HEADER METAL BINDING PROTEIN 15-OCT-02 1N0Y
TITLE CRYSTAL STRUCTURE OF PB-BOUND CALMODULIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CALMODULIN;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PARAMECIUM TETRAURELIA;
SOURCE 3 ORGANISM_TAXID: 5888;
SOURCE 4 GENE: CAM;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: JM109;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PKK233-3
KEYWDS CALMODULIN, LEAD, METAL BINDING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR M.A.WILSON,A.T.BRUNGER
REVDAT 6 14-FEB-24 1N0Y 1 REMARK LINK
REVDAT 5 11-OCT-17 1N0Y 1 REMARK
REVDAT 4 13-JUL-11 1N0Y 1 VERSN
REVDAT 3 01-SEP-09 1N0Y 1 REMARK
REVDAT 2 24-FEB-09 1N0Y 1 VERSN
REVDAT 1 30-SEP-03 1N0Y 0
JRNL AUTH M.A.WILSON,A.T.BRUNGER
JRNL TITL DOMAIN FLEXIBILITY IN THE 1.75 A RESOLUTION STRUCTURE OF
JRNL TITL 2 PB2+-CALMODULIN.
JRNL REF ACTA CRYSTALLOGR.,SECT.D V. 59 1782 2003
JRNL REFN ISSN 0907-4449
JRNL PMID 14501118
JRNL DOI 10.1107/S0907444903016846
REMARK 2
REMARK 2 RESOLUTION. 1.75 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.1.24
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.75
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 53.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.2
REMARK 3 NUMBER OF REFLECTIONS : 33157
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) : 0.214
REMARK 3 R VALUE (WORKING SET) : 0.213
REMARK 3 FREE R VALUE : 0.223
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.000
REMARK 3 FREE R VALUE TEST SET COUNT : 3312
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.75
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.80
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2112
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 94.70
REMARK 3 BIN R VALUE (WORKING SET) : 0.2530
REMARK 3 BIN FREE R VALUE SET COUNT : 215
REMARK 3 BIN FREE R VALUE : 0.2440
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1311
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 23
REMARK 3 SOLVENT ATOMS : 149
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 23.80
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 15.27
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.04000
REMARK 3 B22 (A**2) : -0.94000
REMARK 3 B33 (A**2) : 1.45000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.71000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.097
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.091
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.054
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.653
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.906
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.906
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1331 ; 0.007 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 1781 ; 1.219 ; 1.982
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 164 ; 0.755 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 196 ; 0.075 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1011 ; 0.003 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 711 ; 0.272 ; 0.200
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): 105 ; 0.097 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 40 ; 0.295 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 14 ; 0.161 ; 0.200
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 824 ; 0.544 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1313 ; 1.090 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 507 ; 2.331 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 468 ; 3.825 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1N0Y COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 18-OCT-02.
REMARK 100 THE DEPOSITION ID IS D_1000017382.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 03-JUL-00
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRL
REMARK 200 BEAMLINE : BL9-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.946
REMARK 200 MONOCHROMATOR : SINGLE CRYSTAL SI(311) BENT
REMARK 200 MONOCHROMATOR
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 33157
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.750
REMARK 200 RESOLUTION RANGE LOW (A) : 53.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.1
REMARK 200 DATA REDUNDANCY : 5.400
REMARK 200 R MERGE (I) : 0.11000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 14.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.75
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.81
REMARK 200 COMPLETENESS FOR SHELL (%) : 94.7
REMARK 200 DATA REDUNDANCY IN SHELL : 3.20
REMARK 200 R MERGE FOR SHELL (I) : 0.29100
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 4.100
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: SHELXD, SHARP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.49
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.48
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: MPD, SODIUM CACODYLATE, SODIUM
REMARK 280 ACETATE, LEAD NITRATE, PH 5.0, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
REMARK 290 4555 -X+1/2,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 50.46800
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 15.39600
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 50.46800
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 15.39600
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
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 ALA A 88
REMARK 465 PHE A 89
REMARK 465 LYS A 90
REMARK 465 VAL A 91
REMARK 465 PHE A 92
REMARK 465 ASP A 93
REMARK 465 ARG A 94
REMARK 465 ASP A 95
REMARK 465 GLY A 96
REMARK 465 ASN A 97
REMARK 465 GLY A 98
REMARK 465 LEU A 99
REMARK 465 ILE A 100
REMARK 465 SER A 101
REMARK 465 ALA A 102
REMARK 465 ALA A 103
REMARK 465 GLU A 104
REMARK 465 LEU A 105
REMARK 465 ARG A 106
REMARK 465 HIS A 107
REMARK 465 VAL A 108
REMARK 465 MET A 109
REMARK 465 THR A 110
REMARK 465 ASN A 111
REMARK 465 LEU A 112
REMARK 465 GLY A 113
REMARK 465 GLU A 114
REMARK 465 LYS A 115
REMARK 465 LEU A 116
REMARK 465 THR A 117
REMARK 465 ASP A 118
REMARK 465 ASP A 119
REMARK 465 GLU A 120
REMARK 465 VAL A 121
REMARK 465 ASP A 122
REMARK 465 GLU A 123
REMARK 465 MET A 124
REMARK 465 ILE A 125
REMARK 465 ARG A 126
REMARK 465 GLU A 127
REMARK 465 ALA A 128
REMARK 465 ASP A 129
REMARK 465 ILE A 130
REMARK 465 ASP A 131
REMARK 465 GLY A 132
REMARK 465 ASP A 133
REMARK 465 GLY A 134
REMARK 465 HIS A 135
REMARK 465 ILE A 136
REMARK 465 ASN A 137
REMARK 465 TYR A 138
REMARK 465 GLU A 139
REMARK 465 GLU A 140
REMARK 465 PHE A 141
REMARK 465 VAL A 142
REMARK 465 ARG A 143
REMARK 465 MET A 144
REMARK 465 MET A 145
REMARK 465 VAL A 146
REMARK 465 SER A 147
REMARK 465 LYS A 148
REMARK 465 ALA B 1
REMARK 465 GLU B 2
REMARK 465 GLN B 3
REMARK 465 LEU B 4
REMARK 465 THR B 5
REMARK 465 GLU B 6
REMARK 465 GLU B 7
REMARK 465 GLN B 8
REMARK 465 ILE B 9
REMARK 465 ALA B 10
REMARK 465 GLU B 11
REMARK 465 PHE B 12
REMARK 465 LYS B 13
REMARK 465 GLU B 14
REMARK 465 ALA B 15
REMARK 465 PHE B 16
REMARK 465 ALA B 17
REMARK 465 LEU B 18
REMARK 465 PHE B 19
REMARK 465 ASP B 20
REMARK 465 LYS B 21
REMARK 465 ASP B 22
REMARK 465 GLY B 23
REMARK 465 ASP B 24
REMARK 465 GLY B 25
REMARK 465 THR B 26
REMARK 465 ILE B 27
REMARK 465 THR B 28
REMARK 465 THR B 29
REMARK 465 LYS B 30
REMARK 465 GLU B 31
REMARK 465 LEU B 32
REMARK 465 GLY B 33
REMARK 465 THR B 34
REMARK 465 VAL B 35
REMARK 465 MET B 36
REMARK 465 ARG B 37
REMARK 465 SER B 38
REMARK 465 LEU B 39
REMARK 465 GLY B 40
REMARK 465 GLN B 41
REMARK 465 ASN B 42
REMARK 465 PRO B 43
REMARK 465 THR B 44
REMARK 465 GLU B 45
REMARK 465 ALA B 46
REMARK 465 GLU B 47
REMARK 465 LEU B 48
REMARK 465 GLN B 49
REMARK 465 ASP B 50
REMARK 465 MET B 51
REMARK 465 ILE B 52
REMARK 465 ASN B 53
REMARK 465 GLU B 54
REMARK 465 VAL B 55
REMARK 465 ASP B 56
REMARK 465 ALA B 57
REMARK 465 ASP B 58
REMARK 465 GLY B 59
REMARK 465 ASN B 60
REMARK 465 GLY B 61
REMARK 465 THR B 62
REMARK 465 ILE B 63
REMARK 465 ASP B 64
REMARK 465 PHE B 65
REMARK 465 PRO B 66
REMARK 465 GLU B 67
REMARK 465 PHE B 68
REMARK 465 LYS B 148
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 ASN A 42 57.45 -154.80
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 PB A 507 PB
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 2 OE1
REMARK 620 2 GLU A 2 OE2 50.1
REMARK 620 3 CAC A1001 O2 69.2 116.9
REMARK 620 4 HOH A1020 O 76.3 80.4 69.3
REMARK 620 5 GLU B 83 OE1 131.5 151.9 64.7 74.1
REMARK 620 6 GLU B 84 OE2 111.3 64.5 142.6 74.5 96.8
REMARK 620 7 GLU B 123 OE1 105.4 76.5 143.1 146.8 120.3 74.2
REMARK 620 8 GLU B 123 OE2 81.9 88.1 100.0 158.0 119.8 117.2 43.9
REMARK 620 9 GLU B 127 OE2 114.0 149.5 65.6 124.6 58.5 133.9 85.7 62.3
REMARK 620 N 1 2 3 4 5 6 7 8
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 PB B 505 PB
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 2 OE2
REMARK 620 2 HOH A1031 O 88.6
REMARK 620 3 GLU B 84 OE1 67.9 81.7
REMARK 620 4 GLU B 84 OE2 64.4 130.5 50.6
REMARK 620 5 GLU B 87 OE2 145.3 99.7 80.0 85.4
REMARK 620 6 GLU B 87 OE1 130.2 141.1 111.2 77.6 50.5
REMARK 620 7 GLU B 123 OE1 75.8 127.0 133.0 87.4 121.7 71.5
REMARK 620 8 HOH B2052 O 144.1 72.3 135.1 149.8 69.5 73.5 91.6
REMARK 620 N 1 2 3 4 5 6 7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 PB A 502 PB
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 7 OE1
REMARK 620 2 GLU A 7 OE2 51.6
REMARK 620 3 ASP A 58 OD2 80.8 129.7
REMARK 620 4 GLU B 114 OE1 146.7 161.5 66.8
REMARK 620 5 LYS B 115 O 113.8 63.5 146.8 98.2
REMARK 620 6 GLU B 120 OE1 101.4 76.8 135.4 96.4 73.3
REMARK 620 7 GLU B 120 OE2 78.7 96.8 87.5 91.6 123.6 50.5
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 PB A 504 PB
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 11 OE2
REMARK 620 2 GLU A 11 OE1 50.4
REMARK 620 3 GLU A 14 OE1 84.0 72.6
REMARK 620 4 GLU A 14 OE2 97.4 115.1 46.1
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 PB A 503 PB
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 20 OD1
REMARK 620 2 ASP A 22 OD1 70.2
REMARK 620 3 ASP A 24 OD1 75.2 85.5
REMARK 620 4 THR A 26 O 71.6 141.6 80.3
REMARK 620 5 THR A 26 OG1 108.6 131.3 50.0 58.9
REMARK 620 6 GLU A 31 OE1 112.9 129.5 145.1 71.3 96.9
REMARK 620 7 GLU A 31 OE2 95.0 78.8 163.6 109.5 146.3 50.8
REMARK 620 8 HOH A1006 O 153.8 83.6 102.1 134.3 87.5 84.5 80.7
REMARK 620 N 1 2 3 4 5 6 7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 PB A 501 PB
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 56 OD1
REMARK 620 2 ASP A 58 OD2 112.5
REMARK 620 3 ASP A 58 OD1 76.2 44.2
REMARK 620 4 ASN A 60 OD1 74.4 105.1 71.5
REMARK 620 5 THR A 62 O 69.5 176.2 135.3 72.2
REMARK 620 6 ASP A 64 OD2 148.8 54.7 98.8 134.0 125.3
REMARK 620 7 GLU A 67 OE1 86.0 101.9 124.6 151.1 81.3 71.4
REMARK 620 8 GLU A 67 OE2 76.7 64.7 78.3 142.1 119.0 72.2 46.5
REMARK 620 9 HOH A1015 O 138.8 103.4 121.7 77.4 73.6 70.2 106.2 139.5
REMARK 620 N 1 2 3 4 5 6 7 8
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 PB A 500 PB
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 58 OD2
REMARK 620 2 ASP A 64 OD1 115.2
REMARK 620 3 ASP A 64 OD2 76.9 44.0
REMARK 620 4 GLU A 67 OE2 67.2 77.0 79.8
REMARK 620 5 GLU B 114 OE1 83.3 118.2 94.2 150.5
REMARK 620 6 GLU B 114 OE2 130.1 76.5 84.6 153.0 52.0
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CAC A1001 AS
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 PB B 506 PB
REMARK 620 2 CAC A1001 O1 72.0
REMARK 620 3 CAC A1001 O2 41.7 112.6
REMARK 620 4 CAC A1001 C1 116.4 109.3 110.1
REMARK 620 5 CAC A1001 C2 134.3 109.3 109.1 106.3
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 PB B 506 PB
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CAC A1001 O1
REMARK 620 2 CAC A1001 O2 55.6
REMARK 620 3 ASP B 80 OD1 70.2 78.4
REMARK 620 4 GLU B 83 OE1 128.4 77.4 81.5
REMARK 620 5 GLU B 83 OE2 175.5 122.5 105.6 48.0
REMARK 620 6 GLU B 127 OE1 71.1 81.7 141.3 125.7 113.1
REMARK 620 7 GLU B 127 OE2 108.0 77.6 151.1 77.8 74.7 48.8
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 PB B 509 PB
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CAC A1001 O1
REMARK 620 2 ASP B 80 OD1 81.7
REMARK 620 3 ASP B 80 OD2 95.8 46.6
REMARK 620 4 HOH B2041 O 138.1 120.1 80.4
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 PB B 510 PB
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 93 OD1
REMARK 620 2 ASP B 95 OD1 82.4
REMARK 620 3 ASP B 95 OD2 120.8 38.4
REMARK 620 4 ASN B 97 OD1 82.1 75.4 83.9
REMARK 620 5 LEU B 99 O 90.3 155.0 142.4 79.9
REMARK 620 6 GLU B 104 OE1 101.4 129.1 113.7 155.4 75.8
REMARK 620 7 GLU B 104 OE2 98.9 77.3 71.8 152.4 127.6 51.8
REMARK 620 8 HOH B2050 O 168.0 88.4 50.7 88.1 94.9 90.3 86.5
REMARK 620 N 1 2 3 4 5 6 7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 PB B 508 PB
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 129 OD1
REMARK 620 2 ASP B 131 OD1 72.3
REMARK 620 3 ASP B 131 OD2 111.4 43.3
REMARK 620 4 ASP B 133 OD1 76.8 70.3 96.8
REMARK 620 5 HIS B 135 O 75.5 139.9 171.4 79.6
REMARK 620 6 GLU B 140 OE1 108.9 132.0 100.8 157.7 81.1
REMARK 620 7 GLU B 140 OE2 87.7 83.9 68.0 152.8 118.3 49.0
REMARK 620 8 HOH B2027 O 152.9 83.9 53.0 83.1 118.6 96.7 102.9
REMARK 620 N 1 2 3 4 5 6 7
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PB A 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PB A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PB A 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PB A 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PB A 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PB B 505
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PB B 506
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PB A 507
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PB B 508
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PB B 509
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PB B 510
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAC A 1001
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT B 2001
DBREF 1N0Y A 1 148 UNP P07463 CALM_PARTE 1 148
DBREF 1N0Y B 1 148 UNP P07463 CALM_PARTE 1 148
SEQRES 1 A 148 ALA GLU GLN LEU THR GLU GLU GLN ILE ALA GLU PHE LYS
SEQRES 2 A 148 GLU ALA PHE ALA LEU PHE ASP LYS ASP GLY ASP GLY THR
SEQRES 3 A 148 ILE THR THR LYS GLU LEU GLY THR VAL MET ARG SER LEU
SEQRES 4 A 148 GLY GLN ASN PRO THR GLU ALA GLU LEU GLN ASP MET ILE
SEQRES 5 A 148 ASN GLU VAL ASP ALA ASP GLY ASN GLY THR ILE ASP PHE
SEQRES 6 A 148 PRO GLU PHE LEU SER LEU MET ALA ARG LYS MET LYS GLU
SEQRES 7 A 148 GLN ASP SER GLU GLU GLU LEU ILE GLU ALA PHE LYS VAL
SEQRES 8 A 148 PHE ASP ARG ASP GLY ASN GLY LEU ILE SER ALA ALA GLU
SEQRES 9 A 148 LEU ARG HIS VAL MET THR ASN LEU GLY GLU LYS LEU THR
SEQRES 10 A 148 ASP ASP GLU VAL ASP GLU MET ILE ARG GLU ALA ASP ILE
SEQRES 11 A 148 ASP GLY ASP GLY HIS ILE ASN TYR GLU GLU PHE VAL ARG
SEQRES 12 A 148 MET MET VAL SER LYS
SEQRES 1 B 148 ALA GLU GLN LEU THR GLU GLU GLN ILE ALA GLU PHE LYS
SEQRES 2 B 148 GLU ALA PHE ALA LEU PHE ASP LYS ASP GLY ASP GLY THR
SEQRES 3 B 148 ILE THR THR LYS GLU LEU GLY THR VAL MET ARG SER LEU
SEQRES 4 B 148 GLY GLN ASN PRO THR GLU ALA GLU LEU GLN ASP MET ILE
SEQRES 5 B 148 ASN GLU VAL ASP ALA ASP GLY ASN GLY THR ILE ASP PHE
SEQRES 6 B 148 PRO GLU PHE LEU SER LEU MET ALA ARG LYS MET LYS GLU
SEQRES 7 B 148 GLN ASP SER GLU GLU GLU LEU ILE GLU ALA PHE LYS VAL
SEQRES 8 B 148 PHE ASP ARG ASP GLY ASN GLY LEU ILE SER ALA ALA GLU
SEQRES 9 B 148 LEU ARG HIS VAL MET THR ASN LEU GLY GLU LYS LEU THR
SEQRES 10 B 148 ASP ASP GLU VAL ASP GLU MET ILE ARG GLU ALA ASP ILE
SEQRES 11 B 148 ASP GLY ASP GLY HIS ILE ASN TYR GLU GLU PHE VAL ARG
SEQRES 12 B 148 MET MET VAL SER LYS
HET PB A 500 1
HET PB A 501 1
HET PB A 502 1
HET PB A 503 1
HET PB A 504 1
HET PB A 507 1
HET PB A 513 1
HET CAC A1001 5
HET PB B 505 1
HET PB B 506 1
HET PB B 508 1
HET PB B 509 1
HET PB B 510 1
HET PB B 511 1
HET PB B 512 1
HET ACT B2001 4
HETNAM PB LEAD (II) ION
HETNAM CAC CACODYLATE ION
HETNAM ACT ACETATE ION
HETSYN CAC DIMETHYLARSINATE
FORMUL 3 PB 14(PB 2+)
FORMUL 10 CAC C2 H6 AS O2 1-
FORMUL 18 ACT C2 H3 O2 1-
FORMUL 19 HOH *149(H2 O)
HELIX 1 1 THR A 5 ASP A 20 1 16
HELIX 2 2 THR A 28 SER A 38 1 11
HELIX 3 3 THR A 44 ASP A 56 1 13
HELIX 4 4 PHE A 65 GLU A 84 1 20
HELIX 5 5 LEU B 69 ASP B 93 1 25
HELIX 6 6 SER B 101 LEU B 112 1 12
HELIX 7 7 THR B 117 GLU B 127 1 11
HELIX 8 8 TYR B 138 VAL B 146 1 9
SHEET 1 A 2 THR A 26 ILE A 27 0
SHEET 2 A 2 ILE A 63 ASP A 64 -1 O ILE A 63 N ILE A 27
SHEET 1 B 2 LEU B 99 ILE B 100 0
SHEET 2 B 2 ILE B 136 ASN B 137 -1 O ILE B 136 N ILE B 100
LINK OE1 GLU A 2 PB PB A 507 1555 1555 2.47
LINK OE2 GLU A 2 PB PB A 507 1555 1555 2.69
LINK OE2 GLU A 2 PB PB B 505 1555 1555 3.08
LINK OE1 GLU A 7 PB PB A 502 1555 1555 2.64
LINK OE2 GLU A 7 PB PB A 502 1555 1555 2.36
LINK OE2 GLU A 11 PB PB A 504 1555 1555 2.48
LINK OE1 GLU A 11 PB PB A 504 1555 1555 2.66
LINK OE1 GLU A 14 PB PB A 504 1555 1555 2.32
LINK OE2 GLU A 14 PB PB A 504 1555 1555 3.04
LINK OD1 ASP A 20 PB PB A 503 1555 1555 2.30
LINK OD1 ASP A 22 PB PB A 503 1555 1555 2.51
LINK OD1 ASP A 24 PB PB A 503 1555 1555 2.62
LINK O THR A 26 PB PB A 503 1555 1555 2.67
LINK OG1 THR A 26 PB PB A 503 1555 1555 3.49
LINK OE1 GLU A 31 PB PB A 503 1555 1555 2.58
LINK OE2 GLU A 31 PB PB A 503 1555 1555 2.54
LINK OD1 ASP A 56 PB PB A 501 1555 1555 2.25
LINK OD2 ASP A 58 PB PB A 500 1555 1555 2.41
LINK OD2 ASP A 58 PB PB A 501 1555 1555 3.13
LINK OD1 ASP A 58 PB PB A 501 1555 1555 2.45
LINK OD2 ASP A 58 PB PB A 502 1545 1555 3.12
LINK OD1 ASN A 60 PB PB A 501 1555 1555 2.35
LINK O THR A 62 PB PB A 501 1555 1555 2.52
LINK OD1 ASP A 64 PB PB A 500 1555 1555 3.16
LINK OD2 ASP A 64 PB PB A 500 1555 1555 2.37
LINK OD2 ASP A 64 PB PB A 501 1555 1555 3.34
LINK OE2 GLU A 67 PB PB A 500 1555 1555 3.23
LINK OE1 GLU A 67 PB PB A 501 1555 1555 2.75
LINK OE2 GLU A 67 PB PB A 501 1555 1555 2.82
LINK PB PB A 500 OE1 GLU B 114 1555 1555 2.50
LINK PB PB A 500 OE2 GLU B 114 1555 1555 2.51
LINK PB PB A 501 O HOH A1015 1555 1555 3.24
LINK PB PB A 502 OE1 GLU B 114 1555 1545 2.78
LINK PB PB A 502 O LYS B 115 1555 1545 2.87
LINK PB PB A 502 OE1 GLU B 120 1555 1545 2.67
LINK PB PB A 502 OE2 GLU B 120 1555 1545 2.46
LINK PB PB A 503 O HOH A1006 1555 1555 2.60
LINK PB PB A 507 O2 CAC A1001 1555 1555 2.46
LINK PB PB A 507 O HOH A1020 1555 1555 2.91
LINK PB PB A 507 OE1 GLU B 83 1555 1555 3.13
LINK PB PB A 507 OE2 GLU B 84 1555 1555 3.00
LINK PB PB A 507 OE1 GLU B 123 1555 1545 3.04
LINK PB PB A 507 OE2 GLU B 123 1555 1545 2.78
LINK PB PB A 507 OE2 GLU B 127 1555 1545 3.10
LINK PB PB A 507 O HOH B2034 1555 1545 3.45
LINK AS CAC A1001 PB PB B 506 1555 1555 3.44
LINK O1 CAC A1001 PB PB B 506 1555 1555 3.33
LINK O2 CAC A1001 PB PB B 506 1555 1555 2.45
LINK O1 CAC A1001 PB PB B 509 1555 1555 2.38
LINK O HOH A1031 PB PB B 505 1555 1555 2.90
LINK OD1 ASP B 80 PB PB B 506 1555 1555 2.75
LINK OD1 ASP B 80 PB PB B 509 1555 1555 2.97
LINK OD2 ASP B 80 PB PB B 509 1555 1555 2.44
LINK OE1 GLU B 83 PB PB B 506 1555 1555 2.41
LINK OE2 GLU B 83 PB PB B 506 1555 1555 2.88
LINK OE1 GLU B 84 PB PB B 505 1555 1555 2.56
LINK OE2 GLU B 84 PB PB B 505 1555 1555 2.58
LINK OE2 GLU B 87 PB PB B 505 1555 1555 2.47
LINK OE1 GLU B 87 PB PB B 505 1555 1555 2.66
LINK OD1 ASP B 93 PB PB B 510 1555 1555 2.36
LINK OD1 ASP B 95 PB PB B 510 1555 1555 2.35
LINK OD2 ASP B 95 PB PB B 510 1555 1555 3.48
LINK OD1 ASN B 97 PB PB B 510 1555 1555 2.36
LINK O LEU B 99 PB PB B 510 1555 1555 2.28
LINK OE1 GLU B 104 PB PB B 510 1555 1555 2.49
LINK OE2 GLU B 104 PB PB B 510 1555 1555 2.54
LINK OE1 GLU B 123 PB PB B 505 1545 1555 2.69
LINK OE1 GLU B 127 PB PB B 506 1545 1555 2.82
LINK OE2 GLU B 127 PB PB B 506 1545 1555 2.43
LINK OD1 ASP B 129 PB PB B 508 1555 1555 2.37
LINK OD1 ASP B 131 PB PB B 508 1555 1555 2.47
LINK OD2 ASP B 131 PB PB B 508 1555 1555 3.19
LINK OD1 ASP B 133 PB PB B 508 1555 1555 2.25
LINK O HIS B 135 PB PB B 508 1555 1555 2.52
LINK OE1 GLU B 140 PB PB B 508 1555 1555 2.47
LINK OE2 GLU B 140 PB PB B 508 1555 1555 2.78
LINK PB PB B 505 O HOH B2052 1555 1545 2.77
LINK PB PB B 508 O HOH B2027 1555 1555 2.83
LINK PB PB B 509 O HOH B2041 1555 1555 2.68
LINK PB PB B 510 O HOH B2050 1555 1555 2.38
SITE 1 AC1 4 ASP A 58 ASP A 64 GLU A 67 GLU B 114
SITE 1 AC2 6 ASP A 56 ASP A 58 ASN A 60 THR A 62
SITE 2 AC2 6 ASP A 64 GLU A 67
SITE 1 AC3 5 GLU A 7 ASP A 58 GLU B 114 LYS B 115
SITE 2 AC3 5 GLU B 120
SITE 1 AC4 6 ASP A 20 ASP A 22 ASP A 24 THR A 26
SITE 2 AC4 6 GLU A 31 HOH A1006
SITE 1 AC5 2 GLU A 11 GLU A 14
SITE 1 AC6 6 GLU A 2 HOH A1031 GLU B 84 GLU B 87
SITE 2 AC6 6 GLU B 123 HOH B2052
SITE 1 AC7 4 CAC A1001 ASP B 80 GLU B 83 GLU B 127
SITE 1 AC8 7 GLU A 2 CAC A1001 HOH A1020 GLU B 83
SITE 2 AC8 7 GLU B 84 GLU B 123 GLU B 127
SITE 1 AC9 6 ASP B 129 ASP B 131 ASP B 133 HIS B 135
SITE 2 AC9 6 GLU B 140 HOH B2027
SITE 1 BC1 3 CAC A1001 ASP B 80 HOH B2041
SITE 1 BC2 6 ASP B 93 ASP B 95 ASN B 97 LEU B 99
SITE 2 BC2 6 GLU B 104 HOH B2050
SITE 1 BC3 10 ALA A 1 GLU A 2 PB A 507 HOH A1020
SITE 2 BC3 10 HOH A1034 ASP B 80 GLU B 83 GLU B 127
SITE 3 BC3 10 PB B 506 PB B 509
SITE 1 BC4 3 VAL B 108 ASN B 111 LEU B 112
CRYST1 100.936 30.792 113.084 90.00 109.31 90.00 C 1 2 1 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 0.009907 0.000000 0.003471 0.00000
SCALE2 0.000000 0.032476 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009370 0.00000
(ATOM LINES ARE NOT SHOWN.)
END