HEADER CHEMOATTRACTANT 27-NOV-96 1DOK
TITLE MONOCYTE CHEMOATTRACTANT PROTEIN 1, P-FORM
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MONOCYTE CHEMOATTRACTANT PROTEIN 1;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: MCP-1, MCAF;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: BL21
KEYWDS CHEMOATTRACTANT, CYTOKINE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.LUBKOWSKI,G.BUJACZ,L.BOQUE,A.WLODAWER,P.J.DOMAILLE,T.M.HANDEL
REVDAT 3 09-AUG-23 1DOK 1 REMARK
REVDAT 2 24-FEB-09 1DOK 1 VERSN
REVDAT 1 12-MAR-97 1DOK 0
JRNL AUTH J.LUBKOWSKI,G.BUJACZ,L.BOQUE,P.J.DOMAILLE,T.M.HANDEL,
JRNL AUTH 2 A.WLODAWER
JRNL TITL THE STRUCTURE OF MCP-1 IN TWO CRYSTAL FORMS PROVIDES A RARE
JRNL TITL 2 EXAMPLE OF VARIABLE QUATERNARY INTERACTIONS.
JRNL REF NAT.STRUCT.BIOL. V. 4 64 1997
JRNL REFN ISSN 1072-8368
JRNL PMID 8989326
JRNL DOI 10.1038/NSB0197-64
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH T.M.HANDEL,P.J.DOMAILLE
REMARK 1 TITL HETERONUCLEAR (1H, 13C, 15N) NMR ASSIGNMENTS AND SOLUTION
REMARK 1 TITL 2 STRUCTURE OF THE MONOCYTE CHEMOATTRACTANT PROTEIN-1 (MCP-1)
REMARK 1 TITL 3 DIMER
REMARK 1 REF BIOCHEMISTRY V. 35 6569 1996
REMARK 1 REFN ISSN 0006-2960
REMARK 2
REMARK 2 RESOLUTION. 1.85 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.1
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.85
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 10.00
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) (%) : 97.0
REMARK 3 NUMBER OF REFLECTIONS : 12308
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, UP TO 2.0 A
REMARK 3 R VALUE (WORKING SET) : 0.191
REMARK 3 FREE R VALUE : 0.245
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 7.000
REMARK 3 FREE R VALUE TEST SET COUNT : 572
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.010
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 : 1150
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 10
REMARK 3 SOLVENT ATOMS : 116
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 30.00
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) : 0.014
REMARK 3 BOND ANGLES (DEGREES) : 1.740
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 27.70
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.460
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) : 2.190 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.320 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 2.190 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 2.320 ; 2.500
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 : 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: REFLECTIONS FOR R-FREE TEST SELECTED IN
REMARK 3 10.0 - 2.0 A RESOLUTION RANGE. THE TWO CHAINS WERE REFINED
REMARK 3 INDEPENDENTLY.
REMARK 4
REMARK 4 1DOK 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_1000172872.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 05-NOV-95
REMARK 200 TEMPERATURE (KELVIN) : 298
REMARK 200 PH : 7.5-8.0
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 RUH2R
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : GRAPHITE(002)
REMARK 200 OPTICS : COLLIMATOR
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 12318
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.850
REMARK 200 RESOLUTION RANGE LOW (A) : 10.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.0
REMARK 200 DATA REDUNDANCY : 4.590
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.07800
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 15.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.85
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.92
REMARK 200 COMPLETENESS FOR SHELL (%) : 94.7
REMARK 200 DATA REDUNDANCY IN SHELL : 3.82
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.36300
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.150
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: PDB ENTRY 1DOM
REMARK 200
REMARK 200 REMARK: INITIAL MODEL FOR MOLECULAR REPLACEMENT WAS MODIFIED AS
REMARK 200 DESCRIBED IN JOURNAL ARTICLE.
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 32.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.04
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 10 MG/ML PROTEIN IN 50 MM TRIS BUFFER
REMARK 280 PH 7.5-8 EQUILIBRATED AGAINST 50-55% AMMONIUM SULFATE USING
REMARK 280 HANGING DROP VAPOR DIFFUSION METHOD., PH 8.0, VAPOR DIFFUSION -
REMARK 280 HANGING DROP, VAPOR DIFFUSION, HANGING DROP
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 53.82500
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 25.37000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 25.37000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 80.73750
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 25.37000
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 25.37000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 26.91250
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 25.37000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 25.37000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 80.73750
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 25.37000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 25.37000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 26.91250
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 53.82500
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2130 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 9190 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -23.0 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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 6750 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 16270 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -92.0 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 350 BIOMT1 2 0.000000 -1.000000 0.000000 50.74000
REMARK 350 BIOMT2 2 -1.000000 0.000000 0.000000 50.74000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 53.82500
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 GLN A 72
REMARK 465 THR A 73
REMARK 465 PRO A 74
REMARK 465 LYS A 75
REMARK 465 THR A 76
REMARK 465 GLN B 72
REMARK 465 THR B 73
REMARK 465 PRO B 74
REMARK 465 LYS B 75
REMARK 465 THR B 76
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 GLN B 1 -65.09 -13.06
REMARK 500 SER B 27 -178.85 -170.09
REMARK 500 ALA B 48 40.05 70.68
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 402
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 RESIDUE MET 0 IS AN ARTIFACT OF EXPRESSION.
DBREF 1DOK A 1 76 UNP P13500 CCL2_HUMAN 24 99
DBREF 1DOK B 1 76 UNP P13500 CCL2_HUMAN 24 99
SEQRES 1 A 77 MET GLN PRO ASP ALA ILE ASN ALA PRO VAL THR CYS CYS
SEQRES 2 A 77 TYR ASN PHE THR ASN ARG LYS ILE SER VAL GLN ARG LEU
SEQRES 3 A 77 ALA SER TYR ARG ARG ILE THR SER SER LYS CYS PRO LYS
SEQRES 4 A 77 GLU ALA VAL ILE PHE LYS THR ILE VAL ALA LYS GLU ILE
SEQRES 5 A 77 CYS ALA ASP PRO LYS GLN LYS TRP VAL GLN ASP SER MET
SEQRES 6 A 77 ASP HIS LEU ASP LYS GLN THR GLN THR PRO LYS THR
SEQRES 1 B 77 MET GLN PRO ASP ALA ILE ASN ALA PRO VAL THR CYS CYS
SEQRES 2 B 77 TYR ASN PHE THR ASN ARG LYS ILE SER VAL GLN ARG LEU
SEQRES 3 B 77 ALA SER TYR ARG ARG ILE THR SER SER LYS CYS PRO LYS
SEQRES 4 B 77 GLU ALA VAL ILE PHE LYS THR ILE VAL ALA LYS GLU ILE
SEQRES 5 B 77 CYS ALA ASP PRO LYS GLN LYS TRP VAL GLN ASP SER MET
SEQRES 6 B 77 ASP HIS LEU ASP LYS GLN THR GLN THR PRO LYS THR
HET SO4 A 402 5
HET SO4 B 401 5
HETNAM SO4 SULFATE ION
FORMUL 3 SO4 2(O4 S 2-)
FORMUL 5 HOH *116(H2 O)
HELIX 1 1 PRO A 2 ASN A 6 1 5
HELIX 2 2 VAL A 22 ARG A 24 5 3
HELIX 3 3 LYS A 58 LYS A 69 1 12
HELIX 4 4 ASP B 3 ASN B 6 5 4
HELIX 5 5 LYS B 58 LYS B 69 1 12
SHEET 1 A 2 VAL A 9 CYS A 11 0
SHEET 2 A 2 VAL B 9 CYS B 11 -1 N CYS B 11 O VAL A 9
SHEET 1 B 3 GLU A 50 ALA A 53 0
SHEET 2 B 3 ALA A 40 THR A 45 -1 N PHE A 43 O ILE A 51
SHEET 3 B 3 LEU A 25 ILE A 31 -1 N ILE A 31 O ALA A 40
SHEET 1 C 3 GLU B 50 ALA B 53 0
SHEET 2 C 3 VAL B 41 THR B 45 -1 N PHE B 43 O ILE B 51
SHEET 3 C 3 LEU B 25 ARG B 30 -1 N ARG B 29 O ILE B 42
SSBOND 1 CYS A 11 CYS A 36 1555 1555 2.03
SSBOND 2 CYS A 12 CYS A 52 1555 1555 2.04
SSBOND 3 CYS B 11 CYS B 36 1555 1555 2.02
SSBOND 4 CYS B 12 CYS B 52 1555 1555 2.02
SITE 1 AC1 8 ASN A 6 ASN A 14 THR B 16 ASN B 17
SITE 2 AC1 8 ARG B 18 LYS B 35 HOH B 234 HOH B 299
SITE 1 AC2 4 SER A 33 SER A 34 HOH A 279 HOH A 304
CRYST1 50.740 50.740 107.650 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 0.019708 0.000000 0.000000 0.00000
SCALE2 0.000000 0.019708 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009289 0.00000
MTRIX1 1 -0.652315 -0.596164 0.468052 35.99238 1
MTRIX2 1 -0.546077 -0.058591 -0.835684 84.54701 1
MTRIX3 1 0.525628 -0.800722 -0.287332 71.81376 1
(ATOM LINES ARE NOT SHOWN.)
END