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HEADER VIRAL PROTEIN/IMMUNE SYSTEM 04-JUN-04 1TJG TITLE CRYSTAL STRUCTURE OF THE BROADLY NEUTRALIZING ANTI-HIV-1 TITLE 2 ANTIBODY 2F5 IN COMPLEX WITH A GP41 7MER EPITOPE COMPND MOL_ID: 1; COMPND 2 MOLECULE: FAB 2F5 LIGHT CHAIN; COMPND 3 CHAIN: L; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: FAB 2F5 HEAVY CHAIN; COMPND 7 CHAIN: H; COMPND 8 ENGINEERED: YES; COMPND 9 MOL_ID: 3; COMPND 10 MOLECULE: ENVELOPE GLYCOPROTEIN GP41; COMPND 11 CHAIN: P; COMPND 12 FRAGMENT: TRANSMEMBRANE GLYCOPROTEIN (RESIDUES 659-669); COMPND 13 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_CELL_LINE: CB-F7; SOURCE 6 OTHER_DETAILS: HETEROMYELOMA CELL LINE CB-F7 FUSED WITH SOURCE 7 PERIPHERAL BLOOD MONONUCLEAR 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_CELL_LINE: CB-F7; SOURCE 13 OTHER_DETAILS: HETEROMYELOMA CELL LINE CB-F7 FUSED WITH SOURCE 14 PERIPHERAL BLOOD MONONUCLEAR CELLS; SOURCE 15 MOL_ID: 3; SOURCE 16 SYNTHETIC: YES; SOURCE 17 OTHER_DETAILS: THE PEPTIDE WAS CHEMICALLY SYNTHESIZED. THE SOURCE 18 SEQUENCE OF THE PEPTIDE IS NATURALLY FOUND IN THE HUMAN SOURCE 19 IMMUNODEFICIENCY VIRUS (HIV-1; STRAIN JRFL). KEYWDS 2F5; ANTIBODY; GP41; HIV-1; NEUTRALIZING; MEMBRANE-PROXIMAL EXPDTA X-RAY DIFFRACTION AUTHOR G.OFEK,M.TANG,A.SAMBOR,H.KATINGER,J.R.MASCOLA,R.WYATT, AUTHOR 2 P.D.KWONG REVDAT 1 05-OCT-04 1TJG 0 JRNL AUTH G.OFEK,M.TANG,A.SAMBOR,H.KATINGER,J.R.MASCOLA, JRNL AUTH 2 R.WYATT,P.D.KWONG JRNL TITL STRUCTURE AND MECHANISTIC ANALYSIS OF THE JRNL TITL 2 ANTI-HUMAN IMMUNODEFICIENCY VIRUS TYPE 1 ANTIBODY JRNL TITL 3 2F5 IN COMPLEX WITH ITS GP41 EPITOPE JRNL REF J.VIROL. V. 78 10724 2004 JRNL REFN ASTM JOVIAM US ISSN 0022-538X REMARK 1 REMARK 2 REMARK 2 RESOLUTION. 2.00 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : CNS 1.1 REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE- REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU, REMARK 3 : READ,RICE,SIMONSON,WARREN REMARK 3 REMARK 3 REFINEMENT TARGET : ENGH & HUBER REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000 REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 440552.360 REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000 REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 90.7 REMARK 3 NUMBER OF REFLECTIONS : 40962 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) : 0.198 REMARK 3 FREE R VALUE : 0.225 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.000 REMARK 3 FREE R VALUE TEST SET COUNT : 4108 REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.004 REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : 6 REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.00 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.13 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 66.50 REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 4522 REMARK 3 BIN R VALUE (WORKING SET) : 0.2790 REMARK 3 BIN FREE R VALUE : 0.3110 REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 9.70 REMARK 3 BIN FREE R VALUE TEST SET COUNT : 486 REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.014 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 3481 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 12 REMARK 3 SOLVENT ATOMS : 419 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 14.00 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 31.70 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 1.36000 REMARK 3 B22 (A**2) : 2.79000 REMARK 3 B33 (A**2) : -4.14000 REMARK 3 B12 (A**2) : 0.00000 REMARK 3 B13 (A**2) : 0.00000 REMARK 3 B23 (A**2) : 0.00000 REMARK 3 REMARK 3 ESTIMATED COORDINATE ERROR. REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.23 REMARK 3 ESD FROM SIGMAA (A) : 0.24 REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00 REMARK 3 REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR. REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.27 REMARK 3 ESD FROM C-V SIGMAA (A) : 0.26 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. REMARK 3 BOND LENGTHS (A) : 0.006 REMARK 3 BOND ANGLES (DEGREES) : 1.30 REMARK 3 DIHEDRAL ANGLES (DEGREES) : 27.00 REMARK 3 IMPROPER ANGLES (DEGREES) : 0.86 REMARK 3 REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED REMARK 3 REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA REMARK 3 MAIN-CHAIN BOND (A**2) : 1.410 ; 1.500 REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.250 ; 2.000 REMARK 3 SIDE-CHAIN BOND (A**2) : 2.210 ; 2.000 REMARK 3 SIDE-CHAIN ANGLE (A**2) : 3.260 ; 2.500 REMARK 3 REMARK 3 BULK SOLVENT MODELING. REMARK 3 METHOD USED : FLAT MODEL REMARK 3 KSOL : 0.35 REMARK 3 BSOL : 54.11 REMARK 3 REMARK 3 NCS MODEL : NULL REMARK 3 REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL REMARK 3 REMARK 3 PARAMETER FILE 1 : PROTEIN_REP.PARAM REMARK 3 PARAMETER FILE 2 : WATER_REP.PARAM REMARK 3 PARAMETER FILE 3 : IOH_XPLOR_PARAM REMARK 3 PARAMETER FILE 4 : EGL_XPLOR_PARAM REMARK 3 PARAMETER FILE 5 : NULL REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP REMARK 3 TOPOLOGY FILE 2 : WATER.TOP REMARK 3 TOPOLOGY FILE 3 : IOH_XPLOR_TOP REMARK 3 TOPOLOGY FILE 4 : EGL_XPLOR_TOP REMARK 3 TOPOLOGY FILE 5 : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1TJG 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 (2007-03-17) REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB. REMARK 100 THE RCSB ID CODE IS RCSB022686. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 12-MAR-2003 REMARK 200 TEMPERATURE (KELVIN) : 100.0 REMARK 200 PH : 5.60 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : APS REMARK 200 BEAMLINE : 22-ID REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1 REMARK 200 MONOCHROMATOR : SI (220) REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000 REMARK 200 DATA SCALING SOFTWARE : SCALEPACK REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 43466 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000 REMARK 200 RESOLUTION RANGE LOW (A) : 20.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 97.1 REMARK 200 DATA REDUNDANCY : 4.000 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : 0.08900 REMARK 200 FOR THE DATA SET : 7.5000 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) : 2.07 REMARK 200 COMPLETENESS FOR SHELL (%) : 92.1 REMARK 200 DATA REDUNDANCY IN SHELL : 3.00 REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : 0.53000 REMARK 200 FOR SHELL : 1.470 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 1RZG REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 63.00 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.37 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG 4000, 20% ISOPROPANOL, 0.1M REMARK 280 SODIUM CITRATE, PH 5.6, VAPOR DIFFUSION, HANGING DROP, REMARK 280 TEMPERATURE 293K, PH 5.60 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 28.93000 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 89.70500 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 32.01000 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 89.70500 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 28.93000 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 32.01000 REMARK 290 SMTRY3 4 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 3 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, P 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 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 H 149 CG PRO H 149 CD 0.042 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 LEU L 73 N - CA - C ANGL. DEV. = -8.1 DEGREES REMARK 500 ILE L 75 N - CA - C ANGL. DEV. = -8.7 DEGREES REMARK 500 TYR L 94 N - CA - C ANGL. DEV. = -8.8 DEGREES REMARK 500 HIS L 96 N - CA - C ANGL. DEV. = -9.2 DEGREES REMARK 500 SER L 114 N - CA - C ANGL. DEV. =-10.3 DEGREES REMARK 500 LEU L 136 N - CA - C ANGL. DEV. = -8.1 DEGREES REMARK 500 GLY H 33 N - CA - C ANGL. DEV. = 8.1 DEGREES REMARK 500 ASP H 56 N - CA - C ANGL. DEV. = -8.1 DEGREES REMARK 500 SER H 60 N - CA - C ANGL. DEV. = -8.9 DEGREES REMARK 500 CYS H 92 N - CA - C ANGL. DEV. = -9.3 DEGREES REMARK 500 GLY H 97 N - CA - C ANGL. DEV. = -9.3 DEGREES REMARK 500 MET H 100N N - CA - C ANGL. DEV. =-15.1 DEGREES REMARK 500 ASP H 101 N - CA - C ANGL. DEV. = 8.1 DEGREES REMARK 500 SER H 120 N - CA - C ANGL. DEV. =-10.6 DEGREES REMARK 500 LEU H 124 N - CA - C ANGL. DEV. =-11.0 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 -41.21 68.02 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 2F5B RELATED DB: PDB REMARK 900 2F5 IN COMPLEX WITH ITS GP41 EPTIOPE REMARK 900 RELATED ID: 1TJH RELATED DB: PDB REMARK 900 2F5 FAB COMPLEXED WITH A GP41 11MER REMARK 900 RELATED ID: 1TJI RELATED DB: PDB REMARK 900 2F5 FAB COMPLEXED WITH A GP41 17MER REMARK 999 REMARK 999 SEQUENCE REMARK 999 THERE ARE CURRENTLY NO SEQUENCE DATABASE MATCHES REMARK 999 FOR CHAINS L AND H. CHAINS L AND H ARE REMARK 999 NUMBERED IN KABAT FORMAT. DBREF 1TJG P 662 668 UNP Q75760 Q75760_9HIV1 653 659 SEQRES 1 L 214 ALA LEU GLN LEU THR GLN SER PRO SER SER LEU SER ALA SEQRES 2 L 214 SER VAL GLY ASP ARG ILE THR ILE THR CYS ARG ALA SER SEQRES 3 L 214 GLN GLY VAL THR SER ALA LEU ALA TRP TYR ARG GLN LYS SEQRES 4 L 214 PRO GLY SER PRO PRO GLN LEU LEU ILE TYR ASP ALA SER SEQRES 5 L 214 SER LEU GLU SER GLY VAL PRO SER ARG PHE SER GLY SER SEQRES 6 L 214 GLY SER GLY THR GLU PHE THR LEU THR ILE SER THR LEU SEQRES 7 L 214 ARG PRO GLU ASP PHE ALA THR TYR TYR CYS GLN GLN LEU SEQRES 8 L 214 HIS PHE TYR PRO HIS THR PHE GLY GLY GLY THR ARG VAL SEQRES 9 L 214 ASP VAL ARG 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 YCM SEQRES 1 H 237 ARG ILE THR LEU LYS GLU SER GLY PRO PRO LEU VAL LYS SEQRES 2 H 237 PRO THR GLN THR LEU THR LEU THR CYS SER PHE SER GLY SEQRES 3 H 237 PHE SER LEU SER ASP PHE GLY VAL GLY VAL GLY TRP ILE SEQRES 4 H 237 ARG GLN PRO PRO GLY LYS ALA LEU GLU TRP LEU ALA ILE SEQRES 5 H 237 ILE TYR SER ASP ASP ASP LYS ARG TYR SER PRO SER LEU SEQRES 6 H 237 ASN THR ARG LEU THR ILE THR LYS ASP THR SER LYS ASN SEQRES 7 H 237 GLN VAL VAL LEU VAL MET THR ARG VAL SER PRO VAL ASP SEQRES 8 H 237 THR ALA THR TYR PHE CYS ALA HIS ARG ARG GLY PRO THR SEQRES 9 H 237 THR LEU PHE GLY VAL PRO ILE ALA ARG GLY PRO VAL ASN SEQRES 10 H 237 ALA MET ASP VAL TRP GLY GLN GLY ILE THR VAL THR ILE SEQRES 11 H 237 SER SER THR SER THR LYS GLY PRO SER VAL PHE PRO LEU SEQRES 12 H 237 ALA PRO SER SER LYS SER THR SER GLY GLY THR ALA ALA SEQRES 13 H 237 LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU PRO VAL SEQRES 14 H 237 THR VAL SER TRP ASN SER GLY ALA LEU THR SER GLY VAL SEQRES 15 H 237 HIS THR PHE PRO ALA VAL LEU GLN SER SER GLY LEU TYR SEQRES 16 H 237 SER LEU SER SER VAL VAL THR VAL PRO SER SER SER LEU SEQRES 17 H 237 GLY THR GLN THR TYR ILE CYS ASN VAL ASN HIS LYS PRO SEQRES 18 H 237 SER ASN THR LYS VAL ASP LYS LYS VAL GLU PRO LYS SER SEQRES 19 H 237 YCM ASP LYS SEQRES 1 P 7 GLU LEU ASP LYS TRP ALA SER MODRES 1TJG YCM L 214 CYS MODRES 1TJG YCM H 216 CYS HET YCM L 214 11 HET YCM H 216 10 HET EDO 501 4 HET EDO 502 4 HET EDO 503 4 HET IPA 401 4 HET IPA 402 4 HET IPA 403 4 HET IPA 404 4 HET IPA 405 4 HET IPA 406 4 HET IPA 407 4 HETNAM YCM S-(2-AMINO-2-OXOETHYL)-L-CYSTEINE HETNAM EDO 1,2-ETHANEDIOL HETNAM IPA ISOPROPYL ALCOHOL HETSYN YCM CYSTEINE-S-ACETAMIDE HETSYN EDO ETHYLENE GLYCOL FORMUL 1 YCM 2(C5 H10 N2 O3 S) FORMUL 4 EDO 3(C2 H6 O2) FORMUL 7 IPA 7(C3 H8 O) FORMUL 14 HOH *391(H2 O) HELIX 1 1 ARG L 79 PHE L 83 5 5 HELIX 2 2 SER L 121 GLY L 128 1 8 HELIX 3 3 LYS L 183 GLU L 187 1 5 HELIX 4 4 PRO H 61 ASN H 64 5 4 HELIX 5 5 SER H 83 THR H 87 5 5 HELIX 6 6 ARG H 100H ASN H 100L 5 5 HELIX 7 7 SER H 127 LYS H 129 5 3 HELIX 8 8 SER H 156 ALA H 158 5 3 HELIX 9 9 SER H 187 LEU H 189 5 3 HELIX 10 10 LYS H 201 ASN H 204 5 4 SHEET 1 A 4 LEU L 4 SER L 7 0 SHEET 2 A 4 ILE L 19 ALA L 25 -1 O ARG L 24 N THR L 5 SHEET 3 A 4 GLU 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 ALA L 13 0 SHEET 2 B 6 THR L 102 VAL L 106 1 O ARG L 103 N LEU L 11 SHEET 3 B 6 THR L 85 GLN L 90 -1 N TYR L 86 O THR L 102 SHEET 4 B 6 LEU L 33 GLN L 38 -1 N GLN L 38 O THR L 85 SHEET 5 B 6 GLN 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 ALA L 13 0 SHEET 2 C 4 THR L 102 VAL L 106 1 O ARG L 103 N LEU L 11 SHEET 3 C 4 THR L 85 GLN L 90 -1 N TYR L 86 O THR L 102 SHEET 4 C 4 THR L 97 PHE L 98 -1 O THR L 97 N GLN L 90 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 175 N LEU L 136 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 THR H 3 SER H 7 0 SHEET 2 F 4 LEU H 18 SER H 25 -1 O THR H 21 N SER H 7 SHEET 3 F 4 GLN H 77 MET H 82 -1 O MET H 82 N LEU H 18 SHEET 4 F 4 LEU H 67 ASP H 72 -1 N THR H 68 O VAL H 81 SHEET 1 G 6 LEU H 11 VAL H 12 0 SHEET 2 G 6 ILE H 107 ILE H 111 1 O THR H 110 N VAL H 12 SHEET 3 G 6 ALA H 88 ARG H 95 -1 N TYR H 90 O ILE H 107 SHEET 4 G 6 GLY H 35 GLN H 39 -1 N ILE H 37 O PHE H 91 SHEET 5 G 6 GLU H 46 TYR H 52 -1 O GLU H 46 N ARG H 38 SHEET 6 G 6 LYS H 57 TYR H 59 -1 O ARG H 58 N ILE H 50 SHEET 1 H 4 LEU H 11 VAL H 12 0 SHEET 2 H 4 ILE H 107 ILE H 111 1 O THR H 110 N VAL H 12 SHEET 3 H 4 ALA H 88 ARG H 95 -1 N TYR H 90 O ILE H 107 SHEET 4 H 4 VAL H 102 TRP H 103 -1 O VAL H 102 N HIS H 94 SHEET 1 I 2 THR H 99 LEU H 100A 0 SHEET 2 I 2 VAL H 100D ALA H 100G-1 O VAL H 100D N LEU H 100A SHEET 1 J 4 SER H 120 LEU H 124 0 SHEET 2 J 4 THR H 135 TYR H 145 -1 O LEU H 141 N PHE H 122 SHEET 3 J 4 TYR H 176 PRO H 185 -1 O VAL H 184 N ALA H 136 SHEET 4 J 4 VAL H 163 THR H 165 -1 N HIS H 164 O VAL H 181 SHEET 1 K 4 THR H 131 SER H 132 0 SHEET 2 K 4 THR H 135 TYR H 145 -1 O THR H 135 N SER H 132 SHEET 3 K 4 TYR H 176 PRO H 185 -1 O VAL H 184 N ALA H 136 SHEET 4 K 4 VAL H 169 LEU H 170 -1 N VAL H 169 O SER H 177 SHEET 1 L 3 THR H 151 TRP H 154 0 SHEET 2 L 3 ILE H 195 HIS H 200 -1 O ASN H 197 N SER H 153 SHEET 3 L 3 THR H 205 LYS H 210 -1 O VAL H 207 N VAL H 198 SSBOND 1 CYS L 23 CYS L 88 SSBOND 2 CYS L 134 CYS L 194 SSBOND 3 CYS H 22 CYS H 92 SSBOND 4 CYS H 140 CYS H 196 CISPEP 1 SER L 7 PRO L 8 0 -0.12 CISPEP 2 TYR L 94 PRO L 95 0 -0.14 CISPEP 3 TYR L 140 PRO L 141 0 -0.68 CISPEP 4 PHE H 146 PRO H 147 0 -0.13 CISPEP 5 GLU H 148 PRO H 149 0 0.12 CRYST1 57.860 64.020 179.410 90.00 90.00 90.00 P 21 21 21 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 0.017283 0.000000 0.000000 0.00000 SCALE2 0.000000 0.015620 0.000000 0.00000 SCALE3 0.000000 0.000000 0.005574 0.00000