HEADER IMMUNE SYSTEM/DNA 14-MAR-01 1I8M
TITLE CRYSTAL STRUCTURE OF A RECOMBINANT ANTI-SINGLE-STRANDED DNA ANTIBODY
TITLE 2 FRAGMENT COMPLEXED WITH DT5
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 5'-D(*TP*TP*TP*TP*T)-3';
COMPND 3 CHAIN: T;
COMPND 4 ENGINEERED: YES;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: 5'-D(P*TP*T)-3';
COMPND 7 CHAIN: D;
COMPND 8 ENGINEERED: YES;
COMPND 9 MOL_ID: 3;
COMPND 10 MOLECULE: ANTIBODY LIGHT CHAIN FAB;
COMPND 11 CHAIN: L, A;
COMPND 12 SYNONYM: ANTI-SINGLE-STRANDED DNA ANTIGEN-BINDING FAB FRAGMENT;
COMPND 13 ENGINEERED: YES;
COMPND 14 MOL_ID: 4;
COMPND 15 MOLECULE: ANTIBODY HEAVY CHAIN FAB;
COMPND 16 CHAIN: H, B;
COMPND 17 SYNONYM: ANTI-SINGLE-STRANDED DNA ANTIGEN-BINDING FAB FRAGMENT;
COMPND 18 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 MOL_ID: 2;
SOURCE 4 SYNTHETIC: YES;
SOURCE 5 MOL_ID: 3;
SOURCE 6 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 7 ORGANISM_COMMON: HOUSE MOUSE;
SOURCE 8 ORGANISM_TAXID: 10090;
SOURCE 9 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 10 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 11 EXPRESSION_SYSTEM_STRAIN: DH12S;
SOURCE 12 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 13 EXPRESSION_SYSTEM_PLASMID: PCOMB3/6-HIS;
SOURCE 14 MOL_ID: 4;
SOURCE 15 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 16 ORGANISM_COMMON: HOUSE MOUSE;
SOURCE 17 ORGANISM_TAXID: 10090;
SOURCE 18 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 19 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 20 EXPRESSION_SYSTEM_STRAIN: DH12S;
SOURCE 21 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 22 EXPRESSION_SYSTEM_PLASMID: PCOMB3/6-HIS
KEYWDS FAB, ANTIBODY, ANTI-DNA ANTIBODY, AUTOANTIBODY, LUPUS, IMMUNE SYSTEM-
KEYWDS 2 DNA COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR J.J.TANNER,A.A.KOMISSAROV,S.L.DEUTSCHER
REVDAT 4 09-AUG-23 1I8M 1 REMARK SEQADV SHEET
REVDAT 3 04-OCT-17 1I8M 1 REMARK
REVDAT 2 24-FEB-09 1I8M 1 VERSN
REVDAT 1 07-DEC-01 1I8M 0
JRNL AUTH J.J.TANNER,A.A.KOMISSAROV,S.L.DEUTSCHER
JRNL TITL CRYSTAL STRUCTURE OF AN ANTIGEN-BINDING FRAGMENT BOUND TO
JRNL TITL 2 SINGLE-STRANDED DNA
JRNL REF J.MOL.BIOL. V. 314 807 2001
JRNL REFN ISSN 0022-2836
JRNL PMID 11733999
JRNL DOI 10.1006/JMBI.2001.5178
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH S.P.PREWITT,A.A.KOMISSAROV,S.L.DEUTSCHER,J.J.TANNER
REMARK 1 TITL CRYSTALLIZATION AND MOLECULAR REPLACEMENT STUDIES OF A
REMARK 1 TITL 2 RECOMBINANT ANTIGEN-BINDING FRAGMENT COMPLEXED WITH
REMARK 1 TITL 3 SINGLE-STRANDED DNA.
REMARK 1 REF ACTA CRYSTALLOGR.,SECT.D V. 56 1007 2000
REMARK 1 REFN ISSN 0907-4449
REMARK 1 DOI 10.1107/S0907444900008222
REMARK 2
REMARK 2 RESOLUTION. 2.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.0
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 27.66
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 3972329.880
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 98.8
REMARK 3 NUMBER OF REFLECTIONS : 72520
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) : 0.220
REMARK 3 FREE R VALUE : 0.258
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 9.900
REMARK 3 FREE R VALUE TEST SET COUNT : 7190
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.003
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) : 2.10
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.23
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 97.10
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 10614
REMARK 3 BIN R VALUE (WORKING SET) : 0.2725
REMARK 3 BIN FREE R VALUE : 0.3023
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 9.30
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 1082
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.009
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6414
REMARK 3 NUCLEIC ACID ATOMS : 121
REMARK 3 HETEROGEN ATOMS : 5
REMARK 3 SOLVENT ATOMS : 339
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 23.00
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 38.50
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 3.79000
REMARK 3 B22 (A**2) : 3.79000
REMARK 3 B33 (A**2) : -7.57000
REMARK 3 B12 (A**2) : 1.06000
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) : 0.28
REMARK 3 ESD FROM SIGMAA (A) : 0.24
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) : 0.33
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.27
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.011
REMARK 3 BOND ANGLES (DEGREES) : 1.624
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 27.37
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.999
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) : 1.330 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.050 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 2.090 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 2.930 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.38
REMARK 3 BSOL : 50.21
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 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : DNA-RNA_REP.PARAM
REMARK 3 PARAMETER FILE 3 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 4 : ION.PARAM
REMARK 3 PARAMETER FILE 5 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : DNA-RNA.TOP
REMARK 3 TOPOLOGY FILE 3 : WATER.TOP
REMARK 3 TOPOLOGY FILE 4 : ION.TOP
REMARK 3 TOPOLOGY FILE 5 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1I8M COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-MAR-01.
REMARK 100 THE DEPOSITION ID IS D_1000013041.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 21-SEP-99; 23-MAR-00
REMARK 200 TEMPERATURE (KELVIN) : 173; 173
REMARK 200 PH : 5
REMARK 200 NUMBER OF CRYSTALS USED : 2
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y; Y
REMARK 200 RADIATION SOURCE : NSLS; NSLS
REMARK 200 BEAMLINE : X8C; X12B
REMARK 200 X-RAY GENERATOR MODEL : NULL; NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M; M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.979; 0.978
REMARK 200 MONOCHROMATOR : NSLS X8C BEAMLINE OPTICS; NSLS
REMARK 200 X12B BEAMLINE OPTICS
REMARK 200 OPTICS : NULL; NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD; CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4; ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : SOFTWARE AT X8C AND X12B
REMARK 200 BEAMLINES
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 72520
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100
REMARK 200 RESOLUTION RANGE LOW (A) : 28.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.0
REMARK 200 DATA REDUNDANCY : 6.800
REMARK 200 R MERGE (I) : 0.07900
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 19.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.18
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.0
REMARK 200 DATA REDUNDANCY IN SHELL : 3.60
REMARK 200 R MERGE FOR SHELL (I) : 0.29400
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.600
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH; SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE, X-PLOR
REMARK 200 STARTING MODEL: 1MLC
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 63.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.10
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 2 M AMMONIUM SULFATE, 0.1 M SODIUM
REMARK 280 ACETATE, PH 5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 295K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 65 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+1/6
REMARK 290 6555 X-Y,X,Z+5/6
REMARK 290 7555 Y,X,-Z+2/3
REMARK 290 8555 X-Y,-Y,-Z
REMARK 290 9555 -X,-X+Y,-Z+1/3
REMARK 290 10555 -Y,-X,-Z+1/6
REMARK 290 11555 -X+Y,Y,-Z+1/2
REMARK 290 12555 X,X-Y,-Z+5/6
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 96.37867
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 48.18933
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 72.28400
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 24.09467
REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 120.47333
REMARK 290 SMTRY1 7 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 7 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 96.37867
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 9 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 9 0.000000 0.000000 -1.000000 48.18933
REMARK 290 SMTRY1 10 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 10 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 24.09467
REMARK 290 SMTRY1 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 11 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 72.28400
REMARK 290 SMTRY1 12 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 12 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 120.47333
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 300 REMARK: THE BIOLOGICAL ASSEMBLY IS AN ANTIGEN BINDING FRAGMENT,
REMARK 300 FAB. THERE ARE TWO FABS IN THE ASYMMETRIC UNIT.
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: TRIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: T, L, H
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: TRIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, 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 CYS L 214
REMARK 465 GLY H 127
REMARK 465 SER H 128
REMARK 465 ALA H 129
REMARK 465 ALA H 130
REMARK 465 GLN H 131
REMARK 465 THR H 132
REMARK 465 ASN H 133
REMARK 465 ASP H 214
REMARK 465 CYS H 215
REMARK 465 THR H 216
REMARK 465 SER H 217
REMARK 465 CYS A 214
REMARK 465 GLY B 127
REMARK 465 SER B 128
REMARK 465 ALA B 129
REMARK 465 ALA B 130
REMARK 465 GLN B 131
REMARK 465 THR B 132
REMARK 465 ASN B 133
REMARK 465 ASP B 214
REMARK 465 CYS B 215
REMARK 465 THR B 216
REMARK 465 SER B 217
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 DT D 3 C5' C4' O4' C3' O3' C2' C1'
REMARK 470 DT D 3 N1 C2 O2 N3 C4 O4 C5
REMARK 470 DT D 3 C7 C6
REMARK 470 GLU L 1 CG CD OE1 OE2
REMARK 470 GLN L 3 CG CD OE1 NE2
REMARK 470 GLU L 27 CG CD OE1 OE2
REMARK 470 GLN L 45 CG CD OE1 NE2
REMARK 470 GLU L 56 CG CD OE1 OE2
REMARK 470 GLN L 70 NE2
REMARK 470 LYS L 103 CE NZ
REMARK 470 LYS L 107 CG CD CE NZ
REMARK 470 ASN L 190 CG OD1 ND2
REMARK 470 ASN L 212 CG OD1 ND2
REMARK 470 GLU L 213 CG CD OE1 OE2
REMARK 470 GLN H 1 CG CD OE1 NE2
REMARK 470 LYS H 13 CD CE NZ
REMARK 470 TYR H 53 CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LYS H 64 CD CE NZ
REMARK 470 LYS H 73 CG CD CE NZ
REMARK 470 GLU H 85 OE1 OE2
REMARK 470 TYR H 97 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 ARG H 98 NE CZ NH1 NH2
REMARK 470 LYS H 115 CD CE NZ
REMARK 470 GLN H 171 CG CD OE1 NE2
REMARK 470 GLU H 191 OE1 OE2
REMARK 470 GLU A 1 CG CD OE1 OE2
REMARK 470 GLN A 3 CG CD OE1 NE2
REMARK 470 LYS A 42 CE NZ
REMARK 470 GLN A 45 CG CD OE1 NE2
REMARK 470 ASN A 50 CG OD1 ND2
REMARK 470 LYS A 52 CG CD CE NZ
REMARK 470 LYS A 103 CE NZ
REMARK 470 GLN A 156 NE2
REMARK 470 GLU A 185 OE2
REMARK 470 GLN B 1 CG CD OE1 NE2
REMARK 470 LYS B 13 CD CE NZ
REMARK 470 TYR B 53 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LYS B 58 CG CD CE NZ
REMARK 470 GLU B 61 CD OE1 OE2
REMARK 470 LYS B 73 CG CD CE NZ
REMARK 470 GLU B 85 CD OE1 OE2
REMARK 470 LYS B 115 CG CD CE NZ
REMARK 470 SER B 172 OG
REMARK 470 ASP B 173 CG OD1 OD2
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 CYS H 140 CA - CB - SG ANGL. DEV. = 12.9 DEGREES
REMARK 500 CYS B 140 CA - CB - SG ANGL. DEV. = 10.4 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 TYR L 30 -127.32 62.42
REMARK 500 ALA L 51 -27.91 59.60
REMARK 500 SER L 77 75.82 49.70
REMARK 500 TYR L 92 74.81 -111.54
REMARK 500 PRO H 41 119.86 -32.51
REMARK 500 ASP H 55 16.37 59.36
REMARK 500 ALA H 88 177.48 176.31
REMARK 500 LEU A 11 135.35 -171.12
REMARK 500 TYR A 30 -111.15 57.50
REMARK 500 ALA A 51 -30.01 58.62
REMARK 500 SER A 77 73.49 63.34
REMARK 500 HIS A 91 -165.04 -119.29
REMARK 500 TYR A 92 -53.90 68.05
REMARK 500 LEU A 96 57.98 -90.22
REMARK 500 SER B 82B 61.02 34.28
REMARK 500 SER B 172 60.26 66.79
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 A 401
DBREF 1I8M L 1 214 GB 498315 AAC28909 1 214
DBREF 1I8M A 1 214 GB 498315 AAC28909 1 214
DBREF 1I8M H 5 217 GB 3399661 AAC28908 1 220
DBREF 1I8M B 5 217 GB 3399661 AAC28908 1 220
DBREF 1I8M T 1 5 PDB 1I8M 1I8M 1 5
DBREF 1I8M D 2 3 PDB 1I8M 1I8M 2 3
SEQADV 1I8M GLN H 1 GB 3399661 CLONING ARTIFACT
SEQADV 1I8M VAL H 2 GB 3399661 CLONING ARTIFACT
SEQADV 1I8M LYS H 3 GB 3399661 CLONING ARTIFACT
SEQADV 1I8M LEU H 4 GB 3399661 CLONING ARTIFACT
SEQADV 1I8M GLN B 1 GB 3399661 CLONING ARTIFACT
SEQADV 1I8M VAL B 2 GB 3399661 CLONING ARTIFACT
SEQADV 1I8M LYS B 3 GB 3399661 CLONING ARTIFACT
SEQADV 1I8M LEU B 4 GB 3399661 CLONING ARTIFACT
SEQRES 1 T 5 DT DT DT DT DT
SEQRES 1 D 2 DT DT
SEQRES 1 L 214 GLU LEU GLN MET THR GLN SER PRO ALA SER LEU SER ALA
SEQRES 2 L 214 SER VAL GLY GLU THR VAL THR ILE THR CYS ARG ALA SER
SEQRES 3 L 214 GLU ASN ILE TYR SER TYR LEU ALA TRP TYR GLN GLN LYS
SEQRES 4 L 214 GLN GLY LYS SER PRO GLN LEU LEU VAL TYR ASN ALA LYS
SEQRES 5 L 214 THR LEU ALA GLU GLY VAL PRO SER ARG PHE SER GLY SER
SEQRES 6 L 214 GLY SER GLY THR GLN PHE SER LEU LYS ILE ASN SER LEU
SEQRES 7 L 214 GLN PRO GLU ASP PHE GLY SER TYR TYR CYS GLN HIS HIS
SEQRES 8 L 214 TYR GLY THR PRO LEU THR PHE GLY ALA GLY THR LYS LEU
SEQRES 9 L 214 GLU LEU LYS ARG ALA ASP ALA ALA PRO THR VAL SER ILE
SEQRES 10 L 214 PHE PRO PRO SER SER GLU GLN LEU THR SER GLY GLY ALA
SEQRES 11 L 214 SER VAL VAL CYS PHE LEU ASN ASN PHE TYR PRO LYS ASP
SEQRES 12 L 214 ILE ASN VAL LYS TRP LYS ILE ASP GLY SER GLU ARG GLN
SEQRES 13 L 214 ASN GLY VAL LEU ASN SER TRP THR ASP GLN ASP SER LYS
SEQRES 14 L 214 ASP SER THR TYR SER MET SER SER THR LEU THR LEU THR
SEQRES 15 L 214 LYS ASP GLU TYR GLU ARG HIS ASN SER TYR THR CYS GLU
SEQRES 16 L 214 ALA THR HIS LYS THR SER THR SER PRO ILE VAL LYS SER
SEQRES 17 L 214 PHE ASN ARG ASN GLU CYS
SEQRES 1 H 224 GLN VAL LYS LEU LEU GLU SER GLY PRO GLU LEU VAL LYS
SEQRES 2 H 224 PRO GLY ALA SER VAL LYS MET SER CYS LYS ALA SER GLY
SEQRES 3 H 224 TYR THR PHE THR SER TYR VAL MET HIS TRP VAL LYS GLN
SEQRES 4 H 224 LYS PRO GLY GLN GLY LEU GLU TRP ILE GLY TYR ILE ASN
SEQRES 5 H 224 PRO TYR ASN ASP GLY THR LYS TYR ASN GLU LYS PHE LYS
SEQRES 6 H 224 GLY LYS ALA THR LEU THR SER ASP LYS SER SER SER THR
SEQRES 7 H 224 ALA TYR MET GLU LEU SER SER LEU THR SER GLU ASP SER
SEQRES 8 H 224 ALA VAL TYR TYR CYS VAL ARG GLY GLY TYR ARG PRO TYR
SEQRES 9 H 224 TYR ALA MET ASP TYR TRP GLY GLN GLY THR SER VAL THR
SEQRES 10 H 224 VAL SER SER ALA LYS THR THR PRO PRO SER VAL TYR PRO
SEQRES 11 H 224 LEU ALA PRO GLY SER ALA ALA GLN THR ASN SER MET VAL
SEQRES 12 H 224 THR LEU GLY CYS LEU VAL LYS GLY TYR PHE PRO GLU PRO
SEQRES 13 H 224 VAL THR VAL THR TRP ASN SER GLY SER LEU SER SER GLY
SEQRES 14 H 224 VAL HIS THR PHE PRO ALA VAL LEU GLN SER ASP LEU TYR
SEQRES 15 H 224 THR LEU SER SER SER VAL THR VAL PRO SER SER THR TRP
SEQRES 16 H 224 PRO SER GLU THR VAL THR CYS ASN VAL ALA HIS PRO ALA
SEQRES 17 H 224 SER SER THR LYS VAL ASP LYS LYS ILE VAL PRO ARG ASP
SEQRES 18 H 224 CYS THR SER
SEQRES 1 A 214 GLU LEU GLN MET THR GLN SER PRO ALA SER LEU SER ALA
SEQRES 2 A 214 SER VAL GLY GLU THR VAL THR ILE THR CYS ARG ALA SER
SEQRES 3 A 214 GLU ASN ILE TYR SER TYR LEU ALA TRP TYR GLN GLN LYS
SEQRES 4 A 214 GLN GLY LYS SER PRO GLN LEU LEU VAL TYR ASN ALA LYS
SEQRES 5 A 214 THR LEU ALA GLU GLY VAL PRO SER ARG PHE SER GLY SER
SEQRES 6 A 214 GLY SER GLY THR GLN PHE SER LEU LYS ILE ASN SER LEU
SEQRES 7 A 214 GLN PRO GLU ASP PHE GLY SER TYR TYR CYS GLN HIS HIS
SEQRES 8 A 214 TYR GLY THR PRO LEU THR PHE GLY ALA GLY THR LYS LEU
SEQRES 9 A 214 GLU LEU LYS ARG ALA ASP ALA ALA PRO THR VAL SER ILE
SEQRES 10 A 214 PHE PRO PRO SER SER GLU GLN LEU THR SER GLY GLY ALA
SEQRES 11 A 214 SER VAL VAL CYS PHE LEU ASN ASN PHE TYR PRO LYS ASP
SEQRES 12 A 214 ILE ASN VAL LYS TRP LYS ILE ASP GLY SER GLU ARG GLN
SEQRES 13 A 214 ASN GLY VAL LEU ASN SER TRP THR ASP GLN ASP SER LYS
SEQRES 14 A 214 ASP SER THR TYR SER MET SER SER THR LEU THR LEU THR
SEQRES 15 A 214 LYS ASP GLU TYR GLU ARG HIS ASN SER TYR THR CYS GLU
SEQRES 16 A 214 ALA THR HIS LYS THR SER THR SER PRO ILE VAL LYS SER
SEQRES 17 A 214 PHE ASN ARG ASN GLU CYS
SEQRES 1 B 224 GLN VAL LYS LEU LEU GLU SER GLY PRO GLU LEU VAL LYS
SEQRES 2 B 224 PRO GLY ALA SER VAL LYS MET SER CYS LYS ALA SER GLY
SEQRES 3 B 224 TYR THR PHE THR SER TYR VAL MET HIS TRP VAL LYS GLN
SEQRES 4 B 224 LYS PRO GLY GLN GLY LEU GLU TRP ILE GLY TYR ILE ASN
SEQRES 5 B 224 PRO TYR ASN ASP GLY THR LYS TYR ASN GLU LYS PHE LYS
SEQRES 6 B 224 GLY LYS ALA THR LEU THR SER ASP LYS SER SER SER THR
SEQRES 7 B 224 ALA TYR MET GLU LEU SER SER LEU THR SER GLU ASP SER
SEQRES 8 B 224 ALA VAL TYR TYR CYS VAL ARG GLY GLY TYR ARG PRO TYR
SEQRES 9 B 224 TYR ALA MET ASP TYR TRP GLY GLN GLY THR SER VAL THR
SEQRES 10 B 224 VAL SER SER ALA LYS THR THR PRO PRO SER VAL TYR PRO
SEQRES 11 B 224 LEU ALA PRO GLY SER ALA ALA GLN THR ASN SER MET VAL
SEQRES 12 B 224 THR LEU GLY CYS LEU VAL LYS GLY TYR PHE PRO GLU PRO
SEQRES 13 B 224 VAL THR VAL THR TRP ASN SER GLY SER LEU SER SER GLY
SEQRES 14 B 224 VAL HIS THR PHE PRO ALA VAL LEU GLN SER ASP LEU TYR
SEQRES 15 B 224 THR LEU SER SER SER VAL THR VAL PRO SER SER THR TRP
SEQRES 16 B 224 PRO SER GLU THR VAL THR CYS ASN VAL ALA HIS PRO ALA
SEQRES 17 B 224 SER SER THR LYS VAL ASP LYS LYS ILE VAL PRO ARG ASP
SEQRES 18 B 224 CYS THR SER
HET SO4 A 401 5
HETNAM SO4 SULFATE ION
FORMUL 7 SO4 O4 S 2-
FORMUL 8 HOH *339(H2 O)
HELIX 1 1 GLN L 79 PHE L 83 5 5
HELIX 2 2 SER L 121 THR L 126 1 6
HELIX 3 3 LYS L 183 GLU L 187 1 5
HELIX 4 4 THR H 28 TYR H 32 5 5
HELIX 5 5 GLU H 61 LYS H 64 5 4
HELIX 6 6 THR H 83 SER H 87 5 5
HELIX 7 7 SER H 156 SER H 158 5 3
HELIX 8 8 SER H 186 TRP H 188 5 3
HELIX 9 9 PRO H 200 SER H 203 5 4
HELIX 10 10 GLN A 79 PHE A 83 5 5
HELIX 11 11 SER A 121 THR A 126 1 6
HELIX 12 12 LYS A 183 ARG A 188 1 6
HELIX 13 13 THR B 28 TYR B 32 5 5
HELIX 14 14 GLU B 61 LYS B 64 5 4
HELIX 15 15 THR B 83 SER B 87 5 5
HELIX 16 16 SER B 156 SER B 158 5 3
HELIX 17 17 SER B 186 TRP B 188 5 3
HELIX 18 18 PRO B 200 SER B 203 5 4
SHEET 1 A 4 MET L 4 SER L 7 0
SHEET 2 A 4 VAL L 19 ALA L 25 -1 O THR L 22 N SER L 7
SHEET 3 A 4 GLN L 70 ILE L 75 -1 O PHE L 71 N CYS L 23
SHEET 4 A 4 PHE L 62 SER L 67 -1 N SER L 63 O LYS L 74
SHEET 1 B 5 THR L 53 LEU L 54 0
SHEET 2 B 5 GLN L 45 TYR L 49 -1 N TYR L 49 O THR L 53
SHEET 3 B 5 LEU L 33 GLN L 38 -1 N TRP L 35 O LEU L 47
SHEET 4 B 5 GLY L 84 HIS L 90 -1 O GLN L 89 N ALA L 34
SHEET 5 B 5 THR L 97 PHE L 98 -1 O THR L 97 N HIS L 90
SHEET 1 C 6 THR L 53 LEU L 54 0
SHEET 2 C 6 GLN L 45 TYR L 49 -1 N TYR L 49 O THR L 53
SHEET 3 C 6 LEU L 33 GLN L 38 -1 N TRP L 35 O LEU L 47
SHEET 4 C 6 GLY L 84 HIS L 90 -1 O GLN L 89 N ALA L 34
SHEET 5 C 6 THR L 102 LEU L 106 -1 O LEU L 104 N GLY L 84
SHEET 6 C 6 SER L 10 ALA L 13 1 N LEU L 11 O GLU L 105
SHEET 1 D 4 THR L 114 PHE L 118 0
SHEET 2 D 4 GLY L 129 PHE L 139 -1 O VAL L 133 N PHE L 118
SHEET 3 D 4 TYR L 173 THR L 182 -1 O MET L 175 N LEU L 136
SHEET 4 D 4 VAL L 159 TRP L 163 -1 N LEU L 160 O THR L 178
SHEET 1 E 4 SER L 153 ARG L 155 0
SHEET 2 E 4 ILE L 144 ILE L 150 -1 N ILE L 150 O SER L 153
SHEET 3 E 4 SER L 191 HIS L 198 -1 O GLU L 195 N LYS L 147
SHEET 4 E 4 ILE L 205 ASN L 210 -1 O ILE L 205 N ALA L 196
SHEET 1 F 4 LYS H 3 GLU H 6 0
SHEET 2 F 4 VAL H 18 SER H 25 -1 O LYS H 23 N LEU H 5
SHEET 3 F 4 THR H 77 LEU H 82 -1 O LEU H 82 N VAL H 18
SHEET 4 F 4 ALA H 67 ASP H 72 -1 N ASP H 72 O THR H 77
SHEET 1 G 5 THR H 57 TYR H 59 0
SHEET 2 G 5 GLU H 46 ILE H 51 -1 N TYR H 50 O LYS H 58
SHEET 3 G 5 MET H 34 GLN H 39 -1 N TRP H 36 O ILE H 48
SHEET 4 G 5 ALA H 88 ARG H 94 -1 O VAL H 93 N HIS H 35
SHEET 5 G 5 TYR H 102 TRP H 103 -1 O TYR H 102 N ARG H 94
SHEET 1 H 6 THR H 57 TYR H 59 0
SHEET 2 H 6 GLU H 46 ILE H 51 -1 N TYR H 50 O LYS H 58
SHEET 3 H 6 MET H 34 GLN H 39 -1 N TRP H 36 O ILE H 48
SHEET 4 H 6 ALA H 88 ARG H 94 -1 O VAL H 93 N HIS H 35
SHEET 5 H 6 THR H 107 VAL H 111 -1 O THR H 107 N TYR H 90
SHEET 6 H 6 GLU H 10 VAL H 12 1 N GLU H 10 O THR H 110
SHEET 1 I 4 SER H 120 LEU H 124 0
SHEET 2 I 4 MET H 135 TYR H 145 -1 O LEU H 141 N TYR H 122
SHEET 3 I 4 LEU H 174 PRO H 184 -1 O TYR H 175 N TYR H 145
SHEET 4 I 4 VAL H 163 THR H 165 -1 N HIS H 164 O SER H 180
SHEET 1 J 4 SER H 120 LEU H 124 0
SHEET 2 J 4 MET H 135 TYR H 145 -1 O LEU H 141 N TYR H 122
SHEET 3 J 4 LEU H 174 PRO H 184 -1 O TYR H 175 N TYR H 145
SHEET 4 J 4 VAL H 169 GLN H 171 -1 N VAL H 169 O THR H 176
SHEET 1 K 3 THR H 151 TRP H 154 0
SHEET 2 K 3 THR H 194 HIS H 199 -1 O ASN H 196 N THR H 153
SHEET 3 K 3 THR H 204 LYS H 209 -1 O VAL H 206 N VAL H 197
SHEET 1 L 4 MET A 4 SER A 7 0
SHEET 2 L 4 VAL A 19 ALA A 25 -1 O THR A 22 N SER A 7
SHEET 3 L 4 GLN A 70 ILE A 75 -1 O LEU A 73 N ILE A 21
SHEET 4 L 4 PHE A 62 SER A 67 -1 N SER A 63 O LYS A 74
SHEET 1 M 6 SER A 10 ALA A 13 0
SHEET 2 M 6 THR A 102 LEU A 106 1 O GLU A 105 N LEU A 11
SHEET 3 M 6 GLY A 84 HIS A 90 -1 N GLY A 84 O LEU A 104
SHEET 4 M 6 LEU A 33 GLN A 38 -1 N GLN A 38 O SER A 85
SHEET 5 M 6 GLN A 45 TYR A 49 -1 O LEU A 47 N TRP A 35
SHEET 6 M 6 THR A 53 LEU A 54 -1 O THR A 53 N TYR A 49
SHEET 1 N 4 THR A 114 PHE A 118 0
SHEET 2 N 4 GLY A 129 PHE A 139 -1 O VAL A 133 N PHE A 118
SHEET 3 N 4 TYR A 173 THR A 182 -1 O TYR A 173 N PHE A 139
SHEET 4 N 4 VAL A 159 TRP A 163 -1 N LEU A 160 O THR A 178
SHEET 1 O 4 SER A 153 GLU A 154 0
SHEET 2 O 4 ASN A 145 ILE A 150 -1 N ILE A 150 O SER A 153
SHEET 3 O 4 SER A 191 THR A 197 -1 O THR A 197 N ASN A 145
SHEET 4 O 4 ILE A 205 ASN A 210 -1 O ILE A 205 N ALA A 196
SHEET 1 P 4 LYS B 3 GLU B 6 0
SHEET 2 P 4 VAL B 18 SER B 25 -1 O SER B 25 N LYS B 3
SHEET 3 P 4 THR B 77 LEU B 82 -1 O LEU B 82 N VAL B 18
SHEET 4 P 4 ALA B 67 ASP B 72 -1 N THR B 70 O TYR B 79
SHEET 1 Q 4 THR B 57 TYR B 59 0
SHEET 2 Q 4 LEU B 45 ILE B 51 -1 N TYR B 50 O LYS B 58
SHEET 3 Q 4 MET B 34 GLN B 39 -1 N MET B 34 O ILE B 51
SHEET 4 Q 4 ALA B 88 GLY B 96 -1 O VAL B 93 N HIS B 35
SHEET 1 R 6 THR B 57 TYR B 59 0
SHEET 2 R 6 LEU B 45 ILE B 51 -1 N TYR B 50 O LYS B 58
SHEET 3 R 6 MET B 34 GLN B 39 -1 N MET B 34 O ILE B 51
SHEET 4 R 6 ALA B 88 GLY B 96 -1 O VAL B 93 N HIS B 35
SHEET 5 R 6 THR B 107 VAL B 111 -1 O VAL B 109 N ALA B 88
SHEET 6 R 6 GLU B 10 VAL B 12 1 N GLU B 10 O SER B 108
SHEET 1 S 4 SER B 120 LEU B 124 0
SHEET 2 S 4 MET B 135 TYR B 145 -1 O LEU B 141 N TYR B 122
SHEET 3 S 4 TYR B 175 PRO B 184 -1 O LEU B 177 N VAL B 142
SHEET 4 S 4 VAL B 163 THR B 165 -1 N HIS B 164 O SER B 180
SHEET 1 T 4 SER B 120 LEU B 124 0
SHEET 2 T 4 MET B 135 TYR B 145 -1 O LEU B 141 N TYR B 122
SHEET 3 T 4 TYR B 175 PRO B 184 -1 O LEU B 177 N VAL B 142
SHEET 4 T 4 VAL B 169 LEU B 170 -1 N VAL B 169 O THR B 176
SHEET 1 U 3 THR B 151 TRP B 154 0
SHEET 2 U 3 THR B 194 HIS B 199 -1 O ASN B 196 N THR B 153
SHEET 3 U 3 THR B 204 LYS B 209 -1 O VAL B 206 N VAL B 197
SSBOND 1 CYS L 23 CYS L 88 1555 1555 2.06
SSBOND 2 CYS L 134 CYS L 194 1555 1555 2.05
SSBOND 3 CYS H 22 CYS H 92 1555 1555 2.04
SSBOND 4 CYS H 140 CYS H 195 1555 1555 2.08
SSBOND 5 CYS A 23 CYS A 88 1555 1555 2.05
SSBOND 6 CYS A 134 CYS A 194 1555 1555 2.05
SSBOND 7 CYS B 22 CYS B 92 1555 1555 2.04
SSBOND 8 CYS B 140 CYS B 195 1555 1555 2.08
CISPEP 1 SER L 7 PRO L 8 0 -0.28
CISPEP 2 THR L 94 PRO L 95 0 -0.22
CISPEP 3 TYR L 140 PRO L 141 0 0.19
CISPEP 4 PHE H 146 PRO H 147 0 -0.43
CISPEP 5 GLU H 148 PRO H 149 0 -0.12
CISPEP 6 TRP H 188 PRO H 189 0 0.42
CISPEP 7 SER A 7 PRO A 8 0 -0.35
CISPEP 8 THR A 94 PRO A 95 0 -0.21
CISPEP 9 TYR A 140 PRO A 141 0 0.11
CISPEP 10 ARG B 98 PRO B 99 0 0.07
CISPEP 11 PHE B 146 PRO B 147 0 -0.78
CISPEP 12 GLU B 148 PRO B 149 0 -0.43
CISPEP 13 TRP B 188 PRO B 189 0 0.71
SITE 1 AC1 7 GLU A 185 ARG A 188 HIS A 189 HOH A 458
SITE 2 AC1 7 PRO B 14 THR B 83 SER B 84
CRYST1 171.840 171.840 144.568 90.00 90.00 120.00 P 65 2 2 24
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 0.005819 0.003360 0.000000 0.00000
SCALE2 0.000000 0.006720 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006917 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
