HEADER IMMUNOGLOBULIN 23-MAR-92 8FAB TITLE CRYSTAL STRUCTURE OF THE FAB FRAGMENT FROM THE HUMAN TITLE 2 MYELOMA IMMUNOGLOBULIN IGG HIL AT 1.8 ANGSTROMS RESOLUTION COMPND MOL_ID: 1; COMPND 2 MOLECULE: IGG1-LAMBDA HIL FAB (LIGHT CHAIN); COMPND 3 CHAIN: A, C; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: IGG1-LAMBDA HIL FAB (HEAVY CHAIN); COMPND 7 CHAIN: B, D; COMPND 8 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 MOL_ID: 2 KEYWDS IMMUNOGLOBULIN EXPDTA X-RAY DIFFRACTION AUTHOR F.A.SAUL,R.J.POLJAK REVDAT 1 31-OCT-93 8FAB 0 JRNL AUTH R.K.STRONG,R.CAMPBELL,D.R.ROSE,G.A.PETSKO,J.SHARON, JRNL AUTH 2 M.N.MARGOLIES JRNL TITL THREE-DIMENSIONAL STRUCTURE OF MURINE JRNL TITL 2 ANTI-P-AZOPHENYLARSONATE FAB 36-71. 1. X-RAY JRNL TITL 3 CRYSTALLOGRAPHY, SITE-DIRECTED MUTAGENESIS, AND JRNL TITL 4 MODELING OF THE COMPLEX WITH HAPTEN. JRNL REF BIOCHEMISTRY V. 30 3739 1991 JRNL REFN ASTM BICHAW US ISSN 0006-2960 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH Y.-Y.H.CHIU,J.A.LOPEZ DE CASTRO,R.J.POLJAK REMARK 1 TITL AMINO ACID SEQUENCE OF THE VH REGION OF HUMAN REMARK 1 TITL 2 MYELOMA CRYOIMMUNOGLOBULIN IGG HIL REMARK 1 REF BIOCHEMISTRY V. 18 553 1979 REMARK 1 REFN ASTM BICHAW US ISSN 0006-2960 REMARK 1 REFERENCE 2 REMARK 1 AUTH J.A.LOPEZ DE CASTRO,Y.-Y.H.CHIU,R.J.POLJAK REMARK 1 TITL AMINO ACID SEQUENCE OF THE VARIABLE REGION OF THE REMARK 1 TITL 2 LIGHT (LAMBDA) CHAIN FROM HUMAN MYELOMA REMARK 1 TITL 3 CRYOIMMUNOGLOBULIN IGG HIL REMARK 1 REF BIOCHEMISTRY V. 17 1718 1978 REMARK 1 REFN ASTM BICHAW US ISSN 0006-2960 REMARK 1 REFERENCE 3 REMARK 1 AUTH G.ROSSI,T.K.CHOI,A.NISONOFF REMARK 1 TITL CRYSTALS OF FRAGMENT FAB': PREPARATION FROM PEPSIN REMARK 1 TITL 2 DIGESTS OF HUMAN IGG MYELOMA PROTEINS REMARK 1 REF NATURE V. 223 837 1969 REMARK 1 REFN ASTM NATUAS UK ISSN 0028-0836 REMARK 2 REMARK 2 RESOLUTION. 1.80 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : X-PLOR REMARK 3 AUTHORS : BRUNGER REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 6.00 REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.500 REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL REMARK 3 COMPLETENESS (WORKING+TEST) (%) : NULL REMARK 3 NUMBER OF REFLECTIONS : 64477 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 CROSS-VALIDATION METHOD : NULL REMARK 3 FREE R VALUE TEST SET SELECTION : NULL REMARK 3 R VALUE (WORKING SET) : 0.173 REMARK 3 FREE R VALUE : NULL REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL REMARK 3 FREE R VALUE TEST SET COUNT : NULL 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) : NULL REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL REMARK 3 BIN R VALUE (WORKING SET) : NULL REMARK 3 BIN FREE R VALUE : NULL REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 6405 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 0 REMARK 3 SOLVENT ATOMS : 668 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 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) : 2.96 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 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 8FAB 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 3.100 (2007-03-18) REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : NULL REMARK 200 TEMPERATURE (KELVIN) : NULL REMARK 200 PH : NULL REMARK 200 NUMBER OF CRYSTALS USED : NULL REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : NULL REMARK 200 RADIATION SOURCE : NULL REMARK 200 BEAMLINE : NULL REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : NULL REMARK 200 WAVELENGTH OR RANGE (A) : NULL 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 : NULL REMARK 200 DATA SCALING SOFTWARE : NULL REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : NULL REMARK 200 RESOLUTION RANGE HIGH (A) : NULL REMARK 200 RESOLUTION RANGE LOW (A) : NULL REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : NULL REMARK 200 DATA REDUNDANCY : NULL REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : NULL REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL REMARK 200 COMPLETENESS FOR SHELL (%) : NULL REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : NULL REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: NULL REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL REMARK 200 SOFTWARE USED: X-PLOR REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 50.77 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.50 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: NULL REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 1/2-X,-Y,1/2+Z REMARK 290 3555 -X,1/2+Y,1/2-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 55.30000 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 33.25000 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 63.71000 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 33.25000 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 55.30000 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 63.71000 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: A, B REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 350 BIOMOLECULE: 2 REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D 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 SER A 1 REMARK 465 TYR A 2 REMARK 465 THR A 209 REMARK 465 GLU A 210 REMARK 465 CYS A 211 REMARK 465 SER A 212 REMARK 465 SER B 135 REMARK 465 SER B 136 REMARK 465 LYS B 137 REMARK 465 SER B 138 REMARK 465 THR B 139 REMARK 465 SER B 140 REMARK 465 GLY B 141 REMARK 465 GLY B 142 REMARK 465 CYS B 224 REMARK 465 SER C 1 REMARK 465 TYR C 2 REMARK 465 THR C 209 REMARK 465 GLU C 210 REMARK 465 CYS C 211 REMARK 465 SER C 212 REMARK 465 SER D 223 REMARK 465 CYS D 224 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 TRP A 90 CB CG CD1 CD2 NE1 CE2 CE3 REMARK 470 TRP A 90 CZ2 CZ3 CH2 REMARK 470 SER B 223 CA C O CB OG REMARK 470 TRP C 90 CB CG CD1 CD2 NE1 CE2 CE3 REMARK 470 TRP C 90 CZ2 CZ3 CH2 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 LYS B 222 C SER B 223 N -0.091 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 ASP A 50 -45.58 66.44 REMARK 500 ASP A 151 -109.18 57.72 REMARK 500 ASP C 50 -39.61 61.89 REMARK 500 TRP C 90 -164.15 125.99 REMARK 500 ASP C 151 -95.60 58.56 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 31 DISTANCE = 5.62 ANGSTROMS REMARK 525 HOH 62 DISTANCE = 8.86 ANGSTROMS REMARK 525 HOH 63 DISTANCE = 7.85 ANGSTROMS REMARK 525 HOH 77 DISTANCE = 6.46 ANGSTROMS REMARK 525 HOH 80 DISTANCE = 6.95 ANGSTROMS REMARK 525 HOH 94 DISTANCE = 7.85 ANGSTROMS REMARK 525 HOH 113 DISTANCE = 5.21 ANGSTROMS REMARK 525 HOH 116 DISTANCE = 5.07 ANGSTROMS REMARK 525 HOH 118 DISTANCE = 7.23 ANGSTROMS REMARK 525 HOH 124 DISTANCE = 7.52 ANGSTROMS REMARK 525 HOH 129 DISTANCE = 7.74 ANGSTROMS REMARK 525 HOH 133 DISTANCE = 7.82 ANGSTROMS REMARK 525 HOH 177 DISTANCE = 7.82 ANGSTROMS REMARK 525 HOH 189 DISTANCE = 7.79 ANGSTROMS REMARK 525 HOH 210 DISTANCE = 6.21 ANGSTROMS REMARK 525 HOH 213 DISTANCE = 5.77 ANGSTROMS REMARK 525 HOH 232 DISTANCE = 5.23 ANGSTROMS REMARK 525 HOH 237 DISTANCE = 6.71 ANGSTROMS REMARK 525 HOH 240 DISTANCE = 6.14 ANGSTROMS REMARK 525 HOH 252 DISTANCE = 9.11 ANGSTROMS REMARK 525 HOH 255 DISTANCE = 7.04 ANGSTROMS REMARK 525 HOH 257 DISTANCE = 8.65 ANGSTROMS REMARK 525 HOH 282 DISTANCE = 10.94 ANGSTROMS REMARK 525 HOH 315 DISTANCE = 7.65 ANGSTROMS REMARK 525 HOH 324 DISTANCE = 11.23 ANGSTROMS REMARK 525 HOH 343 DISTANCE = 6.95 ANGSTROMS REMARK 525 HOH 345 DISTANCE = 6.33 ANGSTROMS REMARK 525 HOH 364 DISTANCE = 8.54 ANGSTROMS REMARK 525 HOH 377 DISTANCE = 7.00 ANGSTROMS REMARK 525 HOH 379 DISTANCE = 7.75 ANGSTROMS REMARK 525 HOH 410 DISTANCE = 6.81 ANGSTROMS REMARK 525 HOH 415 DISTANCE = 8.00 ANGSTROMS REMARK 525 HOH 417 DISTANCE = 8.24 ANGSTROMS REMARK 525 HOH 422 DISTANCE = 7.54 ANGSTROMS REMARK 525 HOH 428 DISTANCE = 10.98 ANGSTROMS REMARK 525 HOH 431 DISTANCE = 6.51 ANGSTROMS REMARK 525 HOH 447 DISTANCE = 5.72 ANGSTROMS REMARK 525 HOH 459 DISTANCE = 7.11 ANGSTROMS REMARK 525 HOH 465 DISTANCE = 8.33 ANGSTROMS REMARK 525 HOH 471 DISTANCE = 14.59 ANGSTROMS REMARK 525 HOH 498 DISTANCE = 7.14 ANGSTROMS REMARK 525 HOH 504 DISTANCE = 6.04 ANGSTROMS REMARK 525 HOH 535 DISTANCE = 6.65 ANGSTROMS REMARK 525 HOH 546 DISTANCE = 6.05 ANGSTROMS REMARK 525 HOH 547 DISTANCE = 6.91 ANGSTROMS REMARK 525 HOH 548 DISTANCE = 5.66 ANGSTROMS REMARK 525 HOH 557 DISTANCE = 6.65 ANGSTROMS REMARK 525 HOH 560 DISTANCE = 8.04 ANGSTROMS REMARK 525 HOH 580 DISTANCE = 10.21 ANGSTROMS REMARK 525 HOH 595 DISTANCE = 7.22 ANGSTROMS REMARK 525 HOH 625 DISTANCE = 7.08 ANGSTROMS REMARK 525 HOH 643 DISTANCE = 7.67 ANGSTROMS DBREF 8FAB A 1 212 PIR S25738 S25738 20 231 DBREF 8FAB B 2 224 EMBL Y14737 CAA75032 21 250 DBREF 8FAB C 1 212 PIR S25738 S25738 20 231 DBREF 8FAB D 2 224 EMBL Y14737 CAA75032 21 250 SEQADV 8FAB ARG A 19 PIR S25738 SER 38 CONFLICT SEQADV 8FAB ALA A 24 PIR S25738 GLY 43 CONFLICT SEQADV 8FAB ASN A 25 PIR S25738 ASP 44 CONFLICT SEQADV 8FAB ALA A 26 PIR S25738 THR 45 CONFLICT SEQADV 8FAB PRO A 28 PIR S25738 GLY 47 CONFLICT SEQADV 8FAB ASN A 29 PIR S25738 ASP 48 CONFLICT SEQADV 8FAB GLN A 30 PIR S25738 LYS 49 CONFLICT SEQADV 8FAB TYR A 33 PIR S25738 CYS 52 CONFLICT SEQADV 8FAB ARG A 41 PIR S25738 HIS 60 CONFLICT SEQADV 8FAB ALA A 42 PIR S25738 SER 61 CONFLICT SEQADV 8FAB MET A 45 PIR S25738 LEU 64 CONFLICT SEQADV 8FAB TYR A 48 PIR S25738 PHE 67 CONFLICT SEQADV 8FAB LYS A 49 PIR S25738 GLN 68 CONFLICT SEQADV 8FAB THR A 51 PIR S25738 SER 70 CONFLICT SEQADV 8FAB GLN A 52 PIR S25738 LYS 71 CONFLICT SEQADV 8FAB GLN A 59 PIR S25738 GLU 78 CONFLICT SEQADV 8FAB SER A 63 PIR S25738 GLY 82 CONFLICT SEQADV 8FAB THR A 65 PIR S25738 ASN 84 CONFLICT SEQADV 8FAB THR A 68 PIR S25738 ASN 87 CONFLICT SEQADV 8FAB VAL A 70 PIR S25738 ALA 89 CONFLICT SEQADV 8FAB VAL A 77 PIR S25738 THR 96 CONFLICT SEQADV 8FAB GLU A 80 PIR S25738 MET 99 CONFLICT SEQADV 8FAB ASN A 92 PIR S25738 SER 111 CONFLICT SEQADV 8FAB ALA A 94 PIR S25738 THR 113 CONFLICT SEQADV 8FAB SER A 95 PIR S25738 ALA 114 CONFLICT SEQADV 8FAB ILE A 96 PIR S25738 VAL 115 CONFLICT SEQADV 8FAB ILE A 155 PIR S25738 VAL 174 CONFLICT SEQADV 8FAB LYS B 3 EMBL Y14737 GLN 22 CONFLICT SEQADV 8FAB GLN B 6 EMBL Y14737 GLU 25 CONFLICT SEQADV 8FAB ALA B 7 EMBL Y14737 SER 26 CONFLICT SEQADV 8FAB ILE B 23 EMBL Y14737 ALA 42 CONFLICT SEQADV 8FAB VAL B 50 EMBL Y14737 ALA 69 CONFLICT SEQADV 8FAB ASN B 54 EMBL Y14737 ASP 73 CONFLICT SEQADV 8FAB ARG B 57 EMBL Y14737 ASN 76 CONFLICT SEQADV 8FAB THR B 58 EMBL Y14737 LYS 77 CONFLICT SEQADV 8FAB GLY B 61 EMBL Y14737 ALA 80 CONFLICT SEQADV 8FAB ARG B 77 EMBL Y14737 ASN 96 CONFLICT SEQADV 8FAB THR B 88 EMBL Y14737 ALA 107 CONFLICT SEQADV 8FAB B EMBL Y14737 ARG 117 DELETION SEQADV 8FAB B EMBL Y14737 GLU 118 DELETION SEQADV 8FAB B EMBL Y14737 GLY 119 DELETION SEQADV 8FAB B EMBL Y14737 ARG 120 DELETION SEQADV 8FAB B EMBL Y14737 TRP 121 DELETION SEQADV 8FAB B EMBL Y14737 VAL 122 DELETION SEQADV 8FAB ASP B 99 EMBL Y14737 TYR 124 CONFLICT SEQADV 8FAB PRO B 100 EMBL Y14737 THR 125 CONFLICT SEQADV 8FAB ASP B 101 EMBL Y14737 THR 126 CONFLICT SEQADV 8FAB ILE B 102 EMBL Y14737 VAL 127 CONFLICT SEQADV 8FAB LEU B 103 EMBL Y14737 THR 128 CONFLICT SEQADV 8FAB B EMBL Y14737 ILE 130 DELETION SEQADV 8FAB ALA B 105 EMBL Y14737 GLY 131 CONFLICT SEQADV 8FAB PHE B 106 EMBL Y14737 TYR 132 CONFLICT SEQADV 8FAB SER B 107 EMBL Y14737 TYR 133 CONFLICT SEQADV 8FAB VAL B 115 EMBL Y14737 THR 141 CONFLICT SEQADV 8FAB LYS B 218 EMBL Y14737 ARG 244 CONFLICT SEQADV 8FAB ARG C 19 PIR S25738 SER 38 CONFLICT SEQADV 8FAB ALA C 24 PIR S25738 GLY 43 CONFLICT SEQADV 8FAB ASN C 25 PIR S25738 ASP 44 CONFLICT SEQADV 8FAB ALA C 26 PIR S25738 THR 45 CONFLICT SEQADV 8FAB PRO C 28 PIR S25738 GLY 47 CONFLICT SEQADV 8FAB ASN C 29 PIR S25738 ASP 48 CONFLICT SEQADV 8FAB GLN C 30 PIR S25738 LYS 49 CONFLICT SEQADV 8FAB TYR C 33 PIR S25738 CYS 52 CONFLICT SEQADV 8FAB ARG C 41 PIR S25738 HIS 60 CONFLICT SEQADV 8FAB ALA C 42 PIR S25738 SER 61 CONFLICT SEQADV 8FAB MET C 45 PIR S25738 LEU 64 CONFLICT SEQADV 8FAB TYR C 48 PIR S25738 PHE 67 CONFLICT SEQADV 8FAB LYS C 49 PIR S25738 GLN 68 CONFLICT SEQADV 8FAB THR C 51 PIR S25738 SER 70 CONFLICT SEQADV 8FAB GLN C 52 PIR S25738 LYS 71 CONFLICT SEQADV 8FAB GLN C 59 PIR S25738 GLU 78 CONFLICT SEQADV 8FAB SER C 63 PIR S25738 GLY 82 CONFLICT SEQADV 8FAB THR C 65 PIR S25738 ASN 84 CONFLICT SEQADV 8FAB THR C 68 PIR S25738 ASN 87 CONFLICT SEQADV 8FAB VAL C 70 PIR S25738 ALA 89 CONFLICT SEQADV 8FAB VAL C 77 PIR S25738 THR 96 CONFLICT SEQADV 8FAB GLU C 80 PIR S25738 MET 99 CONFLICT SEQADV 8FAB ASN C 92 PIR S25738 SER 111 CONFLICT SEQADV 8FAB ALA C 94 PIR S25738 THR 113 CONFLICT SEQADV 8FAB SER C 95 PIR S25738 ALA 114 CONFLICT SEQADV 8FAB ILE C 96 PIR S25738 VAL 115 CONFLICT SEQADV 8FAB ILE C 155 PIR S25738 VAL 174 CONFLICT SEQADV 8FAB LYS D 3 EMBL Y14737 GLN 22 CONFLICT SEQADV 8FAB GLN D 6 EMBL Y14737 GLU 25 CONFLICT SEQADV 8FAB ALA D 7 EMBL Y14737 SER 26 CONFLICT SEQADV 8FAB ILE D 23 EMBL Y14737 ALA 42 CONFLICT SEQADV 8FAB VAL D 50 EMBL Y14737 ALA 69 CONFLICT SEQADV 8FAB ASN D 54 EMBL Y14737 ASP 73 CONFLICT SEQADV 8FAB ARG D 57 EMBL Y14737 ASN 76 CONFLICT SEQADV 8FAB THR D 58 EMBL Y14737 LYS 77 CONFLICT SEQADV 8FAB GLY D 61 EMBL Y14737 ALA 80 CONFLICT SEQADV 8FAB ARG D 77 EMBL Y14737 ASN 96 CONFLICT SEQADV 8FAB THR D 88 EMBL Y14737 ALA 107 CONFLICT SEQADV 8FAB D EMBL Y14737 ARG 117 DELETION SEQADV 8FAB D EMBL Y14737 GLU 118 DELETION SEQADV 8FAB D EMBL Y14737 GLY 119 DELETION SEQADV 8FAB D EMBL Y14737 ARG 120 DELETION SEQADV 8FAB D EMBL Y14737 TRP 121 DELETION SEQADV 8FAB D EMBL Y14737 VAL 122 DELETION SEQADV 8FAB ASP D 99 EMBL Y14737 TYR 124 CONFLICT SEQADV 8FAB PRO D 100 EMBL Y14737 THR 125 CONFLICT SEQADV 8FAB ASP D 101 EMBL Y14737 THR 126 CONFLICT SEQADV 8FAB ILE D 102 EMBL Y14737 VAL 127 CONFLICT SEQADV 8FAB LEU D 103 EMBL Y14737 THR 128 CONFLICT SEQADV 8FAB D EMBL Y14737 ILE 130 DELETION SEQADV 8FAB ALA D 105 EMBL Y14737 GLY 131 CONFLICT SEQADV 8FAB PHE D 106 EMBL Y14737 TYR 132 CONFLICT SEQADV 8FAB SER D 107 EMBL Y14737 TYR 133 CONFLICT SEQADV 8FAB VAL D 115 EMBL Y14737 THR 141 CONFLICT SEQADV 8FAB LYS D 218 EMBL Y14737 ARG 244 CONFLICT SEQRES 1 A 212 SER TYR GLU LEU THR GLN PRO PRO SER VAL SER VAL SER SEQRES 2 A 212 PRO GLY GLN THR ALA ARG ILE THR CYS SER ALA ASN ALA SEQRES 3 A 212 LEU PRO ASN GLN TYR ALA TYR TRP TYR GLN GLN LYS PRO SEQRES 4 A 212 GLY ARG ALA PRO VAL MET VAL ILE TYR LYS ASP THR GLN SEQRES 5 A 212 ARG PRO SER GLY ILE PRO GLN ARG PHE SER SER SER THR SEQRES 6 A 212 SER GLY THR THR VAL THR LEU THR ILE SER GLY VAL GLN SEQRES 7 A 212 ALA GLU ASP GLU ALA ASP TYR TYR CYS GLN ALA TRP ASP SEQRES 8 A 212 ASN SER ALA SER ILE PHE GLY GLY GLY THR LYS LEU THR SEQRES 9 A 212 VAL LEU GLY GLN PRO LYS ALA ALA PRO SER VAL THR LEU SEQRES 10 A 212 PHE PRO PRO SER SER GLU GLU LEU GLN ALA ASN LYS ALA SEQRES 11 A 212 THR LEU VAL CYS LEU ILE SER ASP PHE TYR PRO GLY ALA SEQRES 12 A 212 VAL THR VAL ALA TRP LYS ALA ASP SER SER PRO ILE LYS SEQRES 13 A 212 ALA GLY VAL GLU THR THR THR PRO SER LYS GLN SER ASN SEQRES 14 A 212 ASN LYS TYR ALA ALA SER SER TYR LEU SER LEU THR PRO SEQRES 15 A 212 GLU GLN TRP LYS SER HIS ARG SER TYR SER CYS GLN VAL SEQRES 16 A 212 THR HIS GLU GLY SER THR VAL GLU LYS THR VAL ALA PRO SEQRES 17 A 212 THR GLU CYS SER SEQRES 1 B 224 ALA VAL LYS LEU VAL GLN ALA GLY GLY GLY VAL VAL GLN SEQRES 2 B 224 PRO GLY ARG SER LEU ARG LEU SER CYS ILE ALA SER GLY SEQRES 3 B 224 PHE THR PHE SER ASN TYR GLY MET HIS TRP VAL ARG GLN SEQRES 4 B 224 ALA PRO GLY LYS GLY LEU GLU TRP VAL ALA VAL ILE TRP SEQRES 5 B 224 TYR ASN GLY SER ARG THR TYR TYR GLY ASP SER VAL LYS SEQRES 6 B 224 GLY ARG PHE THR ILE SER ARG ASP ASN SER LYS ARG THR SEQRES 7 B 224 LEU TYR MET GLN MET ASN SER LEU ARG THR GLU ASP THR SEQRES 8 B 224 ALA VAL TYR TYR CYS ALA ARG ASP PRO ASP ILE LEU THR SEQRES 9 B 224 ALA PHE SER PHE ASP TYR TRP GLY GLN GLY VAL LEU VAL SEQRES 10 B 224 THR VAL SER SER ALA SER THR LYS GLY PRO SER VAL PHE SEQRES 11 B 224 PRO LEU ALA PRO SER SER LYS SER THR SER GLY GLY THR SEQRES 12 B 224 ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU SEQRES 13 B 224 PRO VAL THR VAL SER TRP ASN SER GLY ALA LEU THR SER SEQRES 14 B 224 GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SER SER GLY SEQRES 15 B 224 LEU TYR SER LEU SER SER VAL VAL THR VAL PRO SER SER SEQRES 16 B 224 SER LEU GLY THR GLN THR TYR ILE CYS ASN VAL ASN HIS SEQRES 17 B 224 LYS PRO SER ASN THR LYS VAL ASP LYS LYS VAL GLU PRO SEQRES 18 B 224 LYS SER CYS SEQRES 1 C 212 SER TYR GLU LEU THR GLN PRO PRO SER VAL SER VAL SER SEQRES 2 C 212 PRO GLY GLN THR ALA ARG ILE THR CYS SER ALA ASN ALA SEQRES 3 C 212 LEU PRO ASN GLN TYR ALA TYR TRP TYR GLN GLN LYS PRO SEQRES 4 C 212 GLY ARG ALA PRO VAL MET VAL ILE TYR LYS ASP THR GLN SEQRES 5 C 212 ARG PRO SER GLY ILE PRO GLN ARG PHE SER SER SER THR SEQRES 6 C 212 SER GLY THR THR VAL THR LEU THR ILE SER GLY VAL GLN SEQRES 7 C 212 ALA GLU ASP GLU ALA ASP TYR TYR CYS GLN ALA TRP ASP SEQRES 8 C 212 ASN SER ALA SER ILE PHE GLY GLY GLY THR LYS LEU THR SEQRES 9 C 212 VAL LEU GLY GLN PRO LYS ALA ALA PRO SER VAL THR LEU SEQRES 10 C 212 PHE PRO PRO SER SER GLU GLU LEU GLN ALA ASN LYS ALA SEQRES 11 C 212 THR LEU VAL CYS LEU ILE SER ASP PHE TYR PRO GLY ALA SEQRES 12 C 212 VAL THR VAL ALA TRP LYS ALA ASP SER SER PRO ILE LYS SEQRES 13 C 212 ALA GLY VAL GLU THR THR THR PRO SER LYS GLN SER ASN SEQRES 14 C 212 ASN LYS TYR ALA ALA SER SER TYR LEU SER LEU THR PRO SEQRES 15 C 212 GLU GLN TRP LYS SER HIS ARG SER TYR SER CYS GLN VAL SEQRES 16 C 212 THR HIS GLU GLY SER THR VAL GLU LYS THR VAL ALA PRO SEQRES 17 C 212 THR GLU CYS SER SEQRES 1 D 224 ALA VAL LYS LEU VAL GLN ALA GLY GLY GLY VAL VAL GLN SEQRES 2 D 224 PRO GLY ARG SER LEU ARG LEU SER CYS ILE ALA SER GLY SEQRES 3 D 224 PHE THR PHE SER ASN TYR GLY MET HIS TRP VAL ARG GLN SEQRES 4 D 224 ALA PRO GLY LYS GLY LEU GLU TRP VAL ALA VAL ILE TRP SEQRES 5 D 224 TYR ASN GLY SER ARG THR TYR TYR GLY ASP SER VAL LYS SEQRES 6 D 224 GLY ARG PHE THR ILE SER ARG ASP ASN SER LYS ARG THR SEQRES 7 D 224 LEU TYR MET GLN MET ASN SER LEU ARG THR GLU ASP THR SEQRES 8 D 224 ALA VAL TYR TYR CYS ALA ARG ASP PRO ASP ILE LEU THR SEQRES 9 D 224 ALA PHE SER PHE ASP TYR TRP GLY GLN GLY VAL LEU VAL SEQRES 10 D 224 THR VAL SER SER ALA SER THR LYS GLY PRO SER VAL PHE SEQRES 11 D 224 PRO LEU ALA PRO SER SER LYS SER THR SER GLY GLY THR SEQRES 12 D 224 ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU SEQRES 13 D 224 PRO VAL THR VAL SER TRP ASN SER GLY ALA LEU THR SER SEQRES 14 D 224 GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SER SER GLY SEQRES 15 D 224 LEU TYR SER LEU SER SER VAL VAL THR VAL PRO SER SER SEQRES 16 D 224 SER LEU GLY THR GLN THR TYR ILE CYS ASN VAL ASN HIS SEQRES 17 D 224 LYS PRO SER ASN THR LYS VAL ASP LYS LYS VAL GLU PRO SEQRES 18 D 224 LYS SER CYS FTNOTE 1 RESIDUE 141 IN CHAINS *A* AND *C* ARE CIS PROLINES. FTNOTE 2 RESIDUES 155 AND 157 IN CHAINS *B* AND *D* ARE CIS FTNOTE 2 PROLINES. FORMUL 5 HOH *668(H2 O) HELIX 1 1 ALA A 26 GLN A 30 5 5 HELIX 2 2 GLN A 78 GLU A 82 5 5 HELIX 3 3 SER A 121 ALA A 127 1 7 HELIX 4 4 THR A 181 SER A 187 1 7 HELIX 5 5 THR B 28 TYR B 32 5 5 HELIX 6 6 ASN B 74 LYS B 76 5 3 HELIX 7 7 ARG B 87 THR B 91 5 5 HELIX 8 8 SER B 164 ALA B 166 5 3 HELIX 9 9 SER B 195 GLN B 200 1 6 HELIX 10 10 LYS B 209 ASN B 212 5 4 HELIX 11 11 ALA C 26 GLN C 30 5 5 HELIX 12 12 GLN C 78 GLU C 82 5 5 HELIX 13 13 SER C 121 ALA C 127 1 7 HELIX 14 14 THR C 181 SER C 187 1 7 HELIX 15 15 THR D 28 TYR D 32 5 5 HELIX 16 16 ARG D 87 THR D 91 5 5 HELIX 17 17 SER D 136 SER D 140 5 5 HELIX 18 18 SER D 164 ALA D 166 5 3 HELIX 19 19 SER D 195 THR D 199 5 5 HELIX 20 20 LYS D 209 ASN D 212 5 4 SHEET 1 A 5 SER A 9 VAL A 12 0 SHEET 2 A 5 THR A 101 VAL A 105 1 O LYS A 102 N VAL A 10 SHEET 3 A 5 ALA A 83 ASP A 91 -1 O ALA A 83 N LEU A 103 SHEET 4 A 5 TYR A 33 GLN A 37 -1 N TYR A 33 O GLN A 88 SHEET 5 A 5 VAL A 44 ILE A 47 -1 O VAL A 44 N GLN A 36 SHEET 1 B 4 SER A 9 VAL A 12 0 SHEET 2 B 4 THR A 101 VAL A 105 1 O LYS A 102 N VAL A 10 SHEET 3 B 4 ALA A 83 ASP A 91 -1 O ALA A 83 N LEU A 103 SHEET 4 B 4 ALA A 94 PHE A 97 -1 N ALA A 94 O ASP A 91 SHEET 1 C 3 ALA A 18 SER A 23 0 SHEET 2 C 3 THR A 69 ILE A 74 -1 N VAL A 70 O CYS A 22 SHEET 3 C 3 PHE A 61 SER A 66 -1 O SER A 62 N THR A 73 SHEET 1 D 4 SER A 114 PHE A 118 0 SHEET 2 D 4 ALA A 130 PHE A 139 -1 O VAL A 133 N PHE A 118 SHEET 3 D 4 TYR A 172 LEU A 180 -1 N TYR A 172 O PHE A 139 SHEET 4 D 4 VAL A 159 THR A 161 -1 O GLU A 160 N TYR A 177 SHEET 1 E 4 SER A 114 PHE A 118 0 SHEET 2 E 4 ALA A 130 PHE A 139 -1 O VAL A 133 N PHE A 118 SHEET 3 E 4 TYR A 172 LEU A 180 -1 N TYR A 172 O PHE A 139 SHEET 4 E 4 SER A 165 LYS A 166 -1 N SER A 165 O ALA A 173 SHEET 1 F 4 SER A 153 ILE A 155 0 SHEET 2 F 4 THR A 145 ALA A 150 -1 O TRP A 148 N ILE A 155 SHEET 3 F 4 TYR A 191 HIS A 197 -1 N SER A 192 O LYS A 149 SHEET 4 F 4 SER A 200 VAL A 206 -1 O SER A 200 N HIS A 197 SHEET 1 G 4 LYS B 3 ALA B 7 0 SHEET 2 G 4 LEU B 18 SER B 25 -1 N SER B 21 O ALA B 7 SHEET 3 G 4 THR B 78 MET B 83 -1 N LEU B 79 O CYS B 22 SHEET 4 G 4 PHE B 68 ASP B 73 -1 O THR B 69 N GLN B 82 SHEET 1 H 5 THR B 58 TYR B 60 0 SHEET 2 H 5 LEU B 45 ILE B 51 -1 N VAL B 50 O TYR B 59 SHEET 3 H 5 MET B 34 GLN B 39 -1 O MET B 34 N ILE B 51 SHEET 4 H 5 ALA B 92 ARG B 98 -1 N VAL B 93 O GLN B 39 SHEET 5 H 5 TYR B 110 TRP B 111 -1 O TYR B 110 N ARG B 98 SHEET 1 I 6 THR B 58 TYR B 60 0 SHEET 2 I 6 LEU B 45 ILE B 51 -1 N VAL B 50 O TYR B 59 SHEET 3 I 6 MET B 34 GLN B 39 -1 O MET B 34 N ILE B 51 SHEET 4 I 6 ALA B 92 ARG B 98 -1 N VAL B 93 O GLN B 39 SHEET 5 I 6 VAL B 115 VAL B 119 -1 O VAL B 115 N TYR B 94 SHEET 6 I 6 GLY B 10 VAL B 12 1 O GLY B 10 N THR B 118 SHEET 1 J 4 SER B 128 LEU B 132 0 SHEET 2 J 4 ALA B 144 TYR B 153 -1 O GLY B 147 N LEU B 132 SHEET 3 J 4 TYR B 184 VAL B 192 -1 N TYR B 184 O TYR B 153 SHEET 4 J 4 VAL B 171 THR B 173 -1 N HIS B 172 O VAL B 189 SHEET 1 K 4 SER B 128 LEU B 132 0 SHEET 2 K 4 ALA B 144 TYR B 153 -1 O GLY B 147 N LEU B 132 SHEET 3 K 4 TYR B 184 VAL B 192 -1 N TYR B 184 O TYR B 153 SHEET 4 K 4 VAL B 177 LEU B 178 -1 N VAL B 177 O SER B 185 SHEET 1 L 3 THR B 159 TRP B 162 0 SHEET 2 L 3 ILE B 203 HIS B 208 -1 N ASN B 205 O SER B 161 SHEET 3 L 3 THR B 213 LYS B 218 -1 O THR B 213 N HIS B 208 SHEET 1 M 5 SER C 9 VAL C 12 0 SHEET 2 M 5 THR C 101 VAL C 105 1 O LYS C 102 N VAL C 10 SHEET 3 M 5 ALA C 83 ASP C 91 -1 O ALA C 83 N LEU C 103 SHEET 4 M 5 TYR C 33 GLN C 37 -1 N TYR C 33 O GLN C 88 SHEET 5 M 5 VAL C 44 ILE C 47 -1 O VAL C 44 N GLN C 36 SHEET 1 N 4 SER C 9 VAL C 12 0 SHEET 2 N 4 THR C 101 VAL C 105 1 O LYS C 102 N VAL C 10 SHEET 3 N 4 ALA C 83 ASP C 91 -1 O ALA C 83 N LEU C 103 SHEET 4 N 4 ALA C 94 PHE C 97 -1 O ALA C 94 N ASP C 91 SHEET 1 O 3 ALA C 18 SER C 23 0 SHEET 2 O 3 THR C 69 ILE C 74 -1 N VAL C 70 O CYS C 22 SHEET 3 O 3 PHE C 61 SER C 66 -1 O SER C 62 N THR C 73 SHEET 1 P 4 SER C 114 PHE C 118 0 SHEET 2 P 4 ALA C 130 PHE C 139 -1 O VAL C 133 N PHE C 118 SHEET 3 P 4 TYR C 172 LEU C 180 -1 N TYR C 172 O PHE C 139 SHEET 4 P 4 VAL C 159 THR C 161 -1 O GLU C 160 N TYR C 177 SHEET 1 Q 4 SER C 114 PHE C 118 0 SHEET 2 Q 4 ALA C 130 PHE C 139 -1 O VAL C 133 N PHE C 118 SHEET 3 Q 4 TYR C 172 LEU C 180 -1 N TYR C 172 O PHE C 139 SHEET 4 Q 4 SER C 165 LYS C 166 -1 O SER C 165 N ALA C 173 SHEET 1 R 4 SER C 153 ILE C 155 0 SHEET 2 R 4 THR C 145 ALA C 150 -1 O TRP C 148 N ILE C 155 SHEET 3 R 4 TYR C 191 HIS C 197 -1 N SER C 192 O LYS C 149 SHEET 4 R 4 SER C 200 VAL C 206 -1 O SER C 200 N HIS C 197 SHEET 1 S 4 LYS D 3 ALA D 7 0 SHEET 2 S 4 LEU D 18 SER D 25 -1 N SER D 21 O ALA D 7 SHEET 3 S 4 THR D 78 MET D 83 -1 N LEU D 79 O CYS D 22 SHEET 4 S 4 PHE D 68 ASP D 73 -1 O THR D 69 N GLN D 82 SHEET 1 T 5 THR D 58 TYR D 60 0 SHEET 2 T 5 LEU D 45 ILE D 51 -1 N VAL D 50 O TYR D 59 SHEET 3 T 5 MET D 34 GLN D 39 -1 O MET D 34 N ILE D 51 SHEET 4 T 5 ALA D 92 ARG D 98 -1 N VAL D 93 O GLN D 39 SHEET 5 T 5 TYR D 110 TRP D 111 -1 O TYR D 110 N ARG D 98 SHEET 1 U 6 THR D 58 TYR D 60 0 SHEET 2 U 6 LEU D 45 ILE D 51 -1 N VAL D 50 O TYR D 59 SHEET 3 U 6 MET D 34 GLN D 39 -1 O MET D 34 N ILE D 51 SHEET 4 U 6 ALA D 92 ARG D 98 -1 N VAL D 93 O GLN D 39 SHEET 5 U 6 VAL D 115 VAL D 119 -1 O VAL D 115 N TYR D 94 SHEET 6 U 6 GLY D 10 VAL D 12 1 O GLY D 10 N THR D 118 SHEET 1 V 4 SER D 128 LEU D 132 0 SHEET 2 V 4 THR D 143 TYR D 153 -1 O GLY D 147 N LEU D 132 SHEET 3 V 4 TYR D 184 PRO D 193 -1 N TYR D 184 O TYR D 153 SHEET 4 V 4 VAL D 171 THR D 173 -1 N HIS D 172 O VAL D 189 SHEET 1 W 4 SER D 128 LEU D 132 0 SHEET 2 W 4 THR D 143 TYR D 153 -1 O GLY D 147 N LEU D 132 SHEET 3 W 4 TYR D 184 PRO D 193 -1 N TYR D 184 O TYR D 153 SHEET 4 W 4 VAL D 177 LEU D 178 -1 N VAL D 177 O SER D 185 SHEET 1 X 3 THR D 159 TRP D 162 0 SHEET 2 X 3 ILE D 203 HIS D 208 -1 N ASN D 205 O SER D 161 SHEET 3 X 3 THR D 213 LYS D 218 -1 O THR D 213 N HIS D 208 SSBOND 1 CYS A 22 CYS A 87 SSBOND 2 CYS A 134 CYS A 193 SSBOND 3 CYS B 22 CYS B 96 SSBOND 4 CYS B 148 CYS B 204 SSBOND 5 CYS C 22 CYS C 87 SSBOND 6 CYS C 134 CYS C 193 SSBOND 7 CYS D 22 CYS D 96 SSBOND 8 CYS D 148 CYS D 204 CISPEP 1 TYR A 140 PRO A 141 0 -6.48 CISPEP 2 PHE B 154 PRO B 155 0 -9.44 CISPEP 3 GLU B 156 PRO B 157 0 -4.93 CISPEP 4 TYR C 140 PRO C 141 0 -3.47 CISPEP 5 PHE D 154 PRO D 155 0 -10.04 CISPEP 6 GLU D 156 PRO D 157 0 1.30 CRYST1 110.600 127.420 66.500 90.00 90.00 90.00 P 21 21 21 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 0.009042 0.000000 0.000000 0.00000 SCALE2 0.000000 0.007848 0.000000 0.00000 SCALE3 0.000000 0.000000 0.015038 0.00000