HEADER IMMUNE SYSTEM 02-MAY-03 1P7K TITLE CRYSTAL STRUCTURE OF AN ANTI-SSDNA ANTIGEN-BINDING FRAGMENT TITLE 2 (FAB) BOUND TO 4-(2-HYDROXYETHYL)PIPERAZINE-1- TITLE 3 ETHANESULFONIC ACID (HEPES) COMPND MOL_ID: 1; COMPND 2 MOLECULE: ANTIBODY LIGHT CHAIN FAB; COMPND 3 CHAIN: L, A; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: ANTIBODY HEAVY CHAIN FAB; COMPND 7 CHAIN: H, B; COMPND 8 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 3 ORGANISM_COMMON: MOUSE; SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 5 EXPRESSION_SYSTEM_COMMON: BACTERIA; SOURCE 6 EXPRESSION_SYSTEM_STRAIN: DH12S; SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PCOMB3/6-HIS; SOURCE 9 MOL_ID: 2; SOURCE 10 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 11 ORGANISM_COMMON: MOUSE; SOURCE 12 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 13 EXPRESSION_SYSTEM_COMMON: BACTERIA; SOURCE 14 EXPRESSION_SYSTEM_STRAIN: DH12S; SOURCE 15 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 16 EXPRESSION_SYSTEM_PLASMID: PCOMB3/6-HIS KEYWDS FAB, ANTIBODY, ANTI-DNA ANTIBODY, AUTOANTIBODY, LUPUS, HEPES EXPDTA X-RAY DIFFRACTION AUTHOR J.P.SCHUERMANN,M.T.HENZL,S.L.DEUTSCHER,J.J.TANNER REVDAT 2 14-SEP-04 1P7K 1 AUTHOR JRNL REVDAT 1 11-MAY-04 1P7K 0 JRNL AUTH J.P.SCHUERMANN,M.T.HENZL,S.L.DEUTSCHER,J.J.TANNER JRNL TITL STRUCTURE OF AN ANTI-DNA FAB COMPLEXED WITH A JRNL TITL 2 NON-DNA LIGAND PROVIDES INSIGHTS INTO JRNL TITL 3 CROSS-REACTIVITY AND MOLECULAR MIMICRY. JRNL REF PROTEINS: STRUCT., FUNCT., V. 57 269 2004 JRNL REF 2 GENET. JRNL REFN ASTM PSFGEY US ISSN 0887-3585 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH J.J.TANNER,A.A.KOMISSAROV,S.L.DEUTSCHER REMARK 1 TITL CRYSTAL STRUCTURE OF AN ANTIGEN-BINDING FRAGMENT REMARK 1 TITL 2 BOUND TO SINGLE-STRANDED DNA REMARK 1 REF J.MOL.BIOL. V. 314 807 2001 REMARK 1 REFN ASTM JMOBAK UK ISSN 0022-2836 REMARK 1 REFERENCE 2 REMARK 1 AUTH S.P.PREWITT,A.A.KOMISSAROV,S.L.DEUTSCHER,J.J.TANNER REMARK 1 TITL CRYSTALLIZATION AND MOLECULAR REPLACEMENT STUDIES REMARK 1 TITL 2 OF A RECOMBINANT ANTIGEN-BINDING FRAGMENT REMARK 1 TITL 3 COMPLEXED WITH SINGLE-STRANDED DNA REMARK 1 REF ACTA CRYSTALLOGR.,SECT.D V. 56 1007 2000 REMARK 1 REFN ASTM ABCRE6 DK ISSN 0907-4449 REMARK 2 REMARK 2 RESOLUTION. 1.75 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : CNS 1.1 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) : 1.75 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 48.14 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) (%) : 93.4 REMARK 3 NUMBER OF REFLECTIONS : 97936 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) : 0.197 REMARK 3 FREE R VALUE : 0.230 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.000 REMARK 3 FREE R VALUE TEST SET COUNT : 9796 REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.002 REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : 10 REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.75 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.81 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 94.10 REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 8668 REMARK 3 BIN R VALUE (WORKING SET) : 0.2940 REMARK 3 BIN FREE R VALUE : 0.3160 REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 10.30 REMARK 3 BIN FREE R VALUE TEST SET COUNT : 992 REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.010 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 6545 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 139 REMARK 3 SOLVENT ATOMS : 881 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 21.30 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 28.50 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 1.15000 REMARK 3 B22 (A**2) : 0.75000 REMARK 3 B33 (A**2) : -1.90000 REMARK 3 B12 (A**2) : 0.00000 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) : 0.21 REMARK 3 ESD FROM SIGMAA (A) : 0.19 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) : 0.24 REMARK 3 ESD FROM C-V SIGMAA (A) : 0.21 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. REMARK 3 BOND LENGTHS (A) : 0.010 REMARK 3 BOND ANGLES (DEGREES) : 1.70 REMARK 3 DIHEDRAL ANGLES (DEGREES) : 27.70 REMARK 3 IMPROPER ANGLES (DEGREES) : 0.96 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) : 1.380 ; 1.500 REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.120 ; 2.000 REMARK 3 SIDE-CHAIN BOND (A**2) : 2.160 ; 2.000 REMARK 3 SIDE-CHAIN ANGLE (A**2) : 3.160 ; 2.500 REMARK 3 REMARK 3 BULK SOLVENT MODELING. REMARK 3 METHOD USED : FLAT MODEL REMARK 3 KSOL : 0.37 REMARK 3 BSOL : 55.30 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 : WATER_REP.PARAM REMARK 3 PARAMETER FILE 3 : ION.PARAM REMARK 3 PARAMETER FILE 4 : MOL3.PARAM REMARK 3 PARAMETER FILE 5 : NULL REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP REMARK 3 TOPOLOGY FILE 2 : MOL3.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 1P7K COMPLIES WITH FORMAT V. 3.0, 1-DEC-2006 REMARK 4 REMARK 4 THIS IS THE REMEDIATED VERSION OF THIS PDB ENTRY. REMARK 4 REMEDIATED DATA FILE REVISION 3.101 (2007-05-29) REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB. REMARK 100 THE RCSB ID CODE IS RCSB019106. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 27-JUL-2000; 22-APR-2001 REMARK 200 TEMPERATURE (KELVIN) : 173; 173 REMARK 200 PH : 8.10 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : N; Y REMARK 200 RADIATION SOURCE : ROTATING ANODE; NSLS REMARK 200 BEAMLINE : NULL; X8C REMARK 200 X-RAY GENERATOR MODEL : RIGAKU RUH3R REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M; M REMARK 200 WAVELENGTH OR RANGE (A) : 1.54; 0.97950 REMARK 200 MONOCHROMATOR : MIRRORS; NSLS X8C BEAMLINE REMARK 200 OPTICS REMARK 200 OPTICS : OSMIC MAXFLUX CONFOCAL REMARK 200 OPTICS; NSLS X8C BEAMLINE REMARK 200 OPTICS REMARK 200 REMARK 200 DETECTOR TYPE : IMAGE PLATE; CCD REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IV; ADSC QUANTUM REMARK 200 4 REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000 REMARK 200 DATA SCALING SOFTWARE : SCALEPACK REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 98022 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.750 REMARK 200 RESOLUTION RANGE LOW (A) : 48.140 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 93.5 REMARK 200 DATA REDUNDANCY : 3.500 REMARK 200 R MERGE (I) : 0.04400 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 21.7000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.75 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.81 REMARK 200 COMPLETENESS FOR SHELL (%) : 94.1 REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : 0.48700 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 2.100 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 REMARK 200 STARTING MODEL: 1I8M REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 54.30 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.69 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: AMMONIUM SULFATE, HEPES, PEG 400, REMARK 280 PH 8.1, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 295K 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 1/2-X,1/2+Y,-Z REMARK 290 4555 1/2+X,1/2-Y,-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 53.83300 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 78.35150 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 53.83300 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 78.35150 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 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT REMARK 300 WHICH CONSISTS OF 4 CHAIN(S). SEE REMARK 350 FOR REMARK 300 INFORMATION ON GENERATING THE BIOLOGICAL MOLECULE(S). REMARK 350 REMARK 350 GENERATING THE BIOMOLECULE 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 APPLY THE FOLLOWING TO CHAINS: 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 BIOMOLECULE: 2 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 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 S SO4 801 LIES ON A SPECIAL POSITION. REMARK 375 S SO4 802 LIES ON A SPECIAL POSITION. 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 GLN H 131 REMARK 465 THR H 132 REMARK 465 THR H 216 REMARK 465 SER H 217 REMARK 465 ALA B 129 REMARK 465 ALA B 130 REMARK 465 GLN B 131 REMARK 465 THR B 132 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 GLN L 3 CD OE1 NE2 REMARK 470 LYS L 52 CE NZ REMARK 470 LYS L 103 CD CE NZ REMARK 470 ASN L 157 CB CG OD1 ND2 REMARK 470 LYS L 169 CG CD CE NZ REMARK 470 ASN L 212 CB CG OD1 ND2 REMARK 470 GLU L 213 O CB CG CD OE1 OE2 REMARK 470 GLN H 1 N REMARK 470 GLU H 61 CD OE1 OE2 REMARK 470 ARG H 98 CG CD NE CZ NH1 NH2 REMARK 470 ALA H 130 C O REMARK 470 GLN H 171 CG CD OE1 NE2 REMARK 470 LYS H 209 CD CE NZ REMARK 470 ASP H 214 CB CG OD1 OD2 REMARK 470 CYS H 215 O SG REMARK 470 GLN A 3 CD OE1 NE2 REMARK 470 ARG A 24 NE CZ NH1 NH2 REMARK 470 TYR A 30 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 GLU A 56 CG CD OE1 OE2 REMARK 470 GLU A 81 CD OE1 OE2 REMARK 470 LYS A 107 CD CE NZ REMARK 470 LYS A 147 CE NZ REMARK 470 ASN A 157 CG OD1 ND2 REMARK 470 LYS A 169 CG CD CE NZ REMARK 470 ASN A 212 O CG OD1 ND2 REMARK 470 GLU A 213 O CB CG CD OE1 OE2 REMARK 470 CYS A 214 O SG REMARK 470 GLN B 1 OE1 NE2 REMARK 470 LYS B 13 CE NZ REMARK 470 LYS B 64 CD CE NZ REMARK 470 ARG B 98 CG CD NE CZ NH1 NH2 REMARK 470 SER B 128 O CB OG REMARK 470 ASN B 133 CB CG OD1 ND2 REMARK 470 GLU B 191 CG CD OE1 OE2 REMARK 470 LYS B 209 CD CE NZ REMARK 470 ASP B 214 O CB CG OD1 OD2 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS REMARK 500 REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15 REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375 REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS. REMARK 500 REMARK 500 DISTANCE CUTOFF: REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE REMARK 500 S SO4 801 O2 SO4 801 2655 1.46 REMARK 500 S SO4 801 O1 SO4 801 2655 1.47 REMARK 500 S SO4 802 O4 SO4 802 2655 1.47 REMARK 500 S SO4 801 O4 SO4 801 2655 1.48 REMARK 500 S SO4 802 O1 SO4 802 2655 1.48 REMARK 500 S SO4 802 O3 SO4 802 2655 1.48 REMARK 500 S SO4 802 O2 SO4 802 2655 1.48 REMARK 500 S SO4 801 O3 SO4 801 2655 1.49 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS 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,2(A3,1X,A1,I4,A1,1X,A4,3X),F6.3) REMARK 500 REMARK 500 EXPECTED VALUES: ENGH AND HUBER, 1991 REMARK 500 REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION REMARK 500 ILE L 117 CG1 ILE L 117 CD1 0.088 REMARK 500 PRO H 99 CB PRO H 99 CG 0.067 REMARK 500 MET H 100C CG MET H 100C SD -0.105 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: ENGH AND HUBER, 1991 REMARK 500 REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3 REMARK 500 THR L 114 N - CA - C ANGL. DEV. =-12.3 DEGREES REMARK 500 LEU L 136 N - CA - C ANGL. DEV. =-11.0 DEGREES REMARK 500 CYS L 194 N - CA - C ANGL. DEV. =-10.2 DEGREES REMARK 500 ILE L 205 N - CA - C ANGL. DEV. =-10.3 DEGREES REMARK 500 CYS H 92 N - CA - C ANGL. DEV. =-13.4 DEGREES REMARK 500 ALA H 100B N - CA - C ANGL. DEV. =-10.2 DEGREES REMARK 500 SER H 120 N - CA - C ANGL. DEV. =-12.3 DEGREES REMARK 500 LEU H 177 CA - CB - CG ANGL. DEV. = 11.5 DEGREES REMARK 500 CYS H 195 CA - CB - SG ANGL. DEV. = 12.1 DEGREES REMARK 500 THR A 114 N - CA - C ANGL. DEV. =-11.1 DEGREES REMARK 500 LEU A 136 N - CA - C ANGL. DEV. =-11.7 DEGREES REMARK 500 ILE A 205 N - CA - C ANGL. DEV. =-10.8 DEGREES REMARK 500 ASN B 60 N - CA - C ANGL. DEV. =-10.9 DEGREES REMARK 500 CYS B 92 N - CA - C ANGL. DEV. =-13.6 DEGREES REMARK 500 PRO B 99 C - N - CA ANGL. DEV. = 10.4 DEGREES REMARK 500 ALA B 100B N - CA - C ANGL. DEV. =-11.1 DEGREES REMARK 500 SER B 120 N - CA - C ANGL. DEV. =-12.5 DEGREES REMARK 500 LYS B 143 N - CA - C ANGL. DEV. = 10.4 DEGREES REMARK 500 CYS B 195 CA - CB - SG ANGL. DEV. = 10.9 DEGREES 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 M RES CSSEQI PSI PHI REMARK 500 ALA L 51 -32.40 62.94 REMARK 500 ALA A 51 -34.39 70.12 REMARK 525 REMARK 525 SOLVENT REMARK 525 THE FOLLOWING SOLVENT MOLECULES LIE FARTHER THAN EXPECTED REMARK 525 FROM THE PROTEIN OR NUCLEIC ACID MOLECULE AND MAY BE REMARK 525 ASSOCIATED WITH A SYMMETRY RELATED MOLECULE (M=MODEL REMARK 525 NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE REMARK 525 NUMBER; I=INSERTION CODE): REMARK 525 REMARK 525 M RES CSSEQI REMARK 525 HOH 580 DISTANCE = 5.36 ANGSTROMS REMARK 525 HOH 612 DISTANCE = 5.62 ANGSTROMS REMARK 525 HOH 638 DISTANCE = 6.01 ANGSTROMS REMARK 525 HOH 655 DISTANCE = 5.21 ANGSTROMS REMARK 525 HOH 664 DISTANCE = 5.28 ANGSTROMS REMARK 525 HOH 673 DISTANCE = 7.03 ANGSTROMS REMARK 525 HOH 687 DISTANCE = 5.04 ANGSTROMS REMARK 525 HOH 716 DISTANCE = 5.56 ANGSTROMS REMARK 525 HOH 747 DISTANCE = 5.41 ANGSTROMS REMARK 525 HOH 750 DISTANCE = 5.81 ANGSTROMS REMARK 525 HOH 758 DISTANCE = 5.36 ANGSTROMS REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1I8M RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF A RECOMBINANT ANTI-SINGLE-STRANDED DNA REMARK 900 ANTIBODY FRAGMENT COMPLEXED WITH DT5 DBREF 1P7K L 1 214 UNP Q8VCP0 Q8VCP0 25 234 DBREF 1P7K H 5 217 UNP Q9JL75 Q9JL75_MOUSE 1 109 DBREF 1P7K A 1 214 UNP Q8VCP0 Q8VCP0 25 234 DBREF 1P7K B 5 217 UNP Q9JL75 Q9JL75_MOUSE 1 109 SEQADV 1P7K GLN H 1 UNP Q9JL75 CLONING ARTIFACT SEQADV 1P7K VAL H 2 UNP Q9JL75 CLONING ARTIFACT SEQADV 1P7K LYS H 3 UNP Q9JL75 CLONING ARTIFACT SEQADV 1P7K LEU H 4 UNP Q9JL75 CLONING ARTIFACT SEQADV 1P7K PRO H 52A UNP Q9JL75 INSERTION SEQADV 1P7K SER H 82A UNP Q9JL75 INSERTION SEQADV 1P7K SER H 82B UNP Q9JL75 INSERTION SEQADV 1P7K LEU H 82C UNP Q9JL75 INSERTION SEQADV 1P7K TYR H 100A UNP Q9JL75 INSERTION SEQADV 1P7K ALA H 100B UNP Q9JL75 INSERTION SEQADV 1P7K MET H 100C UNP Q9JL75 INSERTION SEQADV 1P7K GLN B 1 UNP Q9JL75 CLONING ARTIFACT SEQADV 1P7K VAL B 2 UNP Q9JL75 CLONING ARTIFACT SEQADV 1P7K LYS B 3 UNP Q9JL75 CLONING ARTIFACT SEQADV 1P7K LEU B 4 UNP Q9JL75 CLONING ARTIFACT SEQADV 1P7K PRO B 52A UNP Q9JL75 INSERTION SEQADV 1P7K SER B 82A UNP Q9JL75 INSERTION SEQADV 1P7K SER B 82B UNP Q9JL75 INSERTION SEQADV 1P7K LEU B 82C UNP Q9JL75 INSERTION SEQADV 1P7K TYR B 100A UNP Q9JL75 INSERTION SEQADV 1P7K ALA B 100B UNP Q9JL75 INSERTION SEQADV 1P7K MET B 100C UNP Q9JL75 INSERTION 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 801 5 HET SO4 802 5 HET SO4 803 5 HET SO4 804 5 HET SO4 805 5 HET SO4 806 5 HET SO4 807 5 HET SO4 808 5 HET SO4 809 5 HET EPE 901 15 HET EPE 902 15 HET 1PE 1001 16 HET 1PE 1002 16 HET 1PE 1003 16 HET 1PE 1004 16 HET PEG 1201 7 HET PEG 1202 7 HET GOL 1101 6 HET GOL 1102 6 HET GOL 1103 6 HET GOL 1105 6 HET GOL 1106 6 HET GOL 1107 6 HET GOL 1108 6 HET GOL 1110 6 HET GOL 1111 6 HET GOL 1112 6 HET GOL 1115 6 HET GOL 1116 6 HET GOL 1117 6 HET GOL 1118 6 HET GOL 1119 6 HET GOL 1120 6 HETNAM SO4 SULFATE ION HETNAM EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID HETNAM 1PE PENTAETHYLENE GLYCOL HETNAM PEG DI(HYDROXYETHYL)ETHER HETNAM GOL GLYCEROL HETSYN EPE HEPES HETSYN 1PE PEG400 FORMUL 5 SO4 9(O4 S 2-) FORMUL 14 EPE 2(C8 H18 N2 O4 S) FORMUL 16 1PE 4(C10 H22 O6) FORMUL 20 PEG 2(C4 H10 O3) FORMUL 22 GOL 16(C3 H8 O3) FORMUL 38 HOH *771(H2 O) HELIX 1 1 GLN L 79 PHE L 83 5 5 HELIX 2 2 SER L 121 SER L 127 1 7 HELIX 3 3 LYS L 183 HIS L 189 1 7 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 LYS H 73 SER H 75 5 3 HELIX 7 7 THR H 83 SER H 87 5 5 HELIX 8 8 SER H 156 SER H 158 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 HIS A 189 1 7 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 LYS B 73 SER B 75 5 3 HELIX 16 16 THR B 83 SER B 87 5 5 HELIX 17 17 SER B 156 SER B 158 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 ARG L 24 N THR L 5 SHEET 3 A 4 GLN L 70 ILE L 75 -1 O LEU L 73 N ILE L 21 SHEET 4 A 4 PHE L 62 GLY L 66 -1 N SER L 63 O LYS L 74 SHEET 1 B 6 SER L 10 ALA L 13 0 SHEET 2 B 6 THR L 102 LEU L 106 1 O GLU L 105 N LEU L 11 SHEET 3 B 6 GLY L 84 HIS L 90 -1 N GLY L 84 O LEU L 104 SHEET 4 B 6 LEU L 33 GLN L 38 -1 N ALA L 34 O GLN L 89 SHEET 5 B 6 GLN L 45 TYR L 49 -1 O LEU L 47 N TRP L 35 SHEET 6 B 6 THR L 53 LEU L 54 -1 O THR L 53 N TYR L 49 SHEET 1 C 4 THR L 114 PHE L 118 0 SHEET 2 C 4 GLY L 129 PHE L 139 -1 O ASN L 137 N THR L 114 SHEET 3 C 4 TYR L 173 THR L 182 -1 O MET L 175 N LEU L 136 SHEET 4 C 4 VAL L 159 TRP L 163 -1 N LEU L 160 O THR L 178 SHEET 1 D 4 SER L 153 ARG L 155 0 SHEET 2 D 4 ASN L 145 ILE L 150 -1 N TRP L 148 O ARG L 155 SHEET 3 D 4 SER L 191 THR L 197 -1 O GLU L 195 N LYS L 147 SHEET 4 D 4 ILE L 205 ASN L 210 -1 O ILE L 205 N ALA L 196 SHEET 1 E 4 LYS H 3 GLU H 6 0 SHEET 2 E 4 VAL H 18 SER H 25 -1 O LYS H 23 N LEU H 5 SHEET 3 E 4 THR H 77 LEU H 82 -1 O MET H 80 N MET H 20 SHEET 4 E 4 ALA H 67 ASP H 72 -1 N ASP H 72 O THR H 77 SHEET 1 F 6 GLU H 10 VAL H 12 0 SHEET 2 F 6 THR H 107 VAL H 111 1 O SER H 108 N GLU H 10 SHEET 3 F 6 ALA H 88 GLY H 95 -1 N ALA H 88 O VAL H 109 SHEET 4 F 6 MET H 34 GLN H 39 -1 N HIS H 35 O VAL H 93 SHEET 5 F 6 LEU H 45 ILE H 51 -1 O GLU H 46 N LYS H 38 SHEET 6 F 6 THR H 57 TYR H 59 -1 O LYS H 58 N TYR H 50 SHEET 1 G 4 GLU H 10 VAL H 12 0 SHEET 2 G 4 THR H 107 VAL H 111 1 O SER H 108 N GLU H 10 SHEET 3 G 4 ALA H 88 GLY H 95 -1 N ALA H 88 O VAL H 109 SHEET 4 G 4 MET H 100C TRP H 103 -1 O TYR H 102 N ARG H 94 SHEET 1 H 4 SER H 120 LEU H 124 0 SHEET 2 H 4 MET H 135 TYR H 145 -1 O LEU H 141 N TYR H 122 SHEET 3 H 4 LEU H 174 PRO H 184 -1 O VAL H 183 N VAL H 136 SHEET 4 H 4 VAL H 163 THR H 165 -1 N HIS H 164 O SER H 180 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 VAL H 183 N VAL H 136 SHEET 4 I 4 VAL H 169 GLN H 171 -1 N GLN H 171 O LEU H 174 SHEET 1 J 3 THR H 151 TRP H 154 0 SHEET 2 J 3 THR H 194 HIS H 199 -1 O ASN H 196 N THR H 153 SHEET 3 J 3 THR H 204 LYS H 209 -1 O VAL H 206 N VAL H 197 SHEET 1 K 4 MET A 4 SER A 7 0 SHEET 2 K 4 VAL A 19 ALA A 25 -1 O ARG A 24 N THR A 5 SHEET 3 K 4 GLN A 70 ILE A 75 -1 O ILE A 75 N VAL A 19 SHEET 4 K 4 PHE A 62 SER A 67 -1 N SER A 63 O LYS A 74 SHEET 1 L 6 SER A 10 ALA A 13 0 SHEET 2 L 6 THR A 102 LEU A 106 1 O GLU A 105 N LEU A 11 SHEET 3 L 6 GLY A 84 HIS A 90 -1 N GLY A 84 O LEU A 104 SHEET 4 L 6 LEU A 33 GLN A 38 -1 N ALA A 34 O GLN A 89 SHEET 5 L 6 GLN A 45 TYR A 49 -1 O LEU A 47 N TRP A 35 SHEET 6 L 6 THR A 53 LEU A 54 -1 O THR A 53 N TYR A 49 SHEET 1 M 4 THR A 114 PHE A 118 0 SHEET 2 M 4 GLY A 129 PHE A 139 -1 O ASN A 137 N THR A 114 SHEET 3 M 4 TYR A 173 THR A 182 -1 O LEU A 179 N VAL A 132 SHEET 4 M 4 VAL A 159 TRP A 163 -1 N SER A 162 O SER A 176 SHEET 1 N 4 SER A 153 ARG A 155 0 SHEET 2 N 4 ILE A 144 ILE A 150 -1 N ILE A 150 O SER A 153 SHEET 3 N 4 SER A 191 HIS A 198 -1 O THR A 197 N ASN A 145 SHEET 4 N 4 ILE A 205 ASN A 210 -1 O LYS A 207 N CYS A 194 SHEET 1 O 4 LYS B 3 GLU B 6 0 SHEET 2 O 4 VAL B 18 SER B 25 -1 O LYS B 23 N LEU B 5 SHEET 3 O 4 THR B 77 LEU B 82 -1 O LEU B 82 N VAL B 18 SHEET 4 O 4 ALA B 67 ASP B 72 -1 N ASP B 72 O THR B 77 SHEET 1 P 6 GLU B 10 VAL B 12 0 SHEET 2 P 6 THR B 107 VAL B 111 1 O SER B 108 N GLU B 10 SHEET 3 P 6 ALA B 88 GLY B 95 -1 N ALA B 88 O VAL B 109 SHEET 4 P 6 MET B 34 GLN B 39 -1 N HIS B 35 O VAL B 93 SHEET 5 P 6 GLU B 46 ILE B 51 -1 O GLU B 46 N LYS B 38 SHEET 6 P 6 THR B 57 TYR B 59 -1 O LYS B 58 N TYR B 50 SHEET 1 Q 4 GLU B 10 VAL B 12 0 SHEET 2 Q 4 THR B 107 VAL B 111 1 O SER B 108 N GLU B 10 SHEET 3 Q 4 ALA B 88 GLY B 95 -1 N ALA B 88 O VAL B 109 SHEET 4 Q 4 MET B 100C TRP B 103 -1 O TYR B 102 N ARG B 94 SHEET 1 R 4 SER B 120 LEU B 124 0 SHEET 2 R 4 MET B 135 TYR B 145 -1 O LEU B 141 N TYR B 122 SHEET 3 R 4 LEU B 174 PRO B 184 -1 O TYR B 175 N TYR B 145 SHEET 4 R 4 VAL B 163 THR B 165 -1 N HIS B 164 O SER B 180 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 LEU B 174 PRO B 184 -1 O TYR B 175 N TYR B 145 SHEET 4 S 4 VAL B 169 GLN B 171 -1 N GLN B 171 O LEU B 174 SHEET 1 T 3 THR B 151 TRP B 154 0 SHEET 2 T 3 THR B 194 HIS B 199 -1 O ASN B 196 N THR B 153 SHEET 3 T 3 THR B 204 LYS B 209 -1 O VAL B 206 N VAL B 197 SSBOND 1 CYS L 23 CYS L 88 SSBOND 2 CYS L 134 CYS L 194 SSBOND 3 CYS H 22 CYS H 92 SSBOND 4 CYS H 140 CYS H 195 SSBOND 5 CYS A 23 CYS A 88 SSBOND 6 CYS A 134 CYS A 194 SSBOND 7 CYS B 22 CYS B 92 SSBOND 8 CYS B 140 CYS B 195 CISPEP 1 SER L 7 PRO L 8 0 0.05 CISPEP 2 THR L 94 PRO L 95 0 0.23 CISPEP 3 TYR L 140 PRO L 141 0 0.78 CISPEP 4 PHE H 146 PRO H 147 0 -0.48 CISPEP 5 GLU H 148 PRO H 149 0 0.27 CISPEP 6 TRP H 188 PRO H 189 0 0.73 CISPEP 7 SER A 7 PRO A 8 0 -0.54 CISPEP 8 THR A 94 PRO A 95 0 0.12 CISPEP 9 TYR A 140 PRO A 141 0 0.23 CISPEP 10 ARG B 98 PRO B 99 0 1.00 CISPEP 11 PHE B 146 PRO B 147 0 -0.03 CISPEP 12 GLU B 148 PRO B 149 0 0.11 CISPEP 13 TRP B 188 PRO B 189 0 0.32 CRYST1 107.666 156.703 61.003 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 0.009288 0.000000 0.000000 0.00000 SCALE2 0.000000 0.006381 0.000000 0.00000 SCALE3 0.000000 0.000000 0.016393 0.00000