ALA ASN THR ARG TYR LEU
SEQRES 10 A 383 PHE LEU GLY ASP TYR VAL ASP ARG GLY TYR PHE SER ILE
SEQRES 11 A 383 GLU CYS VAL LEU TYR LEU TRP ALA LEU LYS ILE LEU TYR
SEQRES 12 A 383 PRO LYS THR LEU PHE LEU LEU ARG GLY ASN HIS GLU CYS
SEQRES 13 A 383 ARG HIS LEU THR GLU TYR PHE THR PHE LYS GLN GLU CYS
SEQRES 14 A 383 LYS ILE LYS TYR SER GLU ARG VAL TYR ASP ALA CYS MET
SEQRES 15 A 383 ASP ALA PHE ASP CYS LEU PRO LEU ALA ALA LEU MET ASN
SEQRES 16 A 383 GLN GLN PHE LEU CYS VAL HIS GLY GLY LEU SER PRO GLU
SEQRES 17 A 383 ILE ASN THR LEU ASP ASP ILE ARG LYS LEU ASP ARG PHE
SEQRES 18 A 383 LYS GLU PRO PRO ALA TYR GLY PRO MET CYS ASP ILE LEU
SEQRES 19 A 383 TRP SER ASP PRO LEU GLU ASP PHE GLY ASN GLU LYS THR
SEQRES 20 A 383 GLN GLU HIS PHE THR HIS ASN THR VAL ARG GLY CYS SER
SEQRES 21 A 383 TYR PHE TYR SER TYR PRO ALA VAL CYS GLU PHE LEU GLN
SEQRES 22 A 383 HIS ASN ASN LEU LEU SER ILE LEU ARG ALA HIS GLU ALA
SEQRES 23 A 383 GLN ASP ALA GLY TYR ARG MET TYR ARG LYS SER GLN THR
SEQRES 24 A 383 THR GLY PHE PRO SER LEU ILE THR ILE PHE SER ALA PRO
SEQRES 25 A 383 ASN TYR LEU ASP VAL TYR ASN ASN LYS ALA ALA VAL LEU
SEQRES 26 A 383 LYS TYR GLU ASN ASN VAL MET ASN ILE ARG GLN PHE ASN
SEQRES 27 A 383 CYS SER PRO HIS PRO TYR TRP LEU PRO ASN PHE MET ASP
SEQRES 28 A 383 VAL PHE THR TRP SER LEU PRO PHE VAL GLY GLU LYS VAL
SEQRES 29 A 383 THR GLU MET LEU VAL ASN VAL LEU ASN ILE CYS SER ASP
SEQRES 30 A 383 ASP GLU LEU GLY SER GLU
SEQRES 1 B 156 MET ASP ALA ASP GLU ILE LYS ARG LEU GLY LYS ARG PHE
SEQRES 2 B 156 LYS LYS LEU ASP LEU ASP ASN SER GLY SER LEU SER VAL
SEQRES 3 B 156 GLU GLU PHE MET SER LEU PRO GLU LEU GLN GLN ASN PRO
SEQRES 4 B 156 LEU VAL GLN ARG VAL ILE ASP ILE PHE ASP THR ASP GLY
SEQRES 5 B 156 ASN GLY GLU VAL ASP PHE LYS GLU PHE ILE GLU GLY VAL
SEQRES 6 B 156 SER GLN PHE SER VAL LYS GLY ASP LYS GLU GLN LYS LEU
SEQRES 7 B 156 ARG PHE ALA PHE ARG ILE TYR ASP MET ASP LYS ASP GLY
SEQRES 8 B 156 TYR ILE SER ASN GLY GLU LEU PHE GLN VAL LEU LYS MET
SEQRES 9 B 156 MET VAL GLY ASN ASN LEU LYS ASP THR GLN LEU GLN GLN
SEQRES 10 B 156 ILE VAL ASP LYS THR ILE ILE ASN ALA ASP LYS ASP GLY
SEQRES 11 B 156 ASP GLY ARG ILE SER PHE GLU GLU PHE CYS ALA VAL VAL
SEQRES 12 B 156 GLY GLY LEU ASP ILE HIS LYS LYS MET VAL VAL ASP VAL
SEQRES 1 C 383 GLY SER HIS MET SER GLU PRO LYS ALA ILE ASP PRO LYS
SEQRES 2 C 383 LEU SER THR THR ASP ARG VAL VAL LYS ALA VAL PRO PHE
SEQRES 3 C 383 PRO PRO SER HIS ARG LEU THR ALA LYS GLU VAL PHE ASP
SEQRES 4 C 383 ASN ASP GLY LYS PRO ARG VAL ASP ILE LEU LYS ALA HIS
SEQRES 5 C 383 LEU MET LYS GLU GLY ARG LEU GLU GLU SER VAL ALA LEU
SEQRES 6 C 383 ARG ILE ILE THR GLU GLY ALA SER ILE LEU ARG GLN GLU
SEQRES 7 C 383 LYS ASN LEU LEU ASP ILE ASP ALA PRO VAL THR VAL CYS
SEQRES 8 C 383 GLY ASP ILE HIS GLY GLN PHE PHE ASP LEU MET LYS LEU
SEQRES 9 C 383 PHE GLU VAL GLY GLY SER PRO ALA ASN THR ARG TYR LEU
SEQRES 10 C 383 PHE LEU GLY ASP TYR VAL ASP ARG GLY TYR PHE SER ILE
SEQRES 11 C 383 GLU CYS VAL LEU TYR LEU TRP ALA LEU LYS ILE LEU TYR
SEQRES 12 C 383 PRO LYS THR LEU PHE LEU LEU ARG GLY ASN HIS GLU CYS
SEQRES 13 C 383 ARG HIS LEU THR GLU TYR PHE THR PHE LYS GLN GLU CYS
SEQRES 14 C 383 LYS ILE LYS TYR SER GLU ARG VAL TYR ASP ALA CYS MET
SEQRES 15 C 383 ASP ALA PHE ASP CYS LEU PRO LEU ALA ALA LEU MET ASN
SEQRES 16 C 383 GLN GLN PHE LEU CYS VAL HIS GLY GLY LEU SER PRO GLU
SEQRES 17 C 383 ILE ASN THR LEU ASP ASP ILE ARG LYS LEU ASP ARG PHE
SEQRES 18 C 383 LYS GLU PRO PRO ALA TYR GLY PRO MET CYS ASP ILE LEU
SEQRES 19 C 383 TRP SER ASP PRO LEU GLU ASP PHE GLY ASN GLU LYS THR
SEQRES 20 C 383 GLN GLU HIS PHE THR HIS ASN THR VAL ARG GLY CYS SER
SEQRES 21 C 383 TYR PHE TYR SER TYR PRO ALA VAL CYS GLU PHE LEU GLN
SEQRES 22 C 383 HIS ASN ASN LEU LEU SER ILE LEU ARG ALA HIS GLU ALA
SEQRES 23 C 383 GLN ASP ALA GLY TYR ARG MET TYR ARG LYS SER GLN THR
SEQRES 24 C 383 THR GLY PHE PRO SER LEU ILE THR ILE PHE SER ALA PRO
SEQRES 25 C 383 ASN TYR LEU ASP VAL TYR ASN ASN LYS ALA ALA VAL LEU
SEQRES 26 C 383 LYS TYR GLU ASN ASN VAL MET ASN ILE ARG GLN PHE ASN
SEQRES 27 C 383 CYS SER PRO HIS PRO TYR TRP LEU PRO ASN PHE MET ASP
SEQRES 28 C 383 VAL PHE THR TRP SER LEU PRO PHE VAL GLY GLU LYS VAL
SEQRES 29 C 383 THR GLU MET LEU VAL ASN VAL LEU ASN ILE CYS SER ASP
SEQRES 30 C 383 ASP GLU LEU GLY SER GLU
SEQRES 1 D 156 MET ASP ALA ASP GLU ILE LYS ARG LEU GLY LYS ARG PHE
SEQRES 2 D 156 LYS LYS LEU ASP LEU ASP ASN SER GLY SER LEU SER VAL
SEQRES 3 D 156 GLU GLU PHE MET SER LEU PRO GLU LEU GLN GLN ASN PRO
SEQRES 4 D 156 LEU VAL GLN ARG VAL ILE ASP ILE PHE ASP THR ASP GLY
SEQRES 5 D 156 ASN GLY GLU VAL ASP PHE LYS GLU PHE ILE GLU GLY VAL
SEQRES 6 D 156 SER GLN PHE SER VAL LYS GLY ASP LYS GLU GLN LYS LEU
SEQRES 7 D 156 ARG PHE ALA PHE ARG ILE TYR ASP MET ASP LYS ASP GLY
SEQRES 8 D 156 TYR ILE SER ASN GLY GLU LEU PHE GLN VAL LEU LYS MET
SEQRES 9 D 156 MET VAL GLY ASN ASN LEU LYS ASP THR GLN LEU GLN GLN
SEQRES 10 D 156 ILE VAL ASP LYS THR ILE ILE ASN ALA ASP LYS ASP GLY
SEQRES 11 D 156 ASP GLY ARG ILE SER PHE GLU GLU PHE CYS ALA VAL VAL
SEQRES 12 D 156 GLY GLY LEU ASP ILE HIS LYS LYS MET VAL VAL ASP VAL
HET NH2 E 17 1
HET ZN A 509 1
HET FE A 510 1
HET PO4 A 511 5
HET CA B 501 1
HET CA B 502 1
HET CA B 503 1
HET CA B 504 1
HET ZN C 512 1
HET FE C 513 1
HET PO4 C 514 5
HET CA D 505 1
HET CA D 506 1
HET CA D 507 1
HET CA D 508 1
HETNAM NH2 AMINO GROUP
HETNAM ZN ZINC ION
HETNAM FE FE (III) ION
HETNAM PO4 PHOSPHATE ION
HETNAM CA CALCIUM ION
FORMUL 1 NH2 H2 N
FORMUL 6 ZN 2(ZN 2+)
FORMUL 7 FE 2(FE 3+)
FORMUL 8 PO4 2(O4 P 3-)
FORMUL 9 CA 8(CA 2+)
FORMUL 20 HOH *564(H2 O)
HELIX 1 1 THR A 30 PHE A 35 1 6
HELIX 2 2 ARG A 42 LYS A 52 1 11
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 LEU A 185 1 15
HELIX 9 9 LEU A 209 LYS A 214 1 6
HELIX 10 10 GLY A 225 SER A 233 1 9
HELIX 11 11 SER A 261 ASN A 273 1 13
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 LEU A 369 1 22
HELIX 15 15 ASP B 17 ASP B 30 1 14
HELIX 16 16 SER B 38 MET B 43 1 6
HELIX 17 17 LEU B 53 ASP B 62 1 10
HELIX 18 18 PHE B 71 GLN B 80 1 10
HELIX 19 19 ASP B 86 ASP B 99 1 14
HELIX 20 20 ASN B 108 GLY B 120 1 13
HELIX 21 21 ASN B 121 LEU B 123 5 3
HELIX 22 22 LYS B 124 ASP B 140 1 17
HELIX 23 23 SER B 148 VAL B 156 1 9
HELIX 24 24 THR C 30 PHE C 35 1 6
HELIX 25 25 ARG C 42 MET C 51 1 10
HELIX 26 26 GLU C 57 GLU C 75 1 19
HELIX 27 27 GLN C 94 GLY C 106 1 13
HELIX 28 28 PHE C 125 TYR C 140 1 16
HELIX 29 29 CYS C 153 PHE C 160 1 8
HELIX 30 30 THR C 161 TYR C 170 1 10
HELIX 31 31 SER C 171 ASP C 183 1 13
HELIX 32 32 THR C 208 LEU C 215 1 8
HELIX 33 33 GLY C 225 SER C 233 1 9
HELIX 34 34 SER C 261 ASN C 272 1 12
HELIX 35 35 ASN C 310 VAL C 314 5 5
HELIX 36 36 LEU C 343 MET C 347 5 5
HELIX 37 37 ASP C 348 LEU C 369 1 22
HELIX 38 38 ASP D 15 ASP D 30 1 16
HELIX 39 39 SER D 38 MET D 43 1 6
HELIX 40 40 LEU D 53 ASP D 62 1 10
HELIX 41 41 PHE D 71 GLN D 80 1 10
HELIX 42 42 ASP D 86 ASP D 99 1 14
HELIX 43 43 SER D 107 GLY D 120 1 14
HELIX 44 44 LYS D 124 ASP D 140 1 17
HELIX 45 45 PHE D 149 VAL D 156 1 8
HELIX 46 46 ASP D 160 MET D 165 5 6
SHEET 1 A11 LEU A 144 LEU A 146 0
SHEET 2 A11 TYR A 113 PHE A 115 1 N TYR A 113 O PHE A 145
SHEET 3 A11 VAL A 85 CYS A 88 1 N CYS A 88 O LEU A 114
SHEET 4 A11 ALA A 319 GLU A 325 -1 O LEU A 322 N VAL A 87
SHEET 5 A11 VAL A 328 PHE A 334 -1 O ASN A 330 N LYS A 323
SHEET 6 A11 VAL E 7 THR E 11 1 N VAL E 7 O MET A 329
SHEET 7 A11 VAL C 328 PHE C 334 1 O MET C 329 N ILE E 8
SHEET 8 A11 ALA C 319 GLU C 325 -1 N GLU C 325 O VAL C 328
SHEET 9 A11 VAL C 85 CYS C 88 -1 N VAL C 87 O LEU C 322
SHEET 10 A11 TYR C 113 PHE C 115 1 O LEU C 114 N CYS C 88
SHEET 11 A11 LEU C 144 LEU C 146 1 O PHE C 145 N TYR C 113
SHEET 1 B 6 LEU A 78 ILE A 81 0
SHEET 2 B 6 ALA A 188 MET A 191 1 O LEU A 190 N LEU A 79
SHEET 3 B 6 PHE A 195 CYS A 197 -1 O CYS A 197 N ALA A 189
SHEET 4 B 6 SER A 276 ARG A 279 1 O LEU A 278 N LEU A 196
SHEET 5 B 6 LEU A 302 ILE A 305 1 O ILE A 305 N ARG A 279
SHEET 6 B 6 TYR A 288 MET A 290 -1 N ARG A 289 O THR A 304
SHEET 1 C 3 ASP A 234 PRO A 235 0
SHEET 2 C 3 TYR A 258 TYR A 260 1 O TYR A 260 N ASP A 234
SHEET 3 C 3 PHE A 248 HIS A 250 -1 N THR A 249 O PHE A 259
SHEET 1 D 2 SER B 36 LEU B 37 0
SHEET 2 D 2 VAL B 69 ASP B 70 -1 O VAL B 69 N LEU B 37
SHEET 1 E 2 ILE B 106 SER B 107 0
SHEET 2 E 2 ARG B 146 ILE B 147 -1 O ILE B 147 N ILE B 106
SHEET 1 F 6 LEU C 78 ILE C 81 0
SHEET 2 F 6 ALA C 188 MET C 191 1 O LEU C 190 N LEU C 79
SHEET 3 F 6 PHE C 195 CYS C 197 -1 O CYS C 197 N ALA C 189
SHEET 4 F 6 SER C 276 ARG C 279 1 O LEU C 278 N LEU C 196
SHEET 5 F 6 LEU C 302 ILE C 305 1 O ILE C 305 N ARG C 279
SHEET 6 F 6 TYR C 288 MET C 290 -1 N ARG C 289 O THR C 304
SHEET 1 G 3 ASP C 234 PRO C 235 0
SHEET 2 G 3 TYR C 258 TYR C 260 1 O TYR C 260 N ASP C 234
SHEET 3 G 3 PHE C 248 HIS C 250 -1 N THR C 249 O PHE C 259
SHEET 1 H 2 SER D 36 LEU D 37 0
SHEET 2 H 2 VAL D 69 ASP D 70 -1 O VAL D 69 N LEU D 37
SHEET 1 I 2 TYR D 105 ILE D 106 0
SHEET 2 I 2 ILE D 147 SER D 148 -1 O ILE D 147 N ILE D 106
LINK C GLU E 16 N NH2 E 17 1555 1555 1.25
LINK OD2 ASP A 90 FE FE A 510 1555 1555 2.08
LINK NE2 HIS A 92 FE FE A 510 1555 1555 2.32
LINK OD2 ASP A 118 ZN ZN A 509 1555 1555 2.40
LINK OD2 ASP A 118 FE FE A 510 1555 1555 2.23
LINK OD1 ASN A 150 ZN ZN A 509 1555 1555 2.12
LINK NE2 HIS A 199 ZN ZN A 509 1555 1555 2.22
LINK ND1 HIS A 281 ZN ZN A 509 1555 1555 2.27
LINK ZN ZN A 509 O2 PO4 A 511 1555 1555 2.38
LINK FE FE A 510 O1 PO4 A 511 1555 1555 2.28
LINK FE FE A 510 O HOH A 673 1555 1555 2.37
LINK OD1 ASP B 30 CA CA B 501 1555 1555 3.38
LINK OD1 ASP B 32 CA CA B 501 1555 1555 2.94
LINK OD2 ASP B 32 CA CA B 501 1555 1555 3.06
LINK OG SER B 34 CA CA B 501 1555 1555 2.83
LINK O SER B 36 CA CA B 501 1555 1555 2.93
LINK OE1 GLU B 41 CA CA B 501 1555 1555 3.00
LINK OE2 GLU B 41 CA CA B 501 1555 1555 3.04
LINK OD1 ASP B 62 CA CA B 502 1555 1555 2.64
LINK OD1 ASP B 64 CA CA B 502 1555 1555 2.84
LINK OD2 ASP B 64 CA CA B 502 1555 1555 3.14
LINK OD1 ASN B 66 CA CA B 502 1555 1555 2.75
LINK O GLU B 68 CA CA B 502 1555 1555 2.54
LINK OE1 GLU B 73 CA CA B 502 1555 1555 2.76
LINK OE2 GLU B 73 CA CA B 502 1555 1555 2.83
LINK OD1 ASP B 99 CA CA B 503 1555 1555 2.47
LINK OD2 ASP B 101 CA CA B 503 1555 1555 3.32
LINK OD1 ASP B 101 CA CA B 503 1555 1555 2.70
LINK OD1 ASP B 103 CA CA B 503 1555 1555 2.63
LINK OD2 ASP B 103 CA CA B 503 1555 1555 3.39
LINK O TYR B 105 CA CA B 503 1555 1555 2.52
LINK OE1 GLU B 110 CA CA B 503 1555 1555 2.73
LINK OE2 GLU B 110 CA CA B 503 1555 1555 2.79
LINK OD1 ASP B 140 CA CA B 504 1555 1555 2.56
LINK OD2 ASP B 142 CA CA B 504 1555 1555 2.71
LINK OD1 ASP B 142 CA CA B 504 1555 1555 3.06
LINK OD1 ASP B 144 CA CA B 504 1555 1555 2.84
LINK O ARG B 146 CA CA B 504 1555 1555 2.49
LINK OE2 GLU B 151 CA CA B 504 1555 1555 2.72
LINK OE1 GLU B 151 CA CA B 504 1555 1555 2.68
LINK CA CA B 502 O HOH B 530 1555 1555 2.85
LINK CA CA B 503 O HOH B 521 1555 1555 2.53
LINK CA CA B 504 O HOH B 532 1555 1555 2.77
LINK OD2 ASP C 90 FE FE C 513 1555 1555 2.04
LINK NE2 HIS C 92 FE FE C 513 1555 1555 2.36
LINK OD2 ASP C 118 ZN ZN C 512 1555 1555 2.61
LINK OD2 ASP C 118 FE FE C 513 1555 1555 2.20
LINK OD1 ASN C 150 ZN ZN C 512 1555 1555 2.28
LINK NE2 HIS C 199 ZN ZN C 512 1555 1555 2.21
LINK ND1 HIS C 281 ZN ZN C 512 1555 1555 2.47
LINK ZN ZN C 512 O2 PO4 C 514 1555 1555 2.40
LINK FE FE C 513 O1 PO4 C 514 1555 1555 2.41
LINK FE FE C 513 O HOH C 603 1555 1555 2.36
LINK OD1 ASP D 30 CA CA D 505 1555 1555 2.92
LINK OD2 ASP D 32 CA CA D 505 1555 1555 3.13
LINK OD1 ASP D 32 CA CA D 505 1555 1555 2.91
LINK OG SER D 34 CA CA D 505 1555 1555 2.97
LINK O SER D 36 CA CA D 505 1555 1555 2.72
LINK OE1 GLU D 41 CA CA D 505 1555 1555 2.88
LINK OE2 GLU D 41 CA CA D 505 1555 1555 3.08
LINK OD1 ASP D 62 CA CA D 506 1555 1555 2.79
LINK OD2 ASP D 64 CA CA D 506 1555 1555 3.04
LINK OD1 ASP D 64 CA CA D 506 1555 1555 2.90
LINK OD1 ASN D 66 CA CA D 506 1555 1555 2.74
LINK O GLU D 68 CA CA D 506 1555 1555 2.66
LINK OE2 GLU D 73 CA CA D 506 1555 1555 2.78
LINK OE1 GLU D 73 CA CA D 506 1555 1555 2.79
LINK OD1 ASP D 99 CA CA D 507 1555 1555 2.59
LINK OD1 ASP D 101 CA CA D 507 1555 1555 2.78
LINK OD1 ASP D 103 CA CA D 507 1555 1555 2.92
LINK OD2 ASP D 103 CA CA D 507 1555 1555 3.11
LINK O TYR D 105 CA CA D 507 1555 1555 2.54
LINK OE1 GLU D 110 CA CA D 507 1555 1555 2.67
LINK OE2 GLU D 110 CA CA D 507 1555 1555 3.01
LINK OD1 ASP D 140 CA CA D 508 1555 1555 2.53
LINK OD2 ASP D 142 CA CA D 508 1555 1555 2.73
LINK OD1 ASP D 144 CA CA D 508 1555 1555 2.68
LINK O ARG D 146 CA CA D 508 1555 1555 2.67
LINK OE1 GLU D 151 CA CA D 508 1555 1555 2.66
LINK OE2 GLU D 151 CA CA D 508 1555 1555 2.78
LINK CA CA D 505 O HOH D 533 1555 1555 3.05
LINK CA CA D 506 O HOH D 528 1555 1555 2.86
LINK CA CA D 507 O HOH D 523 1555 1555 2.69
LINK CA CA D 508 O HOH D 530 1555 1555 2.72
CISPEP 1 GLY E 12 PRO E 13 0 0.07
CISPEP 2 ALA A 83 PRO A 84 0 -0.14
CISPEP 3 ALA C 83 PRO C 84 0 -0.17
SITE 1 AC1 6 ASP A 118 ASN A 150 HIS A 199 HIS A 281
SITE 2 AC1 6 FE A 510 PO4 A 511
SITE 1 AC2 6 ASP A 90 HIS A 92 ASP A 118 ZN A 509
SITE 2 AC2 6 PO4 A 511 HOH A 673
SITE 1 AC3 12 HIS A 92 ASP A 118 ARG A 122 ASN A 150
SITE 2 AC3 12 HIS A 151 ARG A 254 HIS A 281 ZN A 509
SITE 3 AC3 12 FE A 510 HOH A 538 HOH A 554 HOH A 615
SITE 1 AC4 6 ASP B 30 ASP B 32 SER B 34 SER B 36
SITE 2 AC4 6 GLU B 41 GLU B 68
SITE 1 AC5 6 ASP B 62 ASP B 64 ASN B 66 GLU B 68
SITE 2 AC5 6 GLU B 73 HOH B 530
SITE 1 AC6 6 ASP B 99 ASP B 101 ASP B 103 TYR B 105
SITE 2 AC6 6 GLU B 110 HOH B 521
SITE 1 AC7 6 ASP B 140 ASP B 142 ASP B 144 ARG B 146
SITE 2 AC7 6 GLU B 151 HOH B 532
SITE 1 AC8 6 ASP C 118 ASN C 150 HIS C 199 HIS C 281
SITE 2 AC8 6 FE C 513 PO4 C 514
SITE 1 AC9 6 ASP C 90 HIS C 92 ASP C 118 ZN C 512
SITE 2 AC9 6 PO4 C 514 HOH C 603
SITE 1 BC1 11 HIS C 92 ASP C 118 ARG C 122 ASN C 150
SITE 2 BC1 11 HIS C 151 ARG C 254 HIS C 281 ZN C 512
SITE 3 BC1 11 FE C 513 HOH C 611 HOH C 623
SITE 1 BC2 6 ASP D 30 ASP D 32 SER D 34 SER D 36
SITE 2 BC2 6 GLU D 41 HOH D 533
SITE 1 BC3 6 ASP D 62 ASP D 64 ASN D 66 GLU D 68
SITE 2 BC3 6 GLU D 73 HOH D 528
SITE 1 BC4 6 ASP D 99 ASP D 101 ASP D 103 TYR D 105
SITE 2 BC4 6 GLU D 110 HOH D 523
SITE 1 BC5 6 ASP D 140 ASP D 142 ASP D 144 ARG D 146
SITE 2 BC5 6 GLU D 151 HOH D 530
CRYST1 86.104 89.155 157.685 90.00 90.00 90.00 P 21 21 21 8
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 0.011614 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011216 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006342 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
