HEADER IMMUNE SYSTEM 15-OCT-02 1N0X TITLE CRYSTAL STRUCTURE OF A BROADLY NEUTRALIZING ANTI-HIV-1 TITLE 2 ANTIBODY IN COMPLEX WITH A PEPTIDE MIMOTOPE COMPND MOL_ID: 1; COMPND 2 MOLECULE: IMMUNOGLOBULIN LIGHT CHAIN; COMPND 3 CHAIN: L, M; COMPND 4 SYNONYM: IGG; COMPND 5 ENGINEERED: YES; COMPND 6 MOL_ID: 2; COMPND 7 MOLECULE: IMMUNOGLOBULIN HEAVY CHAIN; COMPND 8 CHAIN: H, K; COMPND 9 SYNONYM: IGG; COMPND 10 ENGINEERED: YES; COMPND 11 MOL_ID: 3; COMPND 12 MOLECULE: B2.1 PEPTIDE; COMPND 13 CHAIN: P, R; COMPND 14 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 EXPRESSION_SYSTEM: CRICETULUS GRISEUS; SOURCE 5 EXPRESSION_SYSTEM_COMMON: CHINESE HAMSTER; SOURCE 6 EXPRESSION_SYSTEM_STRAIN: CHO K1; SOURCE 7 EXPRESSION_SYSTEM_CELL: OVARY CELLS; SOURCE 8 MOL_ID: 2; SOURCE 9 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 10 ORGANISM_COMMON: HUMAN; SOURCE 11 EXPRESSION_SYSTEM: CRICETULUS GRISEUS; SOURCE 12 EXPRESSION_SYSTEM_COMMON: CHINESE HAMSTER; SOURCE 13 EXPRESSION_SYSTEM_STRAIN: CHO K1; SOURCE 14 EXPRESSION_SYSTEM_CELL: OVARY CELLS; SOURCE 15 MOL_ID: 3; SOURCE 16 SYNTHETIC: YES; SOURCE 17 OTHER_DETAILS: SELECTED FROM PHAGE DISPLAY PEPTIDE LIBRARY, SOURCE 18 THEN CHEMICALLY SYNTHESIZED. KEYWDS ANTIBODY-PEPTIDE COMPLEX, PEPTIDE DIMER EXPDTA X-RAY DIFFRACTION AUTHOR E.O.SAPHIRE,M.MONTERO,A.MENENDEZ,M.B.IRVING,M.B.ZWICK, AUTHOR 2 P.W.H.I.PARREN,D.R.BURTON,J.K.SCOTT,I.A.WILSON REVDAT 1 13-APR-04 1N0X 0 JRNL AUTH E.O.SAPHIRE,M.MONTERO,A.MENENDEZ,M.B.IRVING, JRNL AUTH 2 M.B.ZWICK,P.W.H.I.PARREN,D.R.BURTON,J.K.SCOTT, JRNL AUTH 3 I.A.WILSON JRNL TITL CRYSTAL STRUCTURE OF A BROADLY NEUTRALIZING JRNL TITL 2 ANTI-HIV-1 ANTIBODY IN COMPLEX WITH A PEPTIDE JRNL TITL 3 MIMOTOPE JRNL REF TO BE PUBLISHED JRNL REFN REMARK 1 REMARK 2 REMARK 2 RESOLUTION. 1.80 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : CNS 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) : 1.80 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 45.00 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) (%) : 92.0 REMARK 3 NUMBER OF REFLECTIONS : 84895 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM REMARK 3 R VALUE (WORKING SET) : 0.220 REMARK 3 FREE R VALUE : 0.252 REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL REMARK 3 FREE R VALUE TEST SET COUNT : 1967 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 : 7091 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 35 REMARK 3 SOLVENT ATOMS : 773 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 20.10 REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 0.59000 REMARK 3 B22 (A**2) : 2.67800 REMARK 3 B33 (A**2) : -3.26800 REMARK 3 B12 (A**2) : 0.00000 REMARK 3 B13 (A**2) : -0.34000 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) : NULL REMARK 3 BOND ANGLES (DEGREES) : NULL 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: 10% TEST SET (9419) REFLECTIONS REMARK 3 SELECTED FOR INITIAL ROUNDS OF REFINEMENT. FOR FINAL ROUND OF REMARK 3 REFINEMENT, A 2% TEST SET WAS RANDOMLY SELECTED FROM REMARK 3 REFLECTIONS CONTAINED IN THE ORIGINAL 10% TEST SET. REMARK 4 REMARK 4 1N0X 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 RCSB017381. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 22-MAY-2000 REMARK 200 TEMPERATURE (KELVIN) : 171.0 REMARK 200 PH : 10.50 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : SSRL REMARK 200 BEAMLINE : BL11-1 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.965 REMARK 200 MONOCHROMATOR : SI 111 CHANNEL REMARK 200 OPTICS : FLAT MIRROR REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : QUANTUM 315 (ADSC) REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO REMARK 200 DATA SCALING SOFTWARE : SCALEPACK REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 84895 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.780 REMARK 200 RESOLUTION RANGE LOW (A) : 33.450 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 92.0 REMARK 200 DATA REDUNDANCY : 2.300 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : 0.06000 REMARK 200 FOR THE DATA SET : 17.6000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.78 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.81 REMARK 200 COMPLETENESS FOR SHELL (%) : 87.1 REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : 0.38500 REMARK 200 FOR SHELL : 1.500 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: FAB DOMAINS FROM UNCOMPLEXED IGG1 B12 STRUCTURE REMARK 200 (1HZH) REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 51.61 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.54 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: AMMONIUM SULFATE, LITHIUM SULFATE, REMARK 280 CAPS BUFFER, PH 10.5, VAPOR DIFFUSION, SITTING DROP, REMARK 280 TEMPERATURE 22.5K 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 92.17900 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 6 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, M, K, P, R 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 LYS H 131 REMARK 465 SER H 132 REMARK 465 THR H 133 REMARK 465 SER H 134 REMARK 465 GLY H 135 REMARK 465 GLY H 136 REMARK 465 SER H 229 REMARK 465 CYS H 230 REMARK 465 SER K 130 REMARK 465 LYS K 131 REMARK 465 SER K 132 REMARK 465 THR K 133 REMARK 465 SER K 134 REMARK 465 GLY K 135 REMARK 465 LYS R 21 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 ORN P 19 CG CD NE REMARK 470 LYS P 21 CG CD CE NZ REMARK 470 ORN R 19 CG CD NE REMARK 470 LYS R 20 CG CD CE NZ 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 ND2 ASN M 210 O HOH 719 2.11 REMARK 500 O PHE M 209 O HOH 719 2.16 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 PHE L 83 C ALA L 84 N -0.120 REMARK 500 ALA L 84 C LEU L 85 N 0.281 REMARK 500 PRO H 100D CB PRO H 100D CG -0.081 REMARK 500 PRO H 100D CG PRO H 100D CD -0.115 REMARK 500 PRO H 100D CA PRO H 100D C 0.127 REMARK 500 PRO H 100D C GLN H 100E N -0.090 REMARK 500 MET K 100J SD MET K 100J CE -0.065 REMARK 500 ALA R 17 CA ALA R 17 C -0.053 REMARK 500 GLU R 18 C ORN R 19 N -0.182 REMARK 500 ORN R 19 C LYS R 20 N -0.189 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 ALA L 84 CA - C - N ANGL. DEV. =-12.4 DEGREES REMARK 500 ALA L 84 O - C - N ANGL. DEV. =-10.0 DEGREES REMARK 500 VAL L 90 N - CA - C ANGL. DEV. = -8.6 DEGREES REMARK 500 SER L 114 N - CA - C ANGL. DEV. =-12.2 DEGREES REMARK 500 ASN H 52 N - CA - C ANGL. DEV. = -8.9 DEGREES REMARK 500 SER H 60 N - CA - C ANGL. DEV. = -9.2 DEGREES REMARK 500 CYS H 92 N - CA - C ANGL. DEV. = -8.9 DEGREES REMARK 500 PRO H 100D CA - CB - CG ANGL. DEV. = -9.0 DEGREES REMARK 500 PRO H 100D CA - C - O ANGL. DEV. = -9.4 DEGREES REMARK 500 PRO H 100D O - C - N ANGL. DEV. = 9.1 DEGREES REMARK 500 GLY H 104 N - CA - C ANGL. DEV. =-10.0 DEGREES REMARK 500 SER H 120 N - CA - C ANGL. DEV. =-11.0 DEGREES REMARK 500 LEU H 124 N - CA - C ANGL. DEV. =-11.9 DEGREES REMARK 500 GLU H 150 N - CA - C ANGL. DEV. = -9.0 DEGREES REMARK 500 VAL H 152 N - CA - C ANGL. DEV. = -9.0 DEGREES REMARK 500 LEU H 187 CA - CB - CG ANGL. DEV. = 10.1 DEGREES REMARK 500 LEU M 73 N - CA - C ANGL. DEV. = -8.9 DEGREES REMARK 500 SER M 114 N - CA - C ANGL. DEV. =-11.1 DEGREES REMARK 500 GLY M 128 N - CA - C ANGL. DEV. = 10.6 DEGREES REMARK 500 LEU M 136 N - CA - C ANGL. DEV. =-10.1 DEGREES REMARK 500 SER K 60 N - CA - C ANGL. DEV. = -9.9 DEGREES REMARK 500 CYS K 92 N - CA - C ANGL. DEV. = -9.1 DEGREES REMARK 500 GLY K 104 N - CA - C ANGL. DEV. = -9.1 DEGREES REMARK 500 SER K 120 N - CA - C ANGL. DEV. =-11.8 DEGREES REMARK 500 LEU K 124 N - CA - C ANGL. DEV. =-11.0 DEGREES REMARK 500 LYS K 145 N - CA - C ANGL. DEV. = 10.4 DEGREES REMARK 500 VAL K 152 N - CA - C ANGL. DEV. =-11.1 DEGREES REMARK 500 SER K 189 N - CA - C ANGL. DEV. = -9.5 DEGREES REMARK 500 LEU K 198 N - CA - C ANGL. DEV. = 8.9 DEGREES REMARK 500 ORN R 19 C - N - CA ANGL. DEV. = 20.4 DEGREES REMARK 500 ORN R 19 O - C - N ANGL. DEV. =-11.3 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 VAL L 51 -48.36 74.93 REMARK 500 VAL M 51 -47.22 73.90 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 468 DISTANCE = 9.89 ANGSTROMS REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1HZH RELATED DB: PDB REMARK 900 THE UNCOMPLEXED INTACT IGG OF THIS FAB ENTRY. REMARK 999 REMARK 999 SEQUENCE REMARK 999 THE GENBANK DATABASE SEQUENCE (AAA52919) IS THE REMARK 999 CORRECT MATCH FOR THE VARIABLE PORTION OF THE HEAVY REMARK 999 CHAIN EXCEPT THAT THE N-TERMINUS HAS BEEN CHANGED FROM REMARK 999 LEQSGAE TO QVQLVQSGAE IN THE PROCESS OF CLONING REMARK 999 FROM THE RECOMBINANT FAB FRAGMENT TO THE IGG. REMARK 999 REMARK 999 THE CONSTANT DOMAINS OF THE HEAVY CHAINS H AND K HAVE REMARK 999 THE SAME SEQUENCE AS ALL HUMAN IGG1 ANTIBODIES. REMARK 999 REMARK 999 THE VARIABLE REGION OF THE LIGHT CHAIN MATCHES THE REMARK 999 GENBANK DATABASE SEQUENCE (AAA52920) EXCEPT THAT THE REMARK 999 N-TERMINUS WAS CHANGED IN CLONING TO THE IGG FROM ELTQAPG REMARK 999 TO EIVLTQSPG; THE CONSTANT DOMAINS OF THE LIGHT CHAINS L REMARK 999 AND M HAVE THE SAME SEQUENCE AS ALL HUMAN KAPPA LIGHT REMARK 999 CHAINS. REMARK 999 REMARK 999 THE AUTHORS MAINTAIN THAT THE SEQUENCE OF L AND M, REMARK 999 RESIDUE ALA 34 SHOULD BE AN ALA AND NOT ARG (RESIDUE REMARK 999 33 IN THE SEQUENCE DATABASE). DBREF 1N0X H 4 118 GB 567141 AAA52919 1 129 DBREF 1N0X K 4 118 GB 567141 AAA52919 1 129 DBREF 1N0X L 1 108 GB 567142 AAA52920 1 107 DBREF 1N0X M 1 108 GB 567142 AAA52920 1 107 DBREF 1N0X H 119 230 GB 185362 AAA02914 152 249 DBREF 1N0X K 119 230 GB 185362 AAA02914 152 249 DBREF 1N0X L 109 214 GB 2894829 AAC02819 110 215 DBREF 1N0X M 109 214 GB 2894829 AAC02819 110 215 SEQADV 1N0X GLN H 1 GB 567141 SEE REMARK 999 SEQADV 1N0X VAL H 2 GB 567141 SEE REMARK 999 SEQADV 1N0X GLN H 3 GB 567141 SEE REMARK 999 SEQADV 1N0X VAL H 5 GB 567141 GLU 2 SEE REMARK 999 SEQADV 1N0X GLN K 1 GB 567141 SEE REMARK 999 SEQADV 1N0X VAL K 2 GB 567141 SEE REMARK 999 SEQADV 1N0X GLN K 3 GB 567141 SEE REMARK 999 SEQADV 1N0X VAL K 5 GB 567141 GLU 2 SEE REMARK 999 SEQADV 1N0X ILE L 2 GB 567142 SEE REMARK 999 SEQADV 1N0X VAL L 3 GB 567142 SEE REMARK 999 SEQADV 1N0X SER L 7 GB 567142 ALA 5 SEE REMARK 999 SEQADV 1N0X ALA L 34 GB 567142 ARG 33 SEE REMARK 999 SEQADV 1N0X ILE M 2 GB 567142 SEE REMARK 999 SEQADV 1N0X VAL M 3 GB 567142 SEE REMARK 999 SEQADV 1N0X SER M 7 GB 567142 ALA 5 SEE REMARK 999 SEQADV 1N0X ALA M 34 GB 567142 ARG 33 SEE REMARK 999 SEQRES 1 L 215 GLU ILE VAL LEU THR GLN SER PRO GLY THR LEU SER LEU SEQRES 2 L 215 SER PRO GLY GLU ARG ALA THR PHE SER CYS ARG SER SER SEQRES 3 L 215 HIS SER ILE ARG SER ARG ARG VAL ALA TRP TYR GLN HIS SEQRES 4 L 215 LYS PRO GLY GLN ALA PRO ARG LEU VAL ILE HIS GLY VAL SEQRES 5 L 215 SER ASN ARG ALA SER GLY ILE SER ASP ARG PHE SER GLY SEQRES 6 L 215 SER GLY SER GLY THR ASP PHE THR LEU THR ILE THR ARG SEQRES 7 L 215 VAL GLU PRO GLU ASP PHE ALA LEU TYR TYR CYS GLN VAL SEQRES 8 L 215 TYR GLY ALA SER SER TYR THR PHE GLY GLN GLY THR LYS SEQRES 9 L 215 LEU GLU ARG LYS ARG THR VAL ALA ALA PRO SER VAL PHE SEQRES 10 L 215 ILE PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR SEQRES 11 L 215 ALA SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG SEQRES 12 L 215 GLU ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SEQRES 13 L 215 SER GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER SEQRES 14 L 215 LYS ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SEQRES 15 L 215 SER LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS SEQRES 16 L 215 GLU VAL THR HIS GLN GLY LEU ARG SER PRO VAL THR LYS SEQRES 17 L 215 SER PHE ASN ARG GLY GLU CYS SEQRES 1 H 230 GLN VAL GLN LEU VAL GLN SER GLY ALA GLU VAL LYS LYS SEQRES 2 H 230 PRO GLY ALA SER VAL LYS VAL SER CYS GLN ALA SER GLY SEQRES 3 H 230 TYR ARG PHE SER ASN PHE VAL ILE HIS TRP VAL ARG GLN SEQRES 4 H 230 ALA PRO GLY GLN ARG PHE GLU TRP MET GLY TRP ILE ASN SEQRES 5 H 230 PRO TYR ASN GLY ASN LYS GLU PHE SER ALA LYS PHE GLN SEQRES 6 H 230 ASP ARG VAL THR PHE THR ALA ASP THR SER ALA ASN THR SEQRES 7 H 230 ALA TYR MET GLU LEU ARG SER LEU ARG SER ALA ASP THR SEQRES 8 H 230 ALA VAL TYR TYR CYS ALA ARG VAL GLY PRO TYR SER TRP SEQRES 9 H 230 ASP ASP SER PRO GLN ASP ASN TYR TYR MET ASP VAL TRP SEQRES 10 H 230 GLY LYS GLY THR THR VAL ILE VAL SER SER ALA SER THR SEQRES 11 H 230 LYS GLY PRO SER VAL PHE PRO LEU ALA PRO SER SER LYS SEQRES 12 H 230 SER THR SER GLY GLY THR ALA ALA LEU GLY CYS LEU VAL SEQRES 13 H 230 LYS ASP TYR PHE PRO GLU PRO VAL THR VAL SER TRP ASN SEQRES 14 H 230 SER GLY ALA LEU THR SER GLY VAL HIS THR PHE PRO ALA SEQRES 15 H 230 VAL LEU GLN SER SER GLY LEU TYR SER LEU SER SER VAL SEQRES 16 H 230 VAL THR VAL PRO SER SER SER LEU GLY THR GLN THR TYR SEQRES 17 H 230 ILE CYS ASN VAL ASN HIS LYS PRO SER ASN THR LYS VAL SEQRES 18 H 230 ASP LYS LYS VAL GLU PRO LYS SER CYS SEQRES 1 M 215 GLU ILE VAL LEU THR GLN SER PRO GLY THR LEU SER LEU SEQRES 2 M 215 SER PRO GLY GLU ARG ALA THR PHE SER CYS ARG SER SER SEQRES 3 M 215 HIS SER ILE ARG SER ARG ARG VAL ALA TRP TYR GLN HIS SEQRES 4 M 215 LYS PRO GLY GLN ALA PRO ARG LEU VAL ILE HIS GLY VAL SEQRES 5 M 215 SER ASN ARG ALA SER GLY ILE SER ASP ARG PHE SER GLY SEQRES 6 M 215 SER GLY SER GLY THR ASP PHE THR LEU THR ILE THR ARG SEQRES 7 M 215 VAL GLU PRO GLU ASP PHE ALA LEU TYR TYR CYS GLN VAL SEQRES 8 M 215 TYR GLY ALA SER SER TYR THR PHE GLY GLN GLY THR LYS SEQRES 9 M 215 LEU GLU ARG LYS ARG THR VAL ALA ALA PRO SER VAL PHE SEQRES 10 M 215 ILE PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR SEQRES 11 M 215 ALA SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG SEQRES 12 M 215 GLU ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SEQRES 13 M 215 SER GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER SEQRES 14 M 215 LYS ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SEQRES 15 M 215 SER LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS SEQRES 16 M 215 GLU VAL THR HIS GLN GLY LEU ARG SER PRO VAL THR LYS SEQRES 17 M 215 SER PHE ASN ARG GLY GLU CYS SEQRES 1 K 230 GLN VAL GLN LEU VAL GLN SER GLY ALA GLU VAL LYS LYS SEQRES 2 K 230 PRO GLY ALA SER VAL LYS VAL SER CYS GLN ALA SER GLY SEQRES 3 K 230 TYR ARG PHE SER ASN PHE VAL ILE HIS TRP VAL ARG GLN SEQRES 4 K 230 ALA PRO GLY GLN ARG PHE GLU TRP MET GLY TRP ILE ASN SEQRES 5 K 230 PRO TYR ASN GLY ASN LYS GLU PHE SER ALA LYS PHE GLN SEQRES 6 K 230 ASP ARG VAL THR PHE THR ALA ASP THR SER ALA ASN THR SEQRES 7 K 230 ALA TYR MET GLU LEU ARG SER LEU ARG SER ALA ASP THR SEQRES 8 K 230 ALA VAL TYR TYR CYS ALA ARG VAL GLY PRO TYR SER TRP SEQRES 9 K 230 ASP ASP SER PRO GLN ASP ASN TYR TYR MET ASP VAL TRP SEQRES 10 K 230 GLY LYS GLY THR THR VAL ILE VAL SER SER ALA SER THR SEQRES 11 K 230 LYS GLY PRO SER VAL PHE PRO LEU ALA PRO SER SER LYS SEQRES 12 K 230 SER THR SER GLY GLY THR ALA ALA LEU GLY CYS LEU VAL SEQRES 13 K 230 LYS ASP TYR PHE PRO GLU PRO VAL THR VAL SER TRP ASN SEQRES 14 K 230 SER GLY ALA LEU THR SER GLY VAL HIS THR PHE PRO ALA SEQRES 15 K 230 VAL LEU GLN SER SER GLY LEU TYR SER LEU SER SER VAL SEQRES 16 K 230 VAL THR VAL PRO SER SER SER LEU GLY THR GLN THR TYR SEQRES 17 K 230 ILE CYS ASN VAL ASN HIS LYS PRO SER ASN THR LYS VAL SEQRES 18 K 230 ASP LYS LYS VAL GLU PRO LYS SER CYS SEQRES 1 P 21 HIS GLU ARG SER TYR MET PHE SER ASP LEU GLU ASN ARG SEQRES 2 P 21 CYS ILE ALA ALA GLU ORN LYS LYS SEQRES 1 R 21 HIS GLU ARG SER TYR MET PHE SER ASP LEU GLU ASN ARG SEQRES 2 R 21 CYS ILE ALA ALA GLU ORN LYS LYS MODRES 1N0X ORN P 19 ALA ORNITHINE MODRES 1N0X ORN R 19 ALA ORNITHINE HET ORN P 19 5 HET ORN R 19 5 HET SO4 901 5 HET SO4 902 5 HET SO4 903 5 HET SO4 904 5 HET K 1001 1 HET CXS 1201 14 HET GOL 801 6 HET GOL 803 6 HET GOL 804 6 HET GOL 805 6 HET GOL 806 6 HET GOL 808 6 HET GOL 809 6 HET GOL 800 6 HETNAM ORN ORNITHINE HETNAM SO4 SULFATE ION HETNAM K POTASSIUM ION HETNAM CXS 3-CYCLOHEXYL-1-PROPYLSULFONIC ACID HETNAM GOL GLYCEROL FORMUL 5 ORN 2(C5 H14 N2 O2 2+) FORMUL 7 SO4 4(O4 S 2-) FORMUL 11 K K 1+ FORMUL 12 CXS C9 H19 N O3 S FORMUL 13 GOL 8(C3 H8 O3) FORMUL 21 HOH *725(H2 O) HELIX 1 1 GLU L 79 PHE L 83 5 5 HELIX 2 2 SER L 121 LYS L 126 1 6 HELIX 3 3 LYS L 183 LYS L 188 1 6 HELIX 4 4 ARG H 28 PHE H 32 5 5 HELIX 5 5 THR H 73 ALA H 75 5 3 HELIX 6 6 ARG H 83 THR H 87 5 5 HELIX 7 7 SER H 163 ALA H 165 5 3 HELIX 8 8 PRO H 194 LEU H 198 5 5 HELIX 9 9 LYS H 213 ASN H 216 5 4 HELIX 10 10 GLU M 79 PHE M 83 5 5 HELIX 11 11 SER M 121 GLY M 128 1 8 HELIX 12 12 LYS M 183 LYS M 188 1 6 HELIX 13 13 ARG K 28 PHE K 32 5 5 HELIX 14 14 ALA K 61 GLN K 64 5 4 HELIX 15 15 ARG K 83 THR K 87 5 5 HELIX 16 16 SER K 163 ALA K 165 5 3 HELIX 17 17 SER K 196 LEU K 198 5 3 HELIX 18 18 LYS K 213 ASN K 216 5 4 SHEET 1 A 4 LEU L 4 SER L 7 0 SHEET 2 A 4 ALA L 19 SER L 25 -1 O ARG L 24 N THR L 5 SHEET 3 A 4 ASP L 70 ILE L 75 -1 O LEU L 73 N PHE L 21 SHEET 4 A 4 PHE L 62 SER L 67 -1 N SER L 65 O THR L 72 SHEET 1 B 6 THR L 10 LEU L 13 0 SHEET 2 B 6 THR L 102 ARG L 106 1 O LYS L 103 N LEU L 11 SHEET 3 B 6 ALA L 84 VAL L 90 -1 N ALA L 84 O LEU L 104 SHEET 4 B 6 VAL L 33 HIS L 38 -1 N HIS L 38 O LEU L 85 SHEET 5 B 6 ARG L 45 HIS L 49 -1 O VAL L 47 N TRP L 35 SHEET 6 B 6 ASN L 53 ARG L 54 -1 O ASN L 53 N HIS L 49 SHEET 1 C 4 SER L 114 PHE L 118 0 SHEET 2 C 4 THR L 129 PHE L 139 -1 O LEU L 135 N PHE L 116 SHEET 3 C 4 TYR L 173 SER L 182 -1 O LEU L 179 N VAL L 132 SHEET 4 C 4 SER L 159 VAL L 163 -1 N GLN L 160 O THR L 178 SHEET 1 D 4 ALA L 153 LEU L 154 0 SHEET 2 D 4 LYS L 145 VAL L 150 -1 N VAL L 150 O ALA L 153 SHEET 3 D 4 VAL L 191 THR L 197 -1 O GLU L 195 N GLN L 147 SHEET 4 D 4 VAL L 205 ASN L 210 -1 O VAL L 205 N VAL L 196 SHEET 1 E 4 GLN H 3 GLN H 6 0 SHEET 2 E 4 VAL H 18 SER H 25 -1 O GLN H 23 N VAL H 5 SHEET 3 E 4 THR H 77 LEU H 82 -1 O MET H 80 N VAL H 20 SHEET 4 E 4 VAL H 67 ASP H 72 -1 N THR H 70 O TYR H 79 SHEET 1 F 5 LYS H 57 PHE H 59 0 SHEET 2 F 5 GLU H 46 ILE H 51 -1 N TRP H 50 O GLU H 58 SHEET 3 F 5 ILE H 34 GLN H 39 -1 N ARG H 38 O GLU H 46 SHEET 4 F 5 ALA H 88 ARG H 94 -1 O TYR H 91 N VAL H 37 SHEET 5 F 5 VAL H 102 TRP H 103 -1 O VAL H 102 N ARG H 94 SHEET 1 G 6 LYS H 57 PHE H 59 0 SHEET 2 G 6 GLU H 46 ILE H 51 -1 N TRP H 50 O GLU H 58 SHEET 3 G 6 ILE H 34 GLN H 39 -1 N ARG H 38 O GLU H 46 SHEET 4 G 6 ALA H 88 ARG H 94 -1 O TYR H 91 N VAL H 37 SHEET 5 G 6 THR H 107 VAL H 111 -1 O THR H 107 N TYR H 90 SHEET 6 G 6 GLU H 10 LYS H 12 1 N LYS H 12 O ILE H 110 SHEET 1 H 4 SER H 120 LEU H 124 0 SHEET 2 H 4 ALA H 138 TYR H 147 -1 O LEU H 143 N PHE H 122 SHEET 3 H 4 TYR H 185 VAL H 193 -1 O TYR H 185 N TYR H 147 SHEET 4 H 4 VAL H 171 THR H 173 -1 N HIS H 172 O VAL H 190 SHEET 1 I 4 SER H 120 LEU H 124 0 SHEET 2 I 4 ALA H 138 TYR H 147 -1 O LEU H 143 N PHE H 122 SHEET 3 I 4 TYR H 185 VAL H 193 -1 O TYR H 185 N TYR H 147 SHEET 4 I 4 VAL H 177 LEU H 178 -1 N VAL H 177 O SER H 186 SHEET 1 J 3 THR H 153 TRP H 157 0 SHEET 2 J 3 ILE H 207 HIS H 212 -1 O ASN H 209 N SER H 156 SHEET 3 J 3 THR H 217 LYS H 222 -1 O VAL H 219 N VAL H 210 SHEET 1 K 4 LEU M 4 SER M 7 0 SHEET 2 K 4 ALA M 19 SER M 25 -1 O ARG M 24 N THR M 5 SHEET 3 K 4 ASP M 70 ILE M 75 -1 O LEU M 73 N PHE M 21 SHEET 4 K 4 PHE M 62 SER M 67 -1 N SER M 63 O THR M 74 SHEET 1 L 5 ASN M 53 ARG M 54 0 SHEET 2 L 5 ARG M 45 HIS M 49 -1 N HIS M 49 O ASN M 53 SHEET 3 L 5 VAL M 33 HIS M 38 -1 N TRP M 35 O VAL M 47 SHEET 4 L 5 ALA M 84 VAL M 90 -1 O GLN M 89 N ALA M 34 SHEET 5 L 5 THR M 97 PHE M 98 -1 O THR M 97 N VAL M 90 SHEET 1 M 6 ASN M 53 ARG M 54 0 SHEET 2 M 6 ARG M 45 HIS M 49 -1 N HIS M 49 O ASN M 53 SHEET 3 M 6 VAL M 33 HIS M 38 -1 N TRP M 35 O VAL M 47 SHEET 4 M 6 ALA M 84 VAL M 90 -1 O GLN M 89 N ALA M 34 SHEET 5 M 6 THR M 102 ARG M 106 -1 O LEU M 104 N ALA M 84 SHEET 6 M 6 THR M 10 LEU M 13 1 N LEU M 11 O LYS M 103 SHEET 1 N 4 SER M 114 PHE M 118 0 SHEET 2 N 4 THR M 129 PHE M 139 -1 O VAL M 133 N PHE M 118 SHEET 3 N 4 TYR M 173 SER M 182 -1 O LEU M 179 N VAL M 132 SHEET 4 N 4 SER M 159 VAL M 163 -1 N SER M 162 O SER M 176 SHEET 1 O 4 ALA M 153 LEU M 154 0 SHEET 2 O 4 LYS M 145 VAL M 150 -1 N VAL M 150 O ALA M 153 SHEET 3 O 4 VAL M 191 THR M 197 -1 O GLU M 195 N GLN M 147 SHEET 4 O 4 VAL M 205 ASN M 210 -1 O VAL M 205 N VAL M 196 SHEET 1 P 4 GLN K 3 GLN K 6 0 SHEET 2 P 4 VAL K 18 SER K 25 -1 O GLN K 23 N VAL K 5 SHEET 3 P 4 THR K 77 LEU K 82 -1 O ALA K 78 N CYS K 22 SHEET 4 P 4 VAL K 67 ASP K 72 -1 N THR K 70 O TYR K 79 SHEET 1 Q 5 LYS K 57 PHE K 59 0 SHEET 2 Q 5 GLU K 46 ILE K 51 -1 N TRP K 50 O GLU K 58 SHEET 3 Q 5 ILE K 34 GLN K 39 -1 N ARG K 38 O GLU K 46 SHEET 4 Q 5 ALA K 88 ARG K 94 -1 O TYR K 91 N VAL K 37 SHEET 5 Q 5 VAL K 102 TRP K 103 -1 O VAL K 102 N ARG K 94 SHEET 1 R 6 LYS K 57 PHE K 59 0 SHEET 2 R 6 GLU K 46 ILE K 51 -1 N TRP K 50 O GLU K 58 SHEET 3 R 6 ILE K 34 GLN K 39 -1 N ARG K 38 O GLU K 46 SHEET 4 R 6 ALA K 88 ARG K 94 -1 O TYR K 91 N VAL K 37 SHEET 5 R 6 THR K 107 VAL K 111 -1 O THR K 107 N TYR K 90 SHEET 6 R 6 GLU K 10 LYS K 12 1 N LYS K 12 O ILE K 110 SHEET 1 S 4 SER K 120 LEU K 124 0 SHEET 2 S 4 THR K 137 TYR K 147 -1 O LEU K 143 N PHE K 122 SHEET 3 S 4 TYR K 185 PRO K 194 -1 O VAL K 193 N ALA K 138 SHEET 4 S 4 VAL K 171 THR K 173 -1 N HIS K 172 O VAL K 190 SHEET 1 T 4 SER K 120 LEU K 124 0 SHEET 2 T 4 THR K 137 TYR K 147 -1 O LEU K 143 N PHE K 122 SHEET 3 T 4 TYR K 185 PRO K 194 -1 O VAL K 193 N ALA K 138 SHEET 4 T 4 VAL K 177 LEU K 178 -1 N VAL K 177 O SER K 186 SHEET 1 U 3 THR K 153 TRP K 157 0 SHEET 2 U 3 ILE K 207 HIS K 212 -1 O ASN K 209 N SER K 156 SHEET 3 U 3 THR K 217 LYS K 222 -1 O VAL K 219 N VAL K 210 SHEET 1 V 2 TYR P 5 SER P 8 0 SHEET 2 V 2 ARG P 13 ALA P 16 -1 O ILE P 15 N MET P 6 SHEET 1 W 2 TYR R 5 SER R 8 0 SHEET 2 W 2 ARG R 13 ALA R 16 -1 O ILE R 15 N MET R 6 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 142 CYS H 208 SSBOND 5 CYS M 23 CYS M 88 SSBOND 6 CYS M 134 CYS M 194 SSBOND 7 CYS M 214 CYS K 230 SSBOND 8 CYS K 22 CYS K 92 SSBOND 9 CYS K 142 CYS K 208 SSBOND 10 CYS P 14 CYS R 14 CISPEP 1 SER L 7 PRO L 8 0 -0.18 CISPEP 2 TYR L 140 PRO L 141 0 -0.01 CISPEP 3 PHE H 148 PRO H 149 0 -0.33 CISPEP 4 GLU H 150 PRO H 151 0 -0.17 CISPEP 5 SER M 7 PRO M 8 0 -0.67 CISPEP 6 TYR M 140 PRO M 141 0 -0.36 CISPEP 7 PHE K 148 PRO K 149 0 -0.50 CISPEP 8 GLU K 150 PRO K 151 0 -0.05 CRYST1 51.621 184.358 56.173 90.00 103.05 90.00 P 1 21 1 4 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 0.019372 0.000000 0.004490 0.00000 SCALE2 0.000000 0.005424 0.000000 0.00000 SCALE3 0.000000 0.000000 0.018274 0.00000