HEADER CALCIUM-BINDING 25-JUN-98 1BJF
TITLE CRYSTAL STRUCTURE OF RECOMBINANT BOVINE NEUROCALCIN DELTA AT 2.4
TITLE 2 ANGSTROMS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: NEUROCALCIN DELTA;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BOS TAURUS;
SOURCE 3 ORGANISM_COMMON: CATTLE;
SOURCE 4 ORGANISM_TAXID: 9913;
SOURCE 5 STRAIN: DH5-ALPHA;
SOURCE 6 CELLULAR_LOCATION: CYTOPLASM;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PMAL-C
KEYWDS CALCIUM-BINDING, MYRISTOYLATION, NEURONAL SPECIFIC GUANYLATE CYCLASE
KEYWDS 2 ACTIVATOR
EXPDTA X-RAY DIFFRACTION
AUTHOR S.VIJAY-KUMAR,V.D.KUMAR
REVDAT 4 07-FEB-24 1BJF 1 REMARK LINK
REVDAT 3 24-FEB-09 1BJF 1 VERSN
REVDAT 2 30-SEP-03 1BJF 1 DBREF
REVDAT 1 22-JUL-99 1BJF 0
JRNL AUTH S.VIJAY-KUMAR,V.D.KUMAR
JRNL TITL CRYSTAL STRUCTURE OF RECOMBINANT BOVINE NEUROCALCIN.
JRNL REF NAT.STRUCT.BIOL. V. 6 80 1999
JRNL REFN ISSN 1072-8368
JRNL PMID 9886296
JRNL DOI 10.1038/4956
REMARK 2
REMARK 2 RESOLUTION. 2.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.84
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 40.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 10000000.000
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0010
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 84.3
REMARK 3 NUMBER OF REFLECTIONS : 12990
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) : 0.218
REMARK 3 FREE R VALUE : 0.308
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.400
REMARK 3 FREE R VALUE TEST SET COUNT : 1345
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.009
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.40
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.55
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 48.70
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 1111
REMARK 3 BIN R VALUE (WORKING SET) : 0.3780
REMARK 3 BIN FREE R VALUE : 0.3920
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 10.50
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 130
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.034
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2950
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 6
REMARK 3 SOLVENT ATOMS : 44
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 13.00
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 35.10
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.00000
REMARK 3 B22 (A**2) : 0.00000
REMARK 3 B33 (A**2) : 0.00000
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) : 0.39
REMARK 3 ESD FROM SIGMAA (A) : 0.60
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.44
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.59
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.009
REMARK 3 BOND ANGLES (DEGREES) : 1.300
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 21.10
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.270
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 3.050 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 4.440 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 4.740 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 6.930 ; 2.500
REMARK 3
REMARK 3 NCS MODEL : RESTRAINED
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 : PARHCSDX.PRO
REMARK 3 PARAMETER FILE 2 : NULL
REMARK 3 PARAMETER FILE 3 : NULL
REMARK 3 TOPOLOGY FILE 1 : TOPHCSDX.PRO
REMARK 3 TOPOLOGY FILE 2 : NULL
REMARK 3 TOPOLOGY FILE 3 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1BJF COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000171827.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : JUL-97
REMARK 200 TEMPERATURE (KELVIN) : 295
REMARK 200 PH : 6.1
REMARK 200 NUMBER OF CRYSTALS USED : 20
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU RUH2R
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NI FILTER
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IIC
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : R-AXIS
REMARK 200 DATA SCALING SOFTWARE : R-AXIS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 12105
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.400
REMARK 200 RESOLUTION RANGE LOW (A) : NULL
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 84.3
REMARK 200 DATA REDUNDANCY : 2.400
REMARK 200 R MERGE (I) : 0.07300
REMARK 200 R SYM (I) : 0.07300
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.49
REMARK 200 COMPLETENESS FOR SHELL (%) : 54.2
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MIR
REMARK 200 SOFTWARE USED: X-PLOR 3.84
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 45.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.29
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 6.1
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 46.67500
REMARK 290 SMTRY3 2 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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2830 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 18640 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -85.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 MET A 1
REMARK 465 GLY A 2
REMARK 465 LYS A 3
REMARK 465 GLN A 4
REMARK 465 ASP A 186
REMARK 465 PRO A 187
REMARK 465 SER A 188
REMARK 465 SER A 189
REMARK 465 ALA A 190
REMARK 465 GLY A 191
REMARK 465 GLN A 192
REMARK 465 PHE A 193
REMARK 465 MET B 1
REMARK 465 GLY B 2
REMARK 465 LYS B 3
REMARK 465 GLN B 4
REMARK 465 ASP B 186
REMARK 465 PRO B 187
REMARK 465 SER B 188
REMARK 465 SER B 189
REMARK 465 ALA B 190
REMARK 465 GLY B 191
REMARK 465 GLN B 192
REMARK 465 PHE B 193
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 NE ARG A 160 O HOH A 615 2555 0.88
REMARK 500 CA GLY A 78 NH1 ARG B 160 1655 1.16
REMARK 500 CD ARG A 160 O HOH A 615 2555 1.58
REMARK 500 CZ ARG A 160 O HOH A 615 2555 1.79
REMARK 500 C GLY A 78 NH1 ARG B 160 1655 2.17
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 PRO B 139 C - N - CA ANGL. DEV. = 10.3 DEGREES
REMARK 500 ARG B 160 NE - CZ - NH2 ANGL. DEV. = 3.6 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
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 SER A 6 -80.19 41.56
REMARK 500 LYS A 7 102.91 45.38
REMARK 500 PRO A 10 -34.63 -39.26
REMARK 500 THR A 20 -164.39 -120.35
REMARK 500 PHE A 56 68.39 -114.32
REMARK 500 THR A 92 -76.02 -71.53
REMARK 500 ASP A 109 77.82 -66.93
REMARK 500 SER A 134 75.77 -164.49
REMARK 500 ASP A 176 88.76 -150.01
REMARK 500 PRO A 177 8.01 -69.65
REMARK 500 SER B 6 -92.12 -100.29
REMARK 500 LYS B 7 169.87 52.84
REMARK 500 THR B 20 -165.38 -119.06
REMARK 500 PHE B 56 69.47 -114.25
REMARK 500 THR B 92 -75.07 -71.80
REMARK 500 ASP B 109 78.30 -67.67
REMARK 500 SER B 134 74.19 -160.62
REMARK 500 PRO B 139 -0.43 -40.68
REMARK 500 GLU B 140 29.27 43.64
REMARK 500 MET B 156 -158.56 -89.87
REMARK 500 ASP B 176 88.32 -152.15
REMARK 500 PRO B 177 4.94 -67.57
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 A 402 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 73 OD1
REMARK 620 2 ASN A 75 OD1 77.4
REMARK 620 3 ASN A 75 ND2 129.3 52.1
REMARK 620 4 ASP A 77 OD1 79.4 72.5 88.4
REMARK 620 5 THR A 79 O 73.7 136.2 146.1 70.4
REMARK 620 6 GLU A 84 OE1 100.7 138.9 113.8 148.2 79.1
REMARK 620 7 GLU A 84 OE2 101.5 84.2 72.4 156.1 133.2 55.6
REMARK 620 8 HOH A 505 O 160.1 109.3 61.5 84.8 89.7 86.6 97.9
REMARK 620 N 1 2 3 4 5 6 7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 403 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 109 OD1
REMARK 620 2 ASP A 111 OD1 89.9
REMARK 620 3 ASP A 111 OD2 127.5 39.3
REMARK 620 4 ASN A 113 OD1 77.2 75.0 95.5
REMARK 620 5 TYR A 115 O 62.5 146.2 168.1 79.8
REMARK 620 6 GLU A 120 OE2 101.9 83.8 67.8 158.7 119.0
REMARK 620 7 GLU A 120 OE1 92.0 135.1 113.9 148.7 69.2 51.9
REMARK 620 8 HOH A 587 O 157.8 108.0 73.4 94.4 95.9 93.3 84.6
REMARK 620 N 1 2 3 4 5 6 7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 404 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 157 OD1
REMARK 620 2 ASN A 159 OD1 98.6
REMARK 620 3 ASP A 161 OD1 73.8 78.7
REMARK 620 4 LYS A 163 O 87.5 154.6 79.4
REMARK 620 5 GLU A 168 OE1 109.0 116.1 163.6 84.5
REMARK 620 6 GLU A 168 OE2 126.6 66.6 141.2 128.2 50.5
REMARK 620 7 HOH A 513 O 152.5 92.7 84.0 72.3 88.0 80.9
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 406 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 73 OD1
REMARK 620 2 ASN B 75 OD1 78.9
REMARK 620 3 ASN B 75 ND2 132.2 53.9
REMARK 620 4 ASP B 77 OD1 81.6 71.9 89.7
REMARK 620 5 THR B 79 O 74.4 135.2 144.5 69.2
REMARK 620 6 GLU B 84 OE1 102.8 143.8 110.9 144.2 77.8
REMARK 620 7 GLU B 84 OE2 103.9 87.0 69.8 156.9 133.9 57.2
REMARK 620 8 HOH B 506 O 165.4 109.4 58.8 89.5 91.7 77.8 88.7
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 407 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 109 OD1
REMARK 620 2 ASP B 111 OD1 90.3
REMARK 620 3 ASN B 113 OD1 78.5 74.3
REMARK 620 4 TYR B 115 O 64.3 144.7 76.8
REMARK 620 5 GLU B 120 OE2 105.2 82.4 156.4 126.1
REMARK 620 6 GLU B 120 OE1 92.7 135.5 149.5 73.1 54.1
REMARK 620 7 HOH B 616 O 148.7 82.0 70.3 106.7 103.7 113.9
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 408 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 157 OD1
REMARK 620 2 ASN B 159 OD1 102.1
REMARK 620 3 ASP B 161 OD1 72.4 78.4
REMARK 620 4 LYS B 163 O 88.5 151.5 79.8
REMARK 620 5 GLU B 168 OE1 106.8 115.9 165.1 85.3
REMARK 620 6 GLU B 168 OE2 127.3 66.6 142.2 126.7 50.3
REMARK 620 7 HOH B 507 O 166.5 74.7 94.1 88.8 86.2 64.1
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 CA A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 406
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 407
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 408
DBREF 1BJF A 2 193 UNP P61602 NCALD_BOVIN 1 192
DBREF 1BJF B 2 193 UNP P61602 NCALD_BOVIN 1 192
SEQRES 1 A 193 MET GLY LYS GLN ASN SER LYS LEU ARG PRO GLU VAL MET
SEQRES 2 A 193 GLN ASP LEU LEU GLU SER THR ASP PHE THR GLU HIS GLU
SEQRES 3 A 193 ILE GLN GLU TRP TYR LYS GLY PHE LEU ARG ASP CYS PRO
SEQRES 4 A 193 SER GLY HIS LEU SER MET GLU GLU PHE LYS LYS ILE TYR
SEQRES 5 A 193 GLY ASN PHE PHE PRO TYR GLY ASP ALA SER LYS PHE ALA
SEQRES 6 A 193 GLU HIS VAL PHE ARG THR PHE ASP ALA ASN GLY ASP GLY
SEQRES 7 A 193 THR ILE ASP PHE ARG GLU PHE ILE ILE ALA LEU SER VAL
SEQRES 8 A 193 THR SER ARG GLY LYS LEU GLU GLN LYS LEU LYS TRP ALA
SEQRES 9 A 193 PHE SER MET TYR ASP LEU ASP GLY ASN GLY TYR ILE SER
SEQRES 10 A 193 LYS ALA GLU MET LEU GLU ILE VAL GLN ALA ILE TYR LYS
SEQRES 11 A 193 MET VAL SER SER VAL MET LYS MET PRO GLU ASP GLU SER
SEQRES 12 A 193 THR PRO GLU LYS ARG THR GLU LYS ILE PHE ARG GLN MET
SEQRES 13 A 193 ASP THR ASN ARG ASP GLY LYS LEU SER LEU GLU GLU PHE
SEQRES 14 A 193 ILE ARG GLY ALA LYS SER ASP PRO SER ILE VAL ARG LEU
SEQRES 15 A 193 LEU GLN CYS ASP PRO SER SER ALA GLY GLN PHE
SEQRES 1 B 193 MET GLY LYS GLN ASN SER LYS LEU ARG PRO GLU VAL MET
SEQRES 2 B 193 GLN ASP LEU LEU GLU SER THR ASP PHE THR GLU HIS GLU
SEQRES 3 B 193 ILE GLN GLU TRP TYR LYS GLY PHE LEU ARG ASP CYS PRO
SEQRES 4 B 193 SER GLY HIS LEU SER MET GLU GLU PHE LYS LYS ILE TYR
SEQRES 5 B 193 GLY ASN PHE PHE PRO TYR GLY ASP ALA SER LYS PHE ALA
SEQRES 6 B 193 GLU HIS VAL PHE ARG THR PHE ASP ALA ASN GLY ASP GLY
SEQRES 7 B 193 THR ILE ASP PHE ARG GLU PHE ILE ILE ALA LEU SER VAL
SEQRES 8 B 193 THR SER ARG GLY LYS LEU GLU GLN LYS LEU LYS TRP ALA
SEQRES 9 B 193 PHE SER MET TYR ASP LEU ASP GLY ASN GLY TYR ILE SER
SEQRES 10 B 193 LYS ALA GLU MET LEU GLU ILE VAL GLN ALA ILE TYR LYS
SEQRES 11 B 193 MET VAL SER SER VAL MET LYS MET PRO GLU ASP GLU SER
SEQRES 12 B 193 THR PRO GLU LYS ARG THR GLU LYS ILE PHE ARG GLN MET
SEQRES 13 B 193 ASP THR ASN ARG ASP GLY LYS LEU SER LEU GLU GLU PHE
SEQRES 14 B 193 ILE ARG GLY ALA LYS SER ASP PRO SER ILE VAL ARG LEU
SEQRES 15 B 193 LEU GLN CYS ASP PRO SER SER ALA GLY GLN PHE
HET CA A 402 1
HET CA A 403 1
HET CA A 404 1
HET CA B 406 1
HET CA B 407 1
HET CA B 408 1
HETNAM CA CALCIUM ION
FORMUL 3 CA 6(CA 2+)
FORMUL 9 HOH *44(H2 O)
HELIX 1 1 PRO A 10 SER A 19 1 10
HELIX 2 2 GLU A 24 ASP A 37 1 14
HELIX 3 3 MET A 45 ASN A 54 1 10
HELIX 4 4 SER A 62 PHE A 72 1 11
HELIX 5 5 PHE A 82 THR A 92 1 11
HELIX 6 6 LEU A 97 TYR A 108 1 12
HELIX 7 7 LYS A 118 TYR A 129 1 12
HELIX 8 8 GLU A 140 GLU A 142 5 3
HELIX 9 9 PRO A 145 GLN A 155 1 11
HELIX 10 10 LEU A 166 SER A 175 1 10
HELIX 11 11 SER A 178 ARG A 181 1 4
HELIX 12 12 PRO B 10 SER B 19 1 10
HELIX 13 13 GLU B 24 ASP B 37 1 14
HELIX 14 14 MET B 45 ASN B 54 1 10
HELIX 15 15 SER B 62 PHE B 72 1 11
HELIX 16 16 PHE B 82 THR B 92 1 11
HELIX 17 17 LEU B 97 TYR B 108 1 12
HELIX 18 18 LYS B 118 MET B 131 1 14
HELIX 19 19 PRO B 145 GLN B 155 1 11
HELIX 20 20 LEU B 166 SER B 175 1 10
HELIX 21 21 PRO B 177 ARG B 181 5 5
SHEET 1 A 2 HIS A 42 SER A 44 0
SHEET 2 A 2 THR A 79 ASP A 81 -1 N ILE A 80 O LEU A 43
SHEET 1 B 2 HIS B 42 SER B 44 0
SHEET 2 B 2 THR B 79 ASP B 81 -1 N ILE B 80 O LEU B 43
LINK OD1 ASP A 73 CA CA A 402 1555 1555 2.29
LINK OD1 ASN A 75 CA CA A 402 1555 1555 2.00
LINK ND2 ASN A 75 CA CA A 402 1555 1555 2.81
LINK OD1 ASP A 77 CA CA A 402 1555 1555 2.38
LINK O THR A 79 CA CA A 402 1555 1555 2.46
LINK OE1 GLU A 84 CA CA A 402 1555 1555 2.28
LINK OE2 GLU A 84 CA CA A 402 1555 1555 2.40
LINK OD1 ASP A 109 CA CA A 403 1555 1555 2.59
LINK OD1 ASP A 111 CA CA A 403 1555 1555 2.18
LINK OD2 ASP A 111 CA CA A 403 1555 1555 3.39
LINK OD1 ASN A 113 CA CA A 403 1555 1555 2.13
LINK O TYR A 115 CA CA A 403 1555 1555 2.50
LINK OE2 GLU A 120 CA CA A 403 1555 1555 2.41
LINK OE1 GLU A 120 CA CA A 403 1555 1555 2.57
LINK OD1 ASP A 157 CA CA A 404 1555 1555 2.40
LINK OD1 ASN A 159 CA CA A 404 1555 1555 2.26
LINK OD1 ASP A 161 CA CA A 404 1555 1555 2.01
LINK O LYS A 163 CA CA A 404 1555 1555 2.37
LINK OE1 GLU A 168 CA CA A 404 1555 1555 2.29
LINK OE2 GLU A 168 CA CA A 404 1555 1555 2.75
LINK CA CA A 402 O HOH A 505 1555 1555 2.38
LINK CA CA A 403 O HOH A 587 1555 1555 2.49
LINK CA CA A 404 O HOH A 513 1555 1555 2.29
LINK OD1 ASP B 73 CA CA B 406 1555 1555 2.18
LINK OD1 ASN B 75 CA CA B 406 1555 1555 1.96
LINK ND2 ASN B 75 CA CA B 406 1555 1555 2.75
LINK OD1 ASP B 77 CA CA B 406 1555 1555 2.46
LINK O THR B 79 CA CA B 406 1555 1555 2.50
LINK OE1 GLU B 84 CA CA B 406 1555 1555 2.24
LINK OE2 GLU B 84 CA CA B 406 1555 1555 2.35
LINK OD1 ASP B 109 CA CA B 407 1555 1555 2.52
LINK OD1 ASP B 111 CA CA B 407 1555 1555 2.24
LINK OD1 ASN B 113 CA CA B 407 1555 1555 2.21
LINK O TYR B 115 CA CA B 407 1555 1555 2.41
LINK OE2 GLU B 120 CA CA B 407 1555 1555 2.32
LINK OE1 GLU B 120 CA CA B 407 1555 1555 2.46
LINK OD1 ASP B 157 CA CA B 408 1555 1555 2.53
LINK OD1 ASN B 159 CA CA B 408 1555 1555 2.32
LINK OD1 ASP B 161 CA CA B 408 1555 1555 2.12
LINK O LYS B 163 CA CA B 408 1555 1555 2.31
LINK OE1 GLU B 168 CA CA B 408 1555 1555 2.31
LINK OE2 GLU B 168 CA CA B 408 1555 1555 2.76
LINK CA CA B 406 O HOH B 506 1555 1555 2.36
LINK CA CA B 407 O HOH B 616 1555 1555 2.20
LINK CA CA B 408 O HOH B 507 1555 1555 2.40
SITE 1 AC1 6 ASP A 73 ASN A 75 ASP A 77 THR A 79
SITE 2 AC1 6 GLU A 84 HOH A 505
SITE 1 AC2 6 ASP A 109 ASP A 111 ASN A 113 TYR A 115
SITE 2 AC2 6 GLU A 120 HOH A 587
SITE 1 AC3 6 ASP A 157 ASN A 159 ASP A 161 LYS A 163
SITE 2 AC3 6 GLU A 168 HOH A 513
SITE 1 AC4 6 ASP B 73 ASN B 75 ASP B 77 THR B 79
SITE 2 AC4 6 GLU B 84 HOH B 506
SITE 1 AC5 6 ASP B 109 ASP B 111 ASN B 113 TYR B 115
SITE 2 AC5 6 GLU B 120 HOH B 616
SITE 1 AC6 6 ASP B 157 ASN B 159 ASP B 161 LYS B 163
SITE 2 AC6 6 GLU B 168 HOH B 507
CRYST1 42.680 93.350 50.625 90.00 98.29 90.00 P 1 21 1 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 0.023430 0.000000 0.003414 0.00000
SCALE2 0.000000 0.010712 0.000000 0.00000
SCALE3 0.000000 0.000000 0.019962 0.00000
MTRIX1 1 0.473089 -0.846549 0.244009 11.27731 1
MTRIX2 1 -0.851305 -0.510571 -0.120816 21.92868 1
MTRIX3 1 0.226861 -0.150569 -0.962218 9.56027 1
(ATOM LINES ARE NOT SHOWN.)
END
