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HEADER IMMUNOGLOBULIN 30-MAY-03 1OHQ TITLE CRYSTAL STRUCTURE OF HEL4, A SOLUBLE HUMAN VH ANTIBODY TITLE 2 DOMAIN RESISTANT TO AGGREGATION COMPND MOL_ID: 1; COMPND 2 MOLECULE: IMMUNOGLOBULIN; COMPND 3 CHAIN: A, B; COMPND 4 FRAGMENT: FV FRAGMENT, RESIDUES 1-120; COMPND 5 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 EXPRESSION_SYSTEM: PICHIA PASTORIS KEYWDS ANTIBODY, IMMUNE SYSTEM, FV FRAGMENT, HEL4, IMMUNOGLOBULIN EXPDTA X-RAY DIFFRACTION AUTHOR L.JESPERS,O.SCHON,L.C.JAMES,D.VEPRINTSEV,G.WINTER REVDAT 2 25-MAR-04 1OHQ 1 JRNL REVDAT 1 11-MAR-04 1OHQ 0 JRNL AUTH L.JESPERS,O.SCHON,L.C.JAMES,D.VEPRINTSEV,G.WINTER JRNL TITL CRYSTAL STRUCTURE OF HEL4, A SOLUBLE, REFOLDABLE JRNL TITL 2 HUMAN V(H) SINGLE DOMAIN WITH A GERM-LINE SCAFFOLD. JRNL REF J.MOL.BIOL. V. 337 893 2004 JRNL REFN ASTM JMOBAK UK ISSN 0022-2836 REMARK 1 REMARK 2 REMARK 2 RESOLUTION. 2.00 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : REFMAC REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 70.00 REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000 REMARK 3 COMPLETENESS FOR RANGE (%) : 99.0 REMARK 3 NUMBER OF REFLECTIONS : 19067 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT REMARK 3 FREE R VALUE TEST SET SELECTION : NULL REMARK 3 R VALUE (WORKING + TEST SET) : 0.182 REMARK 3 R VALUE (WORKING SET) : 0.182 REMARK 3 FREE R VALUE : 0.260 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000 REMARK 3 FREE R VALUE TEST SET COUNT : NULL REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 1773 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 0 REMARK 3 SOLVENT ATOMS : NULL REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL 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 OVERALL COORDINATE ERROR. REMARK 3 ESU BASED ON R VALUE (A): NULL REMARK 3 ESU BASED ON FREE R VALUE (A): NULL REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): NULL REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. REMARK 3 DISTANCE RESTRAINTS. RMS SIGMA REMARK 3 BOND LENGTH (A) : NULL ; NULL REMARK 3 ANGLE DISTANCE (A) : NULL ; NULL REMARK 3 INTRAPLANAR 1-4 DISTANCE (A) : NULL ; NULL REMARK 3 H-BOND OR METAL COORDINATION (A) : NULL ; NULL REMARK 3 REMARK 3 PLANE RESTRAINT (A) : NULL ; NULL REMARK 3 CHIRAL-CENTER RESTRAINT (A**3) : NULL ; NULL REMARK 3 REMARK 3 NON-BONDED CONTACT RESTRAINTS. REMARK 3 SINGLE TORSION (A) : NULL ; NULL REMARK 3 MULTIPLE TORSION (A) : NULL ; NULL REMARK 3 H-BOND (X...Y) (A) : NULL ; NULL REMARK 3 H-BOND (X-H...Y) (A) : NULL ; NULL REMARK 3 REMARK 3 CONFORMATIONAL TORSION ANGLE RESTRAINTS. REMARK 3 SPECIFIED (DEGREES) : NULL ; NULL REMARK 3 PLANAR (DEGREES) : NULL ; NULL REMARK 3 STAGGERED (DEGREES) : NULL ; NULL REMARK 3 TRANSVERSE (DEGREES) : NULL ; 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 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1OHQ 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 3.102 (2007-05-31) REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY EBI . REMARK 100 THE EBI ID CODE IS EBI-12807 . REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 15-SEP-2002 REMARK 200 TEMPERATURE (KELVIN) : 100.0 REMARK 200 PH : 6.00 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : ESRF REMARK 200 BEAMLINE : NULL REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.9793 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : NULL REMARK 200 DETECTOR MANUFACTURER : NULL REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM REMARK 200 DATA SCALING SOFTWARE : CCP4 (SCALA) REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 19067 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000 REMARK 200 RESOLUTION RANGE LOW (A) : 70.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.4 REMARK 200 DATA REDUNDANCY : 7.000 REMARK 200 R MERGE (I) : 0.16500 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 4.3000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.11 REMARK 200 COMPLETENESS FOR SHELL (%) : 99.7 REMARK 200 DATA REDUNDANCY IN SHELL : 6.00 REMARK 200 R MERGE FOR SHELL (I) : 0.64100 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 2.200 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: PDB ENTRY 1FGV REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 56.00 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.80 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: PH 6.0 REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 41 2 2 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 1/2-X,1/2-Y,1/2+Z REMARK 290 3555 -Y,1/2+X,1/4+Z REMARK 290 4555 1/2+Y,-X,3/4+Z REMARK 290 5555 1/2-X,Y,3/4-Z REMARK 290 6555 X,1/2-Y,1/4-Z REMARK 290 7555 1/2+Y,1/2+X,1/2-Z REMARK 290 8555 -Y,-X,-Z REMARK 290 9555 1/2+X,1/2+Y,1/2+Z REMARK 290 10555 1-X,1-Y,1+Z REMARK 290 11555 1/2-Y,1+X,3/4+Z REMARK 290 12555 1+Y,1/2-X,5/4+Z REMARK 290 13555 1-X,1/2+Y,5/4-Z REMARK 290 14555 1/2+X,1-Y,3/4-Z REMARK 290 15555 1+Y,1+X,1-Z REMARK 290 16555 1/2-Y,1/2-X,1/2-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 38.06050 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 38.06050 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 93.53450 REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 38.06050 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 46.76725 REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 38.06050 REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 140.30175 REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 38.06050 REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 140.30175 REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 38.06050 REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 46.76725 REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 38.06050 REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 38.06050 REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 93.53450 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 0.00000 REMARK 290 SMTRY1 9 1.000000 0.000000 0.000000 38.06050 REMARK 290 SMTRY2 9 0.000000 1.000000 0.000000 38.06050 REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 93.53450 REMARK 290 SMTRY1 10 -1.000000 0.000000 0.000000 76.12100 REMARK 290 SMTRY2 10 0.000000 -1.000000 0.000000 76.12100 REMARK 290 SMTRY3 10 0.000000 0.000000 1.000000 187.06900 REMARK 290 SMTRY1 11 0.000000 -1.000000 0.000000 38.06050 REMARK 290 SMTRY2 11 1.000000 0.000000 0.000000 76.12100 REMARK 290 SMTRY3 11 0.000000 0.000000 1.000000 140.30175 REMARK 290 SMTRY1 12 0.000000 1.000000 0.000000 76.12100 REMARK 290 SMTRY2 12 -1.000000 0.000000 0.000000 38.06050 REMARK 290 SMTRY3 12 0.000000 0.000000 1.000000 233.83625 REMARK 290 SMTRY1 13 -1.000000 0.000000 0.000000 76.12100 REMARK 290 SMTRY2 13 0.000000 1.000000 0.000000 38.06050 REMARK 290 SMTRY3 13 0.000000 0.000000 -1.000000 233.83625 REMARK 290 SMTRY1 14 1.000000 0.000000 0.000000 38.06050 REMARK 290 SMTRY2 14 0.000000 -1.000000 0.000000 76.12100 REMARK 290 SMTRY3 14 0.000000 0.000000 -1.000000 140.30175 REMARK 290 SMTRY1 15 0.000000 1.000000 0.000000 76.12100 REMARK 290 SMTRY2 15 1.000000 0.000000 0.000000 76.12100 REMARK 290 SMTRY3 15 0.000000 0.000000 -1.000000 187.06900 REMARK 290 SMTRY1 16 0.000000 -1.000000 0.000000 38.06050 REMARK 290 SMTRY2 16 -1.000000 0.000000 0.000000 38.06050 REMARK 290 SMTRY3 16 0.000000 0.000000 -1.000000 93.53450 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: A, B, Y, Z REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 375 REMARK 375 SPECIAL POSITION REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL REMARK 375 POSITIONS. REMARK 375 REMARK 375 ATOM RES CSSEQI REMARK 375 HOH Z 23 LIES ON A SPECIAL POSITION. 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 GLU A 1 CG CD OE1 OE2 REMARK 470 LYS A 65 CG CD CE NZ REMARK 470 GLU A 89 CG CD OE1 OE2 REMARK 470 GLU B 1 CG CD OE1 OE2 REMARK 470 GLN B 13 CD OE1 NE2 REMARK 470 LYS B 65 CG CD CE NZ REMARK 470 GLU B 89 CG CD OE1 OE2 REMARK 470 SER B 120 CA C O CB OG REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT REMARK 500 REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT. REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI REMARK 500 O HOH Z 91 O HOH Z 96 2.18 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 PRO A 54 CB PRO A 54 CG 0.057 REMARK 500 MET A 83 SD MET A 83 CE -0.058 REMARK 500 ASP B 31 C GLU B 32 N 0.116 REMARK 500 SER B 119 C SER B 120 N -0.089 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 B 119 O - C - N ANGL. DEV. =-123.0 DEGREES 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 Y 28 DISTANCE = 5.65 ANGSTROMS DBREF 1OHQ A 1 120 UNP P01764 HV3C_HUMAN 1 120 DBREF 1OHQ B 1 120 UNP P01764 HV3C_HUMAN 1 120 SEQRES 1 A 120 GLU VAL GLN LEU LEU GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 A 120 PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 A 120 PHE ARG ILE SER ASP GLU ASP MET GLY TRP VAL ARG GLN SEQRES 4 A 120 ALA PRO GLY LYS GLY LEU GLU TRP VAL SER SER ILE TYR SEQRES 5 A 120 GLY PRO SER GLY SER THR TYR TYR ALA ASP SER VAL LYS SEQRES 6 A 120 GLY ARG PHE THR ILE SER ARG ASP ASN SER LYS ASN THR SEQRES 7 A 120 LEU TYR LEU GLN MET ASN SER LEU ARG ALA GLU ASP THR SEQRES 8 A 120 ALA VAL TYR TYR CYS ALA SER ALA LEU GLU PRO LEU SER SEQRES 9 A 120 GLU PRO LEU GLY PHE TRP GLY GLN GLY THR LEU VAL THR SEQRES 10 A 120 VAL SER SER SEQRES 1 B 120 GLU VAL GLN LEU LEU GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 B 120 PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 B 120 PHE ARG ILE SER ASP GLU ASP MET GLY TRP VAL ARG GLN SEQRES 4 B 120 ALA PRO GLY LYS GLY LEU GLU TRP VAL SER SER ILE TYR SEQRES 5 B 120 GLY PRO SER GLY SER THR TYR TYR ALA ASP SER VAL LYS SEQRES 6 B 120 GLY ARG PHE THR ILE SER ARG ASP ASN SER LYS ASN THR SEQRES 7 B 120 LEU TYR LEU GLN MET ASN SER LEU ARG ALA GLU ASP THR SEQRES 8 B 120 ALA VAL TYR TYR CYS ALA SER ALA LEU GLU PRO LEU SER SEQRES 9 B 120 GLU PRO LEU GLY PHE TRP GLY GLN GLY THR LEU VAL THR SEQRES 10 B 120 VAL SER SER FORMUL 3 HOH *183(H2 O) HELIX 1 1 ARG A 28 ASP A 31 5 4 HELIX 2 2 ARG A 87 THR A 91 5 5 HELIX 3 3 ASP B 62 LYS B 65 5 4 HELIX 4 4 ARG B 87 THR B 91 5 5 SHEET 1 AA 4 GLN A 3 SER A 7 0 SHEET 2 AA 4 LEU A 18 SER A 25 -1 O SER A 21 N SER A 7 SHEET 3 AA 4 THR A 78 MET A 83 -1 O LEU A 79 N CYS A 22 SHEET 4 AA 4 PHE A 68 ASP A 73 -1 O THR A 69 N GLN A 82 SHEET 1 AB 6 GLY A 10 VAL A 12 0 SHEET 2 AB 6 THR A 114 VAL A 118 1 O LEU A 115 N GLY A 10 SHEET 3 AB 6 ALA A 92 SER A 98 -1 O ALA A 92 N VAL A 116 SHEET 4 AB 6 ASP A 33 ALA A 40 -1 O GLY A 35 N ALA A 97 SHEET 5 AB 6 GLY A 44 TYR A 52 -1 O GLY A 44 N ALA A 40 SHEET 6 AB 6 THR A 58 TYR A 60 -1 O TYR A 59 N SER A 50 SHEET 1 BA 4 GLN B 3 SER B 7 0 SHEET 2 BA 4 LEU B 18 SER B 25 -1 O SER B 21 N SER B 7 SHEET 3 BA 4 THR B 78 MET B 83 -1 O LEU B 79 N CYS B 22 SHEET 4 BA 4 PHE B 68 ASP B 73 -1 O THR B 69 N GLN B 82 SHEET 1 BB 6 GLY B 10 VAL B 12 0 SHEET 2 BB 6 THR B 114 VAL B 118 1 O LEU B 115 N GLY B 10 SHEET 3 BB 6 ALA B 92 LEU B 100 -1 O ALA B 92 N VAL B 116 SHEET 4 BB 6 ASP B 33 GLN B 39 -1 O ASP B 33 N ALA B 99 SHEET 5 BB 6 LEU B 45 TYR B 52 -1 O GLU B 46 N ARG B 38 SHEET 6 BB 6 SER B 57 TYR B 60 -1 O SER B 57 N TYR B 52 SHEET 1 BC 4 GLY B 10 VAL B 12 0 SHEET 2 BC 4 THR B 114 VAL B 118 1 O LEU B 115 N GLY B 10 SHEET 3 BC 4 ALA B 92 LEU B 100 -1 O ALA B 92 N VAL B 116 SHEET 4 BC 4 LEU B 107 TRP B 110 -1 O LEU B 107 N LEU B 100 SSBOND 1 CYS A 22 CYS A 96 SSBOND 2 CYS B 22 CYS B 96 CRYST1 76.121 76.121 187.069 90.00 90.00 90.00 I 41 2 2 32 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 0.013137 0.000000 0.000000 0.00000 SCALE2 0.000000 0.013137 0.000000 0.00000 SCALE3 0.000000 0.000000 0.005346 0.00000