HEADER HYDROLASE(SERINE PROTEASE) 08-DEC-91 2PF2
TITLE THE CA+2 ION AND MEMBRANE BINDING STRUCTURE OF THE GLA DOMAIN OF CA-
TITLE 2 PROTHROMBIN FRAGMENT 1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTHROMBIN FRAGMENT 1;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BOS TAURUS;
SOURCE 3 ORGANISM_COMMON: CATTLE;
SOURCE 4 ORGANISM_TAXID: 9913
KEYWDS HYDROLASE(SERINE PROTEASE)
EXPDTA X-RAY DIFFRACTION
AUTHOR M.SORIANO-GARCIA,K.PADMANABHAN,A.M.DE VOS,A.TULINSKY
REVDAT 5 29-NOV-17 2PF2 1 HELIX
REVDAT 4 06-JUL-11 2PF2 1 AUTHOR
REVDAT 3 24-FEB-09 2PF2 1 VERSN
REVDAT 2 01-APR-03 2PF2 1 JRNL
REVDAT 1 31-JAN-94 2PF2 0
JRNL AUTH M.SORIANO-GARCIA,K.PADMANABHAN,A.M.DE VOS,A.TULINSKY
JRNL TITL THE CA2+ ION AND MEMBRANE BINDING STRUCTURE OF THE GLA
JRNL TITL 2 DOMAIN OF CA-PROTHROMBIN FRAGMENT 1.
JRNL REF BIOCHEMISTRY V. 31 2554 1992
JRNL REFN ISSN 0006-2960
JRNL PMID 1547238
JRNL DOI 10.1021/BI00124A016
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH T.P.SESHADRI,A.TULINSKY,E.SKRZYPCZAK-JANKUN,C.H.PARK
REMARK 1 TITL STRUCTURE OF BOVINE PROTHROMBIN FRAGMENT 1 REFINED AT 2.25
REMARK 1 TITL 2 ANGSTROMS RESOLUTION
REMARK 1 REF J.MOL.BIOL. V. 220 481 1991
REMARK 1 REFN ISSN 0022-2836
REMARK 1 REFERENCE 2
REMARK 1 AUTH M.SORIANO-GARCIA,C.H.PARK,A.TULINSKY,K.G.RAVICHANDRAN,
REMARK 1 AUTH 2 E.SKRZYPCZAK-JANKUN
REMARK 1 TITL STRUCTURE OF CA2+ PROTHROMBIN FRAGMENT 1 INCLUDING THE
REMARK 1 TITL 2 CONFORMATION OF THE GLA DOMAIN
REMARK 1 REF BIOCHEMISTRY V. 28 6805 1989
REMARK 1 REFN ISSN 0006-2960
REMARK 2
REMARK 2 RESOLUTION. 2.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PROFFT
REMARK 3 AUTHORS : KONNERT,HENDRICKSON,FINZEL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 7.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 1.000
REMARK 3 COMPLETENESS FOR RANGE (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : NULL
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING + TEST SET) : 0.171
REMARK 3 R VALUE (WORKING SET) : NULL
REMARK 3 FREE R VALUE : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : NULL
REMARK 3
REMARK 3 FIT/AGREEMENT OF MODEL WITH ALL DATA.
REMARK 3 R VALUE (WORKING + TEST SET, NO CUTOFF) : NULL
REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : NULL
REMARK 3 FREE R VALUE (NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : NULL
REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1166
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 7
REMARK 3 SOLVENT ATOMS : 144
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 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 DISTANCE RESTRAINTS. RMS SIGMA
REMARK 3 BOND LENGTH (A) : 0.017 ; 0.020
REMARK 3 ANGLE DISTANCE (A) : 0.055 ; 0.040
REMARK 3 INTRAPLANAR 1-4 DISTANCE (A) : 0.060 ; 0.050
REMARK 3 H-BOND OR METAL COORDINATION (A) : NULL ; NULL
REMARK 3
REMARK 3 PLANE RESTRAINT (A) : 0.022 ; 0.030
REMARK 3 CHIRAL-CENTER RESTRAINT (A**3) : 0.187 ; 0.150
REMARK 3
REMARK 3 NON-BONDED CONTACT RESTRAINTS.
REMARK 3 SINGLE TORSION (A) : 0.240 ; 0.600
REMARK 3 MULTIPLE TORSION (A) : 0.330 ; 0.600
REMARK 3 H-BOND (X...Y) (A) : NULL ; NULL
REMARK 3 H-BOND (X-H...Y) (A) : 0.340 ; 0.600
REMARK 3
REMARK 3 CONFORMATIONAL TORSION ANGLE RESTRAINTS.
REMARK 3 SPECIFIED (DEGREES) : NULL ; NULL
REMARK 3 PLANAR (DEGREES) : 3.100 ; 3.000
REMARK 3 STAGGERED (DEGREES) : 26.000; 15.000
REMARK 3 TRANSVERSE (DEGREES) : NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 1.100 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 1.800 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 1.700 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 2.500 ; 2.500
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2PF2 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_1000178459.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : NULL
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : NULL
REMARK 200 RADIATION SOURCE : NULL
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : NULL
REMARK 200 WAVELENGTH OR RANGE (A) : NULL
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : NULL
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : NULL
REMARK 200 RESOLUTION RANGE HIGH (A) : NULL
REMARK 200 RESOLUTION RANGE LOW (A) : NULL
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : NULL
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
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) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
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: NULL
REMARK 200 SOFTWARE USED: X-PLOR
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 67.75
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.81
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
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 19.69500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 64.82000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 26.94000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 64.82000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 19.69500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 26.94000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 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 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 ASP A 147
REMARK 465 ARG A 148
REMARK 465 VAL A 149
REMARK 465 THR A 150
REMARK 465 VAL A 151
REMARK 465 GLU A 152
REMARK 465 VAL A 153
REMARK 465 ILE A 154
REMARK 465 PRO A 155
REMARK 465 ARG A 156
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 GLN A 146 CA C O CB CG CD OE1
REMARK 470 GLN A 146 NE2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 OG1 THR A 129 O LEU A 134 1.97
REMARK 500 OD1 ASN A 117 N GLY A 120 2.03
REMARK 500 OE21 CGU A 15 NH2 ARG A 55 2.16
REMARK 500 NH2 ARG A 25 OD1 ASP A 39 2.17
REMARK 500 O TYR A 74 O HOH A 242 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 ARG A 10 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 LEU A 14 CB - CA - C ANGL. DEV. = 11.8 DEGREES
REMARK 500 ARG A 16 NE - CZ - NH2 ANGL. DEV. = 4.3 DEGREES
REMARK 500 CGU A 21 O - C - N ANGL. DEV. = 12.2 DEGREES
REMARK 500 CYS A 23 CA - CB - SG ANGL. DEV. = 12.2 DEGREES
REMARK 500 ARG A 25 CD - NE - CZ ANGL. DEV. = 10.5 DEGREES
REMARK 500 ARG A 52 CD - NE - CZ ANGL. DEV. = 9.5 DEGREES
REMARK 500 ARG A 52 NE - CZ - NH1 ANGL. DEV. = 4.7 DEGREES
REMARK 500 VAL A 70 CB - CA - C ANGL. DEV. = 15.2 DEGREES
REMARK 500 VAL A 70 CA - CB - CG1 ANGL. DEV. = 12.0 DEGREES
REMARK 500 ARG A 75 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 SER A 79 N - CA - CB ANGL. DEV. = -13.6 DEGREES
REMARK 500 ARG A 82 NE - CZ - NH2 ANGL. DEV. = -3.4 DEGREES
REMARK 500 CYS A 87 CA - CB - SG ANGL. DEV. = 11.1 DEGREES
REMARK 500 GLN A 88 CG - CD - OE1 ANGL. DEV. = 13.1 DEGREES
REMARK 500 ARG A 93 CA - CB - CG ANGL. DEV. = 18.2 DEGREES
REMARK 500 TYR A 94 CB - CG - CD2 ANGL. DEV. = 4.7 DEGREES
REMARK 500 TYR A 94 CB - CG - CD1 ANGL. DEV. = -3.9 DEGREES
REMARK 500 ALA A 108 CB - CA - C ANGL. DEV. = 11.6 DEGREES
REMARK 500 ARG A 111 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 ARG A 116 NE - CZ - NH2 ANGL. DEV. = 3.2 DEGREES
REMARK 500 TYR A 128 CB - CG - CD1 ANGL. DEV. = -3.6 DEGREES
REMARK 500 ARG A 135 NE - CZ - NH2 ANGL. DEV. = 3.0 DEGREES
REMARK 500 ARG A 136 NE - CZ - NH2 ANGL. DEV. = 3.0 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 ASN A 2 71.99 72.27
REMARK 500 LYS A 3 35.37 -152.82
REMARK 500 PHE A 5 95.18 -172.93
REMARK 500 LEU A 6 38.35 71.86
REMARK 500 CGU A 33 -105.56 90.13
REMARK 500 SER A 34 126.64 -31.06
REMARK 500 PHE A 41 -73.52 -62.32
REMARK 500 TRP A 42 -33.11 -38.06
REMARK 500 PRO A 54 177.91 -59.55
REMARK 500 ASN A 77 36.72 -97.94
REMARK 500 THR A 81 -175.18 -62.69
REMARK 500 ASP A 109 72.19 -119.40
REMARK 500 GLU A 112 -132.29 41.49
REMARK 500 ARG A 116 -62.87 -140.84
REMARK 500 ASN A 117 74.40 79.29
REMARK 500 GLU A 137 140.17 -170.70
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 ASN A 13 -10.05
REMARK 500 VAL A 70 -10.26
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 174 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CGU A 17 OE21
REMARK 620 2 ASN A 2 N 79.9
REMARK 620 3 ASN A 2 OD1 139.0 59.4
REMARK 620 4 CGU A 7 OE11 68.6 69.1 98.8
REMARK 620 5 CGU A 8 OE21 136.9 111.4 70.0 77.0
REMARK 620 6 CGU A 27 OE11 122.6 128.1 83.4 158.7 84.1
REMARK 620 7 CGU A 17 OE11 73.1 150.0 147.5 88.9 81.3 78.7
REMARK 620 8 CGU A 27 OE22 81.7 72.7 81.5 134.7 141.2 66.6 114.9
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 171 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CGU A 26 OE21
REMARK 620 2 CGU A 30 OE21 76.8
REMARK 620 3 CGU A 26 OE12 63.6 89.6
REMARK 620 4 CGU A 30 OE11 133.3 65.3 89.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 172 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A 266 O
REMARK 620 2 CGU A 8 OE12 79.7
REMARK 620 3 CGU A 27 OE12 67.2 73.2
REMARK 620 4 CGU A 8 OE22 152.9 75.0 96.0
REMARK 620 5 CGU A 30 OE21 92.4 168.9 110.9 114.0
REMARK 620 6 CGU A 30 OE22 120.2 137.3 80.6 74.9 53.6
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 173 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CGU A 27 OE11
REMARK 620 2 CGU A 30 OE22 71.9
REMARK 620 3 HOH A 231 O 126.2 144.3
REMARK 620 4 HOH A 273 O 150.3 80.0 73.5
REMARK 620 5 CGU A 17 OE11 88.7 159.1 54.8 120.3
REMARK 620 6 CGU A 17 OE12 92.9 125.1 87.3 111.6 46.1
REMARK 620 7 CGU A 8 OE22 80.0 76.0 77.8 83.9 109.1 154.7
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 175 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CGU A 7 OE11
REMARK 620 2 CGU A 7 OE12 51.6
REMARK 620 3 CGU A 21 OE22 170.8 134.3
REMARK 620 4 HOH A 224 O 125.9 75.4 61.9
REMARK 620 5 ALA A 1 N 110.7 104.4 62.4 90.3
REMARK 620 6 CGU A 17 OE21 66.8 105.6 104.0 150.7 60.7
REMARK 620 7 CGU A 17 OE22 83.4 134.9 90.5 147.8 90.8 46.5
REMARK 620 8 HOH A 239 O 100.2 93.8 86.9 70.2 149.1 137.7 93.6
REMARK 620 9 ASN A 2 N 73.6 52.4 104.3 83.2 52.4 75.4 121.9 142.0
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 A 176 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CGU A 21 OE21
REMARK 620 2 CGU A 20 OE12 75.7
REMARK 620 3 CGU A 21 OE12 93.0 120.5
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 177 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CGU A 20 OE22
REMARK 620 2 CGU A 15 OE22 75.0
REMARK 620 3 CGU A 20 OE21 49.2 88.3
REMARK 620 N 1 2
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 171
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 172
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 173
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 174
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 175
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 176
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 177
DBREF 2PF2 A 1 156 UNP P00735 THRB_BOVIN 44 199
SEQADV 2PF2 CGU A 7 UNP P00735 GLU 50 CONFLICT
SEQADV 2PF2 CGU A 8 UNP P00735 GLU 51 CONFLICT
SEQADV 2PF2 CGU A 15 UNP P00735 GLU 58 CONFLICT
SEQADV 2PF2 CGU A 17 UNP P00735 GLU 60 CONFLICT
SEQADV 2PF2 CGU A 20 UNP P00735 GLU 63 CONFLICT
SEQADV 2PF2 CGU A 21 UNP P00735 GLU 64 CONFLICT
SEQADV 2PF2 CGU A 26 UNP P00735 GLU 69 CONFLICT
SEQADV 2PF2 CGU A 27 UNP P00735 GLU 70 CONFLICT
SEQADV 2PF2 CGU A 30 UNP P00735 GLU 73 CONFLICT
SEQADV 2PF2 CGU A 33 UNP P00735 GLU 76 CONFLICT
SEQRES 1 A 156 ALA ASN LYS GLY PHE LEU CGU CGU VAL ARG LYS GLY ASN
SEQRES 2 A 156 LEU CGU ARG CGU CYS LEU CGU CGU PRO CYS SER ARG CGU
SEQRES 3 A 156 CGU ALA PHE CGU ALA LEU CGU SER LEU SER ALA THR ASP
SEQRES 4 A 156 ALA PHE TRP ALA LYS TYR THR ALA CYS GLU SER ALA ARG
SEQRES 5 A 156 ASN PRO ARG GLU LYS LEU ASN GLU CYS LEU GLU GLY ASN
SEQRES 6 A 156 CYS ALA GLU GLY VAL GLY MET ASN TYR ARG GLY ASN VAL
SEQRES 7 A 156 SER VAL THR ARG SER GLY ILE GLU CYS GLN LEU TRP ARG
SEQRES 8 A 156 SER ARG TYR PRO HIS LYS PRO GLU ILE ASN SER THR THR
SEQRES 9 A 156 HIS PRO GLY ALA ASP LEU ARG GLU ASN PHE CYS ARG ASN
SEQRES 10 A 156 PRO ASP GLY SER ILE THR GLY PRO TRP CYS TYR THR THR
SEQRES 11 A 156 SER PRO THR LEU ARG ARG GLU GLU CYS SER VAL PRO VAL
SEQRES 12 A 156 CYS GLY GLN ASP ARG VAL THR VAL GLU VAL ILE PRO ARG
MODRES 2PF2 CGU A 7 GLU GAMMA-CARBOXY-GLUTAMIC ACID
MODRES 2PF2 CGU A 8 GLU GAMMA-CARBOXY-GLUTAMIC ACID
MODRES 2PF2 CGU A 15 GLU GAMMA-CARBOXY-GLUTAMIC ACID
MODRES 2PF2 CGU A 17 GLU GAMMA-CARBOXY-GLUTAMIC ACID
MODRES 2PF2 CGU A 20 GLU GAMMA-CARBOXY-GLUTAMIC ACID
MODRES 2PF2 CGU A 21 GLU GAMMA-CARBOXY-GLUTAMIC ACID
MODRES 2PF2 CGU A 26 GLU GAMMA-CARBOXY-GLUTAMIC ACID
MODRES 2PF2 CGU A 27 GLU GAMMA-CARBOXY-GLUTAMIC ACID
MODRES 2PF2 CGU A 30 GLU GAMMA-CARBOXY-GLUTAMIC ACID
MODRES 2PF2 CGU A 33 GLU GAMMA-CARBOXY-GLUTAMIC ACID
HET CGU A 7 12
HET CGU A 8 12
HET CGU A 15 12
HET CGU A 17 12
HET CGU A 20 12
HET CGU A 21 12
HET CGU A 26 12
HET CGU A 27 12
HET CGU A 30 12
HET CGU A 33 12
HET CA A 171 1
HET CA A 172 1
HET CA A 173 1
HET CA A 174 1
HET CA A 175 1
HET CA A 176 1
HET CA A 177 1
HETNAM CGU GAMMA-CARBOXY-GLUTAMIC ACID
HETNAM CA CALCIUM ION
FORMUL 1 CGU 10(C6 H9 N O6)
FORMUL 2 CA 7(CA 2+)
FORMUL 9 HOH *144(H2 O)
HELIX 1 A1 LEU A 14 CGU A 17 1 4
HELIX 2 A2 ARG A 25 ALA A 31 1 7
HELIX 3 A3 SER A 36 ALA A 47 1 12
HELIX 4 A4 ARG A 55 LEU A 62 1 8
SHEET 1 S1 2 SER A 79 THR A 81 0
SHEET 2 S1 2 ILE A 85 CYS A 87 -1
SHEET 1 S2 2 GLN A 88 TRP A 90 0
SHEET 2 S2 2 ARG A 111 ASN A 113 -1
SHEET 1 S3 2 CYS A 127 THR A 129 0
SHEET 2 S3 2 ARG A 136 GLU A 138 -1
SSBOND 1 CYS A 18 CYS A 23 1555 1555 2.03
SSBOND 2 CYS A 48 CYS A 61 1555 1555 1.96
SSBOND 3 CYS A 66 CYS A 144 1555 1555 2.05
SSBOND 4 CYS A 87 CYS A 127 1555 1555 2.02
SSBOND 5 CYS A 115 CYS A 139 1555 1555 2.04
LINK C LEU A 6 N CGU A 7 1555 1555 1.32
LINK C CGU A 7 N CGU A 8 1555 1555 1.29
LINK C CGU A 8 N VAL A 9 1555 1555 1.30
LINK C LEU A 14 N CGU A 15 1555 1555 1.30
LINK C CGU A 15 N ARG A 16 1555 1555 1.33
LINK C ARG A 16 N CGU A 17 1555 1555 1.32
LINK C CGU A 17 N CYS A 18 1555 1555 1.32
LINK OE21 CGU A 17 CA CA A 174 1555 1555 1.99
LINK C LEU A 19 N CGU A 20 1555 1555 1.32
LINK C CGU A 20 N CGU A 21 1555 1555 1.32
LINK C CGU A 21 N PRO A 22 1555 1555 1.32
LINK C ARG A 25 N CGU A 26 1555 1555 1.31
LINK C CGU A 26 N CGU A 27 1555 1555 1.31
LINK C CGU A 27 N ALA A 28 1555 1555 1.36
LINK C PHE A 29 N CGU A 30 1555 1555 1.33
LINK C CGU A 30 N ALA A 31 1555 1555 1.28
LINK C LEU A 32 N CGU A 33 1555 1555 1.31
LINK C CGU A 33 N SER A 34 1555 1555 1.32
LINK CA CA A 171 OE21 CGU A 26 1555 1555 2.47
LINK CA CA A 171 OE21 CGU A 30 1555 1555 2.49
LINK CA CA A 171 OE12 CGU A 26 1555 1555 2.35
LINK CA CA A 171 OE11 CGU A 30 1555 1555 2.36
LINK CA CA A 172 O HOH A 266 1555 1555 2.65
LINK CA CA A 172 OE12 CGU A 8 1555 1555 2.72
LINK CA CA A 172 OE12 CGU A 27 1555 1555 2.83
LINK CA CA A 172 OE22 CGU A 8 1555 1555 2.65
LINK CA CA A 172 OE21 CGU A 30 1555 1555 2.42
LINK CA CA A 172 OE22 CGU A 30 1555 1555 2.46
LINK CA CA A 173 OE11 CGU A 27 1555 1555 2.68
LINK CA CA A 173 OE22 CGU A 30 1555 1555 2.61
LINK CA CA A 173 O HOH A 231 1555 1555 2.43
LINK CA CA A 173 O HOH A 273 1555 1555 2.44
LINK CA CA A 173 OE11 CGU A 17 1555 1555 2.48
LINK CA CA A 173 OE12 CGU A 17 1555 1555 2.68
LINK CA CA A 173 OE22 CGU A 8 1555 1555 2.43
LINK CA CA A 174 N ASN A 2 1555 1555 3.34
LINK CA CA A 174 OD1 ASN A 2 1555 1555 2.08
LINK CA CA A 174 OE11 CGU A 7 1555 1555 2.77
LINK CA CA A 174 OE21 CGU A 8 1555 1555 2.66
LINK CA CA A 174 OE11 CGU A 27 1555 1555 2.59
LINK CA CA A 174 OE11 CGU A 17 1555 1555 3.08
LINK CA CA A 174 OE22 CGU A 27 1555 1555 2.56
LINK CA CA A 175 OE11 CGU A 7 1555 1555 2.49
LINK CA CA A 175 OE12 CGU A 7 1555 1555 2.47
LINK CA CA A 175 OE22 CGU A 21 1555 1555 2.77
LINK CA CA A 175 O HOH A 224 1555 1555 3.21
LINK CA CA A 175 N ALA A 1 1555 1555 2.84
LINK CA CA A 175 OE21 CGU A 17 1555 1555 2.52
LINK CA CA A 175 OE22 CGU A 17 1555 1555 2.90
LINK CA CA A 175 O HOH A 239 1555 1555 3.11
LINK CA CA A 175 N ASN A 2 1555 1555 3.25
LINK CA CA A 176 OE21 CGU A 21 1555 1555 2.42
LINK CA CA A 176 OE12 CGU A 20 1555 1555 2.55
LINK CA CA A 176 OE12 CGU A 21 1555 1555 2.66
LINK CA CA A 177 OE22 CGU A 20 1555 1555 2.74
LINK CA CA A 177 OE22 CGU A 15 1555 1555 2.84
LINK CA CA A 177 OE21 CGU A 20 1555 1555 2.45
CISPEP 1 ASN A 53 PRO A 54 0 -1.58
CISPEP 2 TYR A 94 PRO A 95 0 0.31
SITE 1 AC1 2 CGU A 26 CGU A 30
SITE 1 AC2 4 CGU A 8 CGU A 27 CGU A 30 HOH A 266
SITE 1 AC3 6 CGU A 8 CGU A 17 CGU A 27 CGU A 30
SITE 2 AC3 6 HOH A 231 HOH A 273
SITE 1 AC4 5 ASN A 2 CGU A 7 CGU A 8 CGU A 17
SITE 2 AC4 5 CGU A 27
SITE 1 AC5 5 ALA A 1 ASN A 2 CGU A 7 CGU A 17
SITE 2 AC5 5 CGU A 21
SITE 1 AC6 2 CGU A 20 CGU A 21
SITE 1 AC7 2 CGU A 15 CGU A 20
CRYST1 39.390 53.880 129.640 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 0.025387 0.000000 0.000000 0.00000
SCALE2 0.000000 0.018560 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007714 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
