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HEADER IMMUNE SYSTEM 03-AUG-01 1JPT TITLE CRYSTAL STRUCTURE OF FAB D3H44 COMPND MOL_ID: 1; COMPND 2 MOLECULE: IMMUNOGLOBULIN FAB D3H44, LIGHT CHAIN; COMPND 3 CHAIN: L; COMPND 4 FRAGMENT: FAB FRAGMENT; COMPND 5 ENGINEERED: YES; COMPND 6 MOL_ID: 2; COMPND 7 MOLECULE: IMMUNOGLOBULIN FAB D3H44, HEAVY CHAIN; COMPND 8 CHAIN: H; COMPND 9 FRAGMENT: FAB FRAGMENT; COMPND 10 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 5 EXPRESSION_SYSTEM_COMMON: BACTERIA; SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 7 EXPRESSION_SYSTEM_PLASMID: PEMX1; SOURCE 8 MOL_ID: 2; SOURCE 9 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 10 ORGANISM_COMMON: HUMAN; SOURCE 11 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 12 EXPRESSION_SYSTEM_COMMON: BACTERIA; SOURCE 13 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 14 EXPRESSION_SYSTEM_PLASMID: PEMX1 KEYWDS ANTIGEN-ANTIBODY RECOGNITION, HUMANIZED ANTIBODY, BLOOD KEYWDS 2 COAGULATION, CRYSTAL STRUCTURE EXPDTA X-RAY DIFFRACTION AUTHOR K.FAELBER,D.KIRCHHOFER,L.PRESTA,R.F.KELLEY,Y.A.MULLER REVDAT 2 18-DEC-02 1JPT 1 REMARK REVDAT 1 03-FEB-02 1JPT 0 JRNL AUTH K.FAELBER,D.KIRCHHOFER,L.PRESTA,R.F.KELLEY, JRNL AUTH 2 Y.A.MULLER JRNL TITL THE 1.85 A RESOLUTION CRYSTAL STRUCTURES OF TISSUE JRNL TITL 2 FACTOR IN COMPLEX WITH HUMANIZED FAB D3H44 AND OF JRNL TITL 3 FREE HUMANIZED FAB D3H44: REVISITING THE SOLVATION JRNL TITL 4 OF ANTIGEN COMBINING SITES. JRNL REF J.MOL.BIOL. V. 313 83 2001 JRNL REFN ASTM JMOBAK UK ISSN 0022-2836 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH L.PRESTA,P.SIMS,Y.G.MENG,P.MORAN,S.BULLENS, REMARK 1 AUTH 2 S.BUNTING,J.SCHOENFELD,D.LOWE,J.LAI,P.RANCATORE, REMARK 1 AUTH 3 M.IVERSON,A.LIM,V.CHISHOLM,R.F.KELLEY,M.RIEDERER, REMARK 1 AUTH 4 D.KIRCHHOFER REMARK 1 TITL GENERATION OF A HUMANIZED, HIGH AFFINITY REMARK 1 TITL 2 ANTI-TISSUE FACTOR ANTIBODY FOR USE AS A NOVEL REMARK 1 TITL 3 ANTITHROMBOTIC THERAPEUTIC REMARK 1 REF THROMB.HAEMOST. V. 85 379 2001 REMARK 1 REFN GW ISSN 0340-6245 REMARK 2 REMARK 2 RESOLUTION. 1.85 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) : 1.85 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 40.00 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) (%) : 99.2 REMARK 3 NUMBER OF REFLECTIONS : 36025 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) : 0.182 REMARK 3 FREE R VALUE : 0.228 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 7.095 REMARK 3 FREE R VALUE TEST SET COUNT : 2556 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) : 1.85 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.97 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.60 REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL REMARK 3 BIN R VALUE (WORKING SET) : 0.2420 REMARK 3 BIN FREE R VALUE : 0.2700 REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL REMARK 3 BIN FREE R VALUE TEST SET COUNT : 421 REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.013 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 3241 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 0 REMARK 3 SOLVENT ATOMS : 372 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 24.70 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 20.50 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : -2.90100 REMARK 3 B22 (A**2) : 1.53500 REMARK 3 B33 (A**2) : 1.36600 REMARK 3 B12 (A**2) : 0.00000 REMARK 3 B13 (A**2) : 2.90600 REMARK 3 B23 (A**2) : 0.00000 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) : 0.013 REMARK 3 BOND ANGLES (DEGREES) : 1.83 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 BULK SOLVENT MODELING. REMARK 3 METHOD USED : NULL REMARK 3 KSOL : NULL REMARK 3 BSOL : 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 1JPT 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 PDBJ . REMARK 100 THE RCSB ID CODE IS RCSB014045. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 10-DEC-1999 REMARK 200 TEMPERATURE (KELVIN) : 110.0 REMARK 200 PH : 4.60 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : ESRF REMARK 200 BEAMLINE : BM14 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.933 REMARK 200 MONOCHROMATOR : DIAMOND + GERMANIUM REMARK 200 OPTICS : MIRRORS REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MAR REMARK 200 DATA SCALING SOFTWARE : XDS REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 36063 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.850 REMARK 200 RESOLUTION RANGE LOW (A) : 40.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 96.3 REMARK 200 DATA REDUNDANCY : 3.400 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : 0.07700 REMARK 200 FOR THE DATA SET : 11.3000 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) : 1.90 REMARK 200 COMPLETENESS FOR SHELL (%) : 91.6 REMARK 200 DATA REDUNDANCY IN SHELL : 3.40 REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : 0.41600 REMARK 200 FOR SHELL : 2.800 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: COMPLEX D3H44 - TF REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 45.73 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.27 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: AMMONIUM SULPHATE, SODIUM ACETATE, REMARK 280 PH 4.6, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -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 39.10000 REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT REMARK 300 WHICH CONSISTS OF 2 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 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 SER H 132 REMARK 465 LYS H 133 REMARK 465 SER H 134 REMARK 465 THR H 135 REMARK 465 SER H 136 REMARK 465 LYS H 218 REMARK 465 SER H 219 REMARK 465 CYS H 220 REMARK 465 ASP H 221 REMARK 465 LYS H 222 REMARK 465 THR H 223 REMARK 465 HIS H 224 REMARK 465 THR H 225 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 MET L 4 SD MET L 4 CE -0.078 REMARK 500 PRO H 153 CB PRO H 153 CG 0.096 REMARK 500 GLN H 196 CB GLN H 196 CG -0.088 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 SER L 114 N - CA - C ANGL. DEV. =-12.6 DEGREES REMARK 500 SER H 124 N - CA - C ANGL. DEV. =-12.3 DEGREES REMARK 500 LEU H 128 N - CA - C ANGL. DEV. =-13.5 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 -38.86 63.11 REMARK 500 ALA H 101 -44.01 107.42 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1JPS RELATED DB: PDB REMARK 900 1JPS CONTAINS TISSUE FACTOR COMPLEXED WITH HUMANIZED FAB REMARK 900 D3H44 SEQRES 1 L 214 ASP ILE GLN MET THR GLN SER PRO SER SER LEU SER ALA SEQRES 2 L 214 SER VAL GLY ASP ARG VAL THR ILE THR CYS ARG ALA SER SEQRES 3 L 214 ARG ASP ILE LYS SER TYR LEU ASN TRP TYR GLN GLN LYS SEQRES 4 L 214 PRO GLY LYS ALA PRO LYS VAL LEU ILE TYR TYR ALA THR SEQRES 5 L 214 SER LEU ALA GLU GLY VAL PRO SER ARG PHE SER GLY SER SEQRES 6 L 214 GLY SER GLY THR ASP TYR THR LEU THR ILE SER SER LEU SEQRES 7 L 214 GLN PRO GLU ASP PHE ALA THR TYR TYR CYS LEU GLN HIS SEQRES 8 L 214 GLY GLU SER PRO TRP THR PHE GLY GLN GLY THR LYS VAL SEQRES 9 L 214 GLU ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE ILE SEQRES 10 L 214 PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR ALA SEQRES 11 L 214 SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG GLU SEQRES 12 L 214 ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SER SEQRES 13 L 214 GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER LYS SEQRES 14 L 214 ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SER SEQRES 15 L 214 LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS GLU SEQRES 16 L 214 VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SER SEQRES 17 L 214 PHE ASN ARG GLY GLU CYS SEQRES 1 H 225 GLU VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 H 225 PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 H 225 PHE ASN ILE LYS GLU TYR TYR MET HIS TRP VAL ARG GLN SEQRES 4 H 225 ALA PRO GLY LYS GLY LEU GLU TRP VAL GLY LEU ILE ASP SEQRES 5 H 225 PRO GLU GLN GLY ASN THR ILE TYR ASP PRO LYS PHE GLN SEQRES 6 H 225 ASP ARG ALA THR ILE SER ALA ASP ASN SER LYS ASN THR SEQRES 7 H 225 ALA TYR LEU GLN MET ASN SER LEU ARG ALA GLU ASP THR SEQRES 8 H 225 ALA VAL TYR TYR CYS ALA ARG ASP THR ALA ALA TYR PHE SEQRES 9 H 225 ASP TYR TRP GLY GLN GLY THR LEU VAL THR VAL SER SER SEQRES 10 H 225 ALA SER THR LYS GLY PRO SER VAL PHE PRO LEU ALA PRO SEQRES 11 H 225 SER SER LYS SER THR SER GLY GLY THR ALA ALA LEU GLY SEQRES 12 H 225 CYS LEU VAL LYS ASP TYR PHE PRO GLU PRO VAL THR VAL SEQRES 13 H 225 SER TRP ASN SER GLY ALA LEU THR SER GLY VAL HIS THR SEQRES 14 H 225 PHE PRO ALA VAL LEU GLN SER SER GLY LEU TYR SER LEU SEQRES 15 H 225 SER SER VAL VAL THR VAL PRO SER SER SER LEU GLY THR SEQRES 16 H 225 GLN THR TYR ILE CYS ASN VAL ASN HIS LYS PRO SER ASN SEQRES 17 H 225 THR LYS VAL ASP LYS LYS VAL GLU PRO LYS SER CYS ASP SEQRES 18 H 225 LYS THR HIS THR FORMUL 3 HOH *372(H2 O) HELIX 1 1 GLN L 79 PHE L 83 5 5 HELIX 2 2 GLU L 123 SER L 127 5 5 HELIX 3 3 LYS L 183 HIS L 189 1 7 HELIX 4 4 ASN H 28 TYR H 32 5 5 HELIX 5 5 ASN H 74 LYS H 76 5 3 HELIX 6 6 ARG H 87 THR H 91 5 5 HELIX 7 7 SER H 160 ALA H 162 5 3 HELIX 8 8 SER H 191 THR H 195 5 5 HELIX 9 9 LYS H 205 ASN H 208 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 ASP L 70 ILE L 75 -1 O LEU L 73 N ILE L 21 SHEET 4 A 4 PHE L 62 SER L 67 -1 N SER L 63 O THR L 74 SHEET 1 B 6 SER L 10 SER L 14 0 SHEET 2 B 6 THR L 102 LYS L 107 1 O LYS L 107 N ALA L 13 SHEET 3 B 6 ALA L 84 GLN L 90 -1 N ALA L 84 O VAL L 104 SHEET 4 B 6 LEU L 33 GLN L 38 0 SHEET 5 B 6 LYS L 45 TYR L 49 -1 O LEU L 47 N TRP L 35 SHEET 6 B 6 SER L 53 LEU L 54 -1 O SER L 53 N TYR L 49 SHEET 1 C 4 SER L 10 SER L 14 0 SHEET 2 C 4 THR L 102 LYS L 107 1 O LYS L 107 N ALA L 13 SHEET 3 C 4 ALA L 84 GLN L 90 -1 N ALA L 84 O VAL L 104 SHEET 4 C 4 THR L 97 PHE L 98 0 SHEET 1 D 4 SER L 114 PHE L 118 0 SHEET 2 D 4 THR L 129 PHE L 139 -1 O VAL L 133 N PHE L 118 SHEET 3 D 4 TYR L 173 SER L 182 -1 O LEU L 179 N VAL L 132 SHEET 4 D 4 SER L 159 VAL L 163 -1 N GLN L 160 O THR L 178 SHEET 1 E 4 ALA L 153 LEU L 154 0 SHEET 2 E 4 LYS L 145 VAL L 150 -1 N VAL L 150 O ALA L 153 SHEET 3 E 4 VAL L 191 THR L 197 -1 O GLU L 195 N GLN L 147 SHEET 4 E 4 VAL L 205 ASN L 210 -1 O VAL L 205 N VAL L 196 SHEET 1 F 4 GLN H 3 SER H 7 0 SHEET 2 F 4 LEU H 18 SER H 25 -1 O ALA H 23 N VAL H 5 SHEET 3 F 4 THR H 78 MET H 83 -1 O LEU H 81 N LEU H 20 SHEET 4 F 4 ALA H 68 ASP H 73 -1 N ASP H 73 O THR H 78 SHEET 1 G 5 THR H 58 TYR H 60 0 SHEET 2 G 5 LEU H 45 ILE H 51 -1 N LEU H 50 O ILE H 59 SHEET 3 G 5 TYR H 33 GLN H 39 -1 N TRP H 36 O VAL H 48 SHEET 4 G 5 ALA H 92 ASP H 99 -1 O TYR H 95 N VAL H 37 SHEET 5 G 5 PHE H 104 TRP H 107 0 SHEET 1 H 6 THR H 58 TYR H 60 0 SHEET 2 H 6 LEU H 45 ILE H 51 -1 N LEU H 50 O ILE H 59 SHEET 3 H 6 TYR H 33 GLN H 39 -1 N TRP H 36 O VAL H 48 SHEET 4 H 6 ALA H 92 ASP H 99 -1 O TYR H 95 N VAL H 37 SHEET 5 H 6 THR H 111 VAL H 115 0 SHEET 6 H 6 GLY H 10 VAL H 12 1 N VAL H 12 O THR H 114 SHEET 1 I 4 SER H 124 LEU H 128 0 SHEET 2 I 4 THR H 139 TYR H 149 -1 O LEU H 145 N PHE H 126 SHEET 3 I 4 TYR H 180 PRO H 189 -1 O LEU H 182 N VAL H 146 SHEET 4 I 4 VAL H 167 THR H 169 0 SHEET 1 J 4 SER H 124 LEU H 128 0 SHEET 2 J 4 THR H 139 TYR H 149 -1 O LEU H 145 N PHE H 126 SHEET 3 J 4 TYR H 180 PRO H 189 -1 O LEU H 182 N VAL H 146 SHEET 4 J 4 VAL H 173 LEU H 174 0 SHEET 1 K 3 THR H 155 TRP H 158 0 SHEET 2 K 3 TYR H 198 HIS H 204 -1 O ASN H 201 N SER H 157 SHEET 3 K 3 THR H 209 VAL H 215 -1 O VAL H 211 N VAL H 202 SSBOND 1 CYS L 23 CYS L 88 SSBOND 2 CYS L 134 CYS L 194 SSBOND 3 CYS H 22 CYS H 96 SSBOND 4 CYS H 144 CYS H 200 CISPEP 1 SER L 7 PRO L 8 0 -0.90 CISPEP 2 SER L 94 PRO L 95 0 -0.31 CISPEP 3 TYR L 140 PRO L 141 0 0.37 CISPEP 4 PHE H 150 PRO H 151 0 -0.47 CISPEP 5 GLU H 152 PRO H 153 0 0.55 CRYST1 49.120 78.200 58.920 90.00 107.61 90.00 P 1 21 1 2 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 0.020358 0.000000 0.006462 0.00000 SCALE2 0.000000 0.012788 0.000000 0.00000 SCALE3 0.000000 0.000000 0.017807 0.00000