HEADER BLOOD CLOTTING 07-SEP-99 1CZV
TITLE CRYSTAL STRUCTURE OF THE C2 DOMAIN OF HUMAN COAGULATION FACTOR V:
TITLE 2 DIMERIC CRYSTAL FORM
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN (COAGULATION FACTOR V);
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: C2 DISCOIDIN-LIKE DOMAIN;
COMPND 5 SYNONYM: ACTIVATED PROTEIN C COFACTOR;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 TISSUE: BLOOD;
SOURCE 6 EXPRESSION_SYSTEM_COMMON: BACULOVIRUS-DRIVEN INSECT CELL SYSTEM
KEYWDS COAGULATION, MEMBRANE-BINDING, DISCOIDIN FAMILY, CALCIUM-INDEPENDENT,
KEYWDS 2 BLOOD CLOTTING
EXPDTA X-RAY DIFFRACTION
AUTHOR S.MACEDO-RIBEIRO,W.BODE,R.HUBER,W.H.KANE,P.FUENTES-PRIOR
REVDAT 4 09-AUG-23 1CZV 1 REMARK
REVDAT 3 24-FEB-09 1CZV 1 VERSN
REVDAT 2 01-APR-03 1CZV 1 JRNL
REVDAT 1 26-NOV-99 1CZV 0
JRNL AUTH S.MACEDO-RIBEIRO,W.BODE,R.HUBER,M.A.QUINN-ALLEN,S.W.KIM,
JRNL AUTH 2 T.L.ORTEL,G.P.BOURENKOV,H.D.BARTUNIK,M.T.STUBBS,W.H.KANE,
JRNL AUTH 3 P.FUENTES-PRIOR
JRNL TITL CRYSTAL STRUCTURES OF THE MEMBRANE-BINDING C2 DOMAIN OF
JRNL TITL 2 HUMAN COAGULATION FACTOR V.
JRNL REF NATURE V. 402 434 1999
JRNL REFN ISSN 0028-0836
JRNL PMID 10586886
JRNL DOI 10.1038/46594
REMARK 2
REMARK 2 RESOLUTION. 2.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.851
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) : 8.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 1.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 14119
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.205
REMARK 3 FREE R VALUE : 0.257
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 718
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2616
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 88
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.006
REMARK 3 BOND ANGLES (DEGREES) : 1.390
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1CZV COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-SEP-99.
REMARK 100 THE DEPOSITION ID IS D_1000009658.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 07-JUN-98
REMARK 200 TEMPERATURE (KELVIN) : 289.0
REMARK 200 PH : 10.00
REMARK 200 NUMBER OF CRYSTALS USED : 1
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
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA, CCP4 (SCALA)
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 14635
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.400
REMARK 200 RESOLUTION RANGE LOW (A) : 24.600
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.8
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.09400
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) : 2.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.51
REMARK 200 COMPLETENESS FOR SHELL (%) : 90.7
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.39900
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: AMORE
REMARK 200 STARTING MODEL: 1CZS
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): 2.48
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 10.00
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
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 43.26000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 35.27000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 43.26000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 35.27000
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 GLY A 0
REMARK 465 GLY B 0
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 LYS A 15 NZ
REMARK 480 LYS A 50 NZ
REMARK 480 LYS A 55 CG CD CE NZ
REMARK 480 SER A 80 CB OG
REMARK 480 GLN A 95 CG CD OE1 NE2
REMARK 480 GLU A 98 CD OE1 OE2
REMARK 480 LYS A 100 CD CE NZ
REMARK 480 LYS A 105 CG CD CE NZ
REMARK 480 SER A 106 CB OG
REMARK 480 SER A 107 CB OG
REMARK 480 MET A 108 CE
REMARK 480 LYS B 11 NZ
REMARK 480 SER B 80 CB OG
REMARK 480 GLU B 94 CG CD OE1 OE2
REMARK 480 GLN B 95 CG CD OE1 NE2
REMARK 480 LYS B 100 CD CE NZ
REMARK 480 LYS B 105 CD CE NZ
REMARK 480 TYR B 159 CA C O CB CG CD1 CD2
REMARK 480 TYR B 159 CE1 CE2 CZ OH OXT
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 O LEU A 104 OG SER A 107 2.18
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 2 32.07 -150.61
REMARK 500 ALA A 36 48.77 -75.81
REMARK 500 LEU A 63 -37.35 75.32
REMARK 500 LEU A 79 -128.32 57.76
REMARK 500 LYS A 105 108.75 -55.42
REMARK 500 SER A 106 19.98 96.28
REMARK 500 SER A 133 -174.00 -170.92
REMARK 500 GLN A 145 -63.76 74.98
REMARK 500 SER B 2 21.67 -155.69
REMARK 500 ALA B 36 49.16 -75.54
REMARK 500 LEU B 63 -38.79 76.26
REMARK 500 LEU B 79 -127.96 56.97
REMARK 500 LYS B 105 109.00 -55.58
REMARK 500 SER B 106 21.64 95.15
REMARK 500 SER B 133 -174.18 -170.98
REMARK 500 GLN B 145 -61.99 74.16
REMARK 500 CYS B 156 -178.32 -170.40
REMARK 500
REMARK 500 REMARK: NULL
REMARK 615
REMARK 615 ZERO OCCUPANCY ATOM
REMARK 615 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 615 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 615 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 615 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 615 M RES C SSEQI
REMARK 615 HOH B 182
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1CZS RELATED DB: PDB
REMARK 900 PHENYLMERCURY COMPLEX-MONOMERIC CRYSTAL FORM
REMARK 900 RELATED ID: 1CZT RELATED DB: PDB
REMARK 900 NATIVE MONOMERIC CRYSTAL FORM
DBREF 1CZV A 0 159 UNP P12259 FA5_HUMAN 2065 2224
DBREF 1CZV B 0 159 UNP P12259 FA5_HUMAN 2065 2224
SEQRES 1 A 160 GLY CYS SER THR PRO LEU GLY MET GLU ASN GLY LYS ILE
SEQRES 2 A 160 GLU ASN LYS GLN ILE THR ALA SER SER PHE LYS LYS SER
SEQRES 3 A 160 TRP TRP GLY ASP TYR TRP GLU PRO PHE ARG ALA ARG LEU
SEQRES 4 A 160 ASN ALA GLN GLY ARG VAL ASN ALA TRP GLN ALA LYS ALA
SEQRES 5 A 160 ASN ASN ASN LYS GLN TRP LEU GLU ILE ASP LEU LEU LYS
SEQRES 6 A 160 ILE LYS LYS ILE THR ALA ILE ILE THR GLN GLY CYS LYS
SEQRES 7 A 160 SER LEU SER SER GLU MET TYR VAL LYS SER TYR THR ILE
SEQRES 8 A 160 HIS TYR SER GLU GLN GLY VAL GLU TRP LYS PRO TYR ARG
SEQRES 9 A 160 LEU LYS SER SER MET VAL ASP LYS ILE PHE GLU GLY ASN
SEQRES 10 A 160 THR ASN THR LYS GLY HIS VAL LYS ASN PHE PHE ASN PRO
SEQRES 11 A 160 PRO ILE ILE SER ARG PHE ILE ARG VAL ILE PRO LYS THR
SEQRES 12 A 160 TRP ASN GLN SER ILE THR LEU ARG LEU GLU LEU PHE GLY
SEQRES 13 A 160 CYS ASP ILE TYR
SEQRES 1 B 160 GLY CYS SER THR PRO LEU GLY MET GLU ASN GLY LYS ILE
SEQRES 2 B 160 GLU ASN LYS GLN ILE THR ALA SER SER PHE LYS LYS SER
SEQRES 3 B 160 TRP TRP GLY ASP TYR TRP GLU PRO PHE ARG ALA ARG LEU
SEQRES 4 B 160 ASN ALA GLN GLY ARG VAL ASN ALA TRP GLN ALA LYS ALA
SEQRES 5 B 160 ASN ASN ASN LYS GLN TRP LEU GLU ILE ASP LEU LEU LYS
SEQRES 6 B 160 ILE LYS LYS ILE THR ALA ILE ILE THR GLN GLY CYS LYS
SEQRES 7 B 160 SER LEU SER SER GLU MET TYR VAL LYS SER TYR THR ILE
SEQRES 8 B 160 HIS TYR SER GLU GLN GLY VAL GLU TRP LYS PRO TYR ARG
SEQRES 9 B 160 LEU LYS SER SER MET VAL ASP LYS ILE PHE GLU GLY ASN
SEQRES 10 B 160 THR ASN THR LYS GLY HIS VAL LYS ASN PHE PHE ASN PRO
SEQRES 11 B 160 PRO ILE ILE SER ARG PHE ILE ARG VAL ILE PRO LYS THR
SEQRES 12 B 160 TRP ASN GLN SER ILE THR LEU ARG LEU GLU LEU PHE GLY
SEQRES 13 B 160 CYS ASP ILE TYR
FORMUL 3 HOH *88(H2 O)
HELIX 1 1 GLU A 13 LYS A 15 5 3
HELIX 2 2 GLU A 32 ALA A 36 5 5
HELIX 3 3 GLU B 13 LYS B 15 5 3
HELIX 4 4 GLU B 32 ALA B 36 5 5
SHEET 1 A 1 GLN A 16 SER A 20 0
SHEET 1 B 1 TRP A 57 ASP A 61 0
SHEET 1 C 1 ALA A 70 GLY A 75 0
SHEET 1 D 1 VAL A 85 SER A 93 0
SHEET 1 E 1 PHE A 113 THR A 117 0
SHEET 1 F 1 VAL A 123 PHE A 127 0
SHEET 1 G 1 PHE A 135 ILE A 139 0
SHEET 1 H 1 ARG A 150 PHE A 154 0
SHEET 1 I 1 GLN B 16 SER B 20 0
SHEET 1 J 1 TRP B 57 ASP B 61 0
SHEET 1 K 1 ALA B 70 GLY B 75 0
SHEET 1 L 1 VAL B 85 SER B 93 0
SHEET 1 M 1 PHE B 113 THR B 117 0
SHEET 1 N 1 VAL B 123 PHE B 127 0
SHEET 1 O 1 PHE B 135 ILE B 139 0
SHEET 1 P 1 ARG B 150 PHE B 154 0
SSBOND 1 CYS A 1 CYS A 156 1555 1555 2.49
SSBOND 2 CYS B 1 CYS B 156 1555 1555 2.69
CISPEP 1 ASN A 128 PRO A 129 0 0.20
CISPEP 2 ASN B 128 PRO B 129 0 0.61
CRYST1 86.520 70.540 60.580 90.00 90.00 90.00 P 21 21 2 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 0.011558 0.000000 0.000000 0.00000
SCALE2 0.000000 0.014176 0.000000 0.00000
SCALE3 0.000000 0.000000 0.016507 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
