HEADER COAGULATION FACTOR 21-MAR-96 1EDM
TITLE EPIDERMAL GROWTH FACTOR-LIKE DOMAIN FROM HUMAN FACTOR IX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: FACTOR IX;
COMPND 3 CHAIN: B, C;
COMPND 4 FRAGMENT: EPIDERMAL GROWTH FACTOR-LIKE DOMAIN;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 STRAIN: RZ1032, XL1-BLUE, MC1061;
SOURCE 6 GENE: HUMAN FACTOR IX;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PMA91;
SOURCE 10 EXPRESSION_SYSTEM_GENE: HUMAN FACTOR IX
KEYWDS EPIDERMAL GROWTH FACTOR, EGF, CALCIUM-BINDING, EGF-LIKE DOMAIN,
KEYWDS 2 STRUCTURE AND FUNCTION, HUMAN FACTOR IX, COAGULATION FACTOR
EXPDTA X-RAY DIFFRACTION
AUTHOR Z.RAO,P.HANDFORD,M.MAYHEW,V.KNOTT,G.G.BROWNLEE,D.STUART
REVDAT 3 03-APR-24 1EDM 1 REMARK LINK
REVDAT 2 24-FEB-09 1EDM 1 VERSN
REVDAT 1 14-OCT-96 1EDM 0
JRNL AUTH Z.RAO,P.HANDFORD,M.MAYHEW,V.KNOTT,G.G.BROWNLEE,D.STUART
JRNL TITL THE STRUCTURE OF A CA(2+)-BINDING EPIDERMAL GROWTH
JRNL TITL 2 FACTOR-LIKE DOMAIN: ITS ROLE IN PROTEIN-PROTEIN
JRNL TITL 3 INTERACTIONS.
JRNL REF CELL(CAMBRIDGE,MASS.) V. 82 131 1995
JRNL REFN ISSN 0092-8674
JRNL PMID 7606779
JRNL DOI 10.1016/0092-8674(95)90059-4
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH Z.RAO,P.HANDFORD,M.MAYHEW,V.KNOTT,G.G.BROWNLEE,D.STUART
REMARK 1 TITL CRYSTALLIZATION OF A CALCIUM-BINDING EGF-LIKE DOMAIN
REMARK 1 REF ACTA CRYSTALLOGR.,SECT.D V. 51 402 1995
REMARK 1 REFN ISSN 0907-4449
REMARK 2
REMARK 2 RESOLUTION. 1.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00
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) (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 13041
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 SET) : 0.157
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 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 : 590
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 3
REMARK 3 SOLVENT ATOMS : 131
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 17.50
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) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 1.250
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 1EDM 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_1000173027.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-JAN-92
REMARK 200 TEMPERATURE (KELVIN) : 293
REMARK 200 PH : 7.3
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : CHESS
REMARK 200 BEAMLINE : F1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.54
REMARK 200 MONOCHROMATOR : Y
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : SIEMENS
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : 3D-SCALE (D. STUART), XDS
REMARK 200 DATA SCALING SOFTWARE : XDS, 3DSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 1196
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.500
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.6
REMARK 200 DATA REDUNDANCY : 3.500
REMARK 200 R MERGE (I) : 0.05800
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) : 1.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.65
REMARK 200 COMPLETENESS FOR SHELL (%) : 92.0
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
REMARK 200 STARTING MODEL: NMR MODEL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 30.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.33
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 7.3
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y+1/2,X+1/2,Z+3/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+1/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+3/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+1/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z+1/2
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 49.15000
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 20.15000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 20.15000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 73.72500
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 20.15000
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 20.15000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 24.57500
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 20.15000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 20.15000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 73.72500
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 20.15000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 20.15000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 24.57500
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 49.15000
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 APPLY THE FOLLOWING TO CHAINS: B, C
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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH B 446 LIES ON A SPECIAL POSITION.
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 CG2 VAL B 46 O HOH B 276 1.25
REMARK 500 NZ LYS B 63 O HOH B 247 1.27
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 ASP B 65 -165.39 -121.75
REMARK 500 ASP C 65 -167.28 -121.73
REMARK 500 SER C 68 -175.37 -173.06
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 B 2 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 47 OD2
REMARK 620 2 GLY B 48 O 91.0
REMARK 620 3 GLN B 50 OE1 83.4 86.4
REMARK 620 4 ASP B 64 OD2 153.2 95.1 123.0
REMARK 620 5 ASP B 64 OD1 153.5 91.8 70.5 52.5
REMARK 620 6 ASP B 65 O 90.8 171.6 85.7 87.0 83.0
REMARK 620 7 ASN C 58 OD1 75.3 94.3 158.7 78.2 130.6 94.0
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 3 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 SER B 53 O
REMARK 620 2 SER B 53 OG 72.0
REMARK 620 3 HOH B 204 O 116.0 71.7
REMARK 620 4 HOH B 208 O 82.3 149.7 136.1
REMARK 620 5 HOH B 209 O 140.0 78.3 77.7 114.7
REMARK 620 6 HOH B 210 O 77.0 89.6 150.7 68.8 76.6
REMARK 620 7 HOH B 234 O 71.6 120.3 84.1 63.3 148.2 125.1
REMARK 620 8 HOH B 254 O 143.3 139.4 95.7 61.6 61.2 83.9 95.5
REMARK 620 N 1 2 3 4 5 6 7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA C 1 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN B 58 OD1
REMARK 620 2 ASP C 47 OD2 84.2
REMARK 620 3 GLY C 48 O 93.6 90.7
REMARK 620 4 GLN C 50 OE1 163.4 79.2 87.0
REMARK 620 5 ASP C 64 OD1 124.9 150.3 93.1 71.6
REMARK 620 6 ASP C 64 OD2 75.3 159.4 88.8 121.3 50.2
REMARK 620 7 ASP C 65 O 90.5 91.7 175.4 89.6 82.9 90.2
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 B 3
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA C 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 2
DBREF 1EDM B 46 84 UNP P00740 FA9_HUMAN 92 130
DBREF 1EDM C 46 84 UNP P00740 FA9_HUMAN 92 130
SEQRES 1 B 39 VAL ASP GLY ASP GLN CYS GLU SER ASN PRO CYS LEU ASN
SEQRES 2 B 39 GLY GLY SER CYS LYS ASP ASP ILE ASN SER TYR GLU CYS
SEQRES 3 B 39 TRP CYS PRO PHE GLY PHE GLU GLY LYS ASN CYS GLU LEU
SEQRES 1 C 39 VAL ASP GLY ASP GLN CYS GLU SER ASN PRO CYS LEU ASN
SEQRES 2 C 39 GLY GLY SER CYS LYS ASP ASP ILE ASN SER TYR GLU CYS
SEQRES 3 C 39 TRP CYS PRO PHE GLY PHE GLU GLY LYS ASN CYS GLU LEU
HET CA B 3 1
HET CA B 2 1
HET CA C 1 1
HETNAM CA CALCIUM ION
FORMUL 3 CA 3(CA 2+)
FORMUL 6 HOH *131(H2 O)
SHEET 1 A 2 SER B 61 ASP B 65 0
SHEET 2 A 2 SER B 68 TRP B 72 -1 N TRP B 72 O SER B 61
SHEET 1 B 2 SER C 61 ASP C 64 0
SHEET 2 B 2 TYR C 69 TRP C 72 -1 N TRP C 72 O SER C 61
SSBOND 1 CYS B 51 CYS B 62 1555 1555 2.03
SSBOND 2 CYS B 56 CYS B 71 1555 1555 2.01
SSBOND 3 CYS B 73 CYS B 82 1555 1555 2.03
SSBOND 4 CYS C 51 CYS C 62 1555 1555 2.01
SSBOND 5 CYS C 56 CYS C 71 1555 1555 2.03
SSBOND 6 CYS C 73 CYS C 82 1555 1555 2.04
LINK CA CA B 2 OD2 ASP B 47 1555 1555 2.30
LINK CA CA B 2 O GLY B 48 1555 1555 2.27
LINK CA CA B 2 OE1 GLN B 50 1555 1555 2.41
LINK CA CA B 2 OD2 ASP B 64 1555 1555 2.40
LINK CA CA B 2 OD1 ASP B 64 1555 1555 2.55
LINK CA CA B 2 O ASP B 65 1555 1555 2.29
LINK CA CA B 2 OD1 ASN C 58 1555 1555 2.36
LINK CA CA B 3 O SER B 53 1555 1555 2.37
LINK CA CA B 3 OG SER B 53 1555 1555 2.59
LINK CA CA B 3 O HOH B 204 1555 6446 2.50
LINK CA CA B 3 O HOH B 208 1555 1555 2.56
LINK CA CA B 3 O HOH B 209 1555 1555 2.40
LINK CA CA B 3 O HOH B 210 1555 1555 2.50
LINK CA CA B 3 O HOH B 234 1555 1555 2.33
LINK CA CA B 3 O HOH B 254 1555 1555 2.47
LINK OD1 ASN B 58 CA CA C 1 3544 1555 2.48
LINK CA CA C 1 OD2 ASP C 47 1555 1555 2.26
LINK CA CA C 1 O GLY C 48 1555 1555 2.37
LINK CA CA C 1 OE1 GLN C 50 1555 1555 2.36
LINK CA CA C 1 OD1 ASP C 64 1555 1555 2.57
LINK CA CA C 1 OD2 ASP C 64 1555 1555 2.60
LINK CA CA C 1 O ASP C 65 1555 1555 2.21
SITE 1 AC1 7 SER B 53 HOH B 204 HOH B 208 HOH B 209
SITE 2 AC1 7 HOH B 210 HOH B 234 HOH B 254
SITE 1 AC2 6 ASN B 58 ASP C 47 GLY C 48 GLN C 50
SITE 2 AC2 6 ASP C 64 ASP C 65
SITE 1 AC3 6 ASP B 47 GLY B 48 GLN B 50 ASP B 64
SITE 2 AC3 6 ASP B 65 ASN C 58
CRYST1 40.300 40.300 98.300 90.00 90.00 90.00 P 43 21 2 16
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 0.024814 0.000000 0.000000 0.00000
SCALE2 0.000000 0.024814 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010173 0.00000
(ATOM LINES ARE NOT SHOWN.)
END