HEADER VIRAL PROTEIN/IMMUNE SYSTEM 04-JUN-04 1TJH TITLE CRYSTAL STRUCTURE OF THE BROADLY NEUTRALIZING ANTI-HIV-1 TITLE 2 ANTIBODY 2F5 IN COMPLEX WITH A GP41 11MER EPITOPE COMPND MOL_ID: 1; COMPND 2 MOLECULE: ANTI-HIV-1 ANTIBODY 2F5 LIGHT CHAIN; COMPND 3 CHAIN: L; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: ANTI-HIV-1 ANTIBODY 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 1TJH 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. 2.10 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) : 2.10 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000 REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 236355.730 REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000 REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 90.4 REMARK 3 NUMBER OF REFLECTIONS : 35852 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) : 0.200 REMARK 3 FREE R VALUE : 0.233 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.000 REMARK 3 FREE R VALUE TEST SET COUNT : 3619 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) : 2.10 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.23 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 67.50 REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 3958 REMARK 3 BIN R VALUE (WORKING SET) : 0.3010 REMARK 3 BIN FREE R VALUE : 0.3240 REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 9.30 REMARK 3 BIN FREE R VALUE TEST SET COUNT : 408 REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.016 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 3522 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 8 REMARK 3 SOLVENT ATOMS : 510 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 19.90 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 40.90 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 5.24000 REMARK 3 B22 (A**2) : 1.86000 REMARK 3 B33 (A**2) : -7.10000 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) : 0.24 REMARK 3 ESD FROM SIGMAA (A) : 0.29 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) : 0.30 REMARK 3 ESD FROM C-V SIGMAA (A) : 0.32 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. REMARK 3 BOND LENGTHS (A) : 0.006 REMARK 3 BOND ANGLES (DEGREES) : 1.40 REMARK 3 DIHEDRAL ANGLES (DEGREES) : 27.20 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) : 1.400 ; 1.500 REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.300 ; 2.000 REMARK 3 SIDE-CHAIN BOND (A**2) : 2.080 ; 2.000 REMARK 3 SIDE-CHAIN ANGLE (A**2) : 3.040 ; 2.500 REMARK 3 REMARK 3 BULK SOLVENT MODELING. REMARK 3 METHOD USED : FLAT MODEL REMARK 3 KSOL : 0.35 REMARK 3 BSOL : 84.48 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 : CAPPING.PARAM REMARK 3 PARAMETER FILE 6 : 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 : CAPPING.TOP REMARK 3 TOPOLOGY FILE 6 : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1TJH 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 RCSB022687. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 04-JUN-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 : 45339 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100 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 (%) : 96.4 REMARK 200 DATA REDUNDANCY : 6.600 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : 0.08400 REMARK 200 FOR THE DATA SET : 19.4000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.18 REMARK 200 COMPLETENESS FOR SHELL (%) : 72.4 REMARK 200 DATA REDUNDANCY IN SHELL : 3.60 REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : 0.38500 REMARK 200 FOR SHELL : 1.570 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: DIFFERENCE FOURIER REMARK 200 METHOD REMARK 200 SOFTWARE USED: CNS REMARK 200 STARTING MODEL: PDB ENTRY 1TJG REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 62.30 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.33 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG 4000, 20% ISOPROPANOL, 0.1 REMARK 280 M NACITRATE, 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 29.14300 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 89.46750 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 31.76100 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 89.46750 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 29.14300 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 31.76100 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 MET H 82 SD MET H 82 CE -0.036 REMARK 500 PRO H 149 CG PRO H 149 CD 0.035 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 51 N - CA - C ANGL. DEV. = 8.6 DEGREES REMARK 500 TYR L 94 N - CA - C ANGL. DEV. = -9.1 DEGREES REMARK 500 HIS L 96 N - CA - C ANGL. DEV. = -9.7 DEGREES REMARK 500 SER L 114 N - CA - C ANGL. DEV. =-11.4 DEGREES REMARK 500 SER H 60 N - CA - C ANGL. DEV. = -9.6 DEGREES REMARK 500 ASP H 72 N - CA - C ANGL. DEV. = -9.4 DEGREES REMARK 500 THR H 89 N - CA - C ANGL. DEV. = -8.6 DEGREES REMARK 500 GLY H 97 N - CA - C ANGL. DEV. = -9.1 DEGREES REMARK 500 GLY H 100I N - CA - C ANGL. DEV. = 10.4 DEGREES REMARK 500 MET H 100N N - CA - C ANGL. DEV. =-13.3 DEGREES REMARK 500 ASP H 101 N - CA - C ANGL. DEV. = 8.6 DEGREES REMARK 500 SER H 120 N - CA - C ANGL. DEV. =-11.7 DEGREES REMARK 500 LEU H 124 N - CA - C ANGL. DEV. =-12.0 DEGREES REMARK 500 LYS H 143 N - CA - C ANGL. DEV. = 8.7 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 -40.25 70.95 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 190 DISTANCE = 11.14 ANGSTROMS REMARK 525 HOH 233 DISTANCE = 6.26 ANGSTROMS REMARK 525 HOH 373 DISTANCE = 7.57 ANGSTROMS REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 2F5B RELATED DB: PDB REMARK 900 2F5 IN COMPLEX WITH ITS GP41 EPITOPE REMARK 900 RELATED ID: 1TJG RELATED DB: PDB REMARK 900 2F5 FAB COMPLEXED WITH A GP41 7MER REMARK 900 RELATED ID: 1TJI RELATED DB: PDB REMARK 900 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 NUMBERED REMARK 999 IN KABAT FORMAT. DBREF 1TJH P 660 670 UNP P04580 ENV_HV1Z6 659 669 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 11 LEU LEU GLU LEU ASP LYS TRP ALA SER LEU TRP MODRES 1TJH YCM L 214 CYS MODRES 1TJH YCM H 216 CYS HET YCM L 214 11 HET YCM H 216 10 HET ACE P 659 3 HET NH2 P 671 1 HET EDO 771 4 HET EDO 772 4 HET IPA 661 4 HET IPA 662 4 HET IPA 663 4 HET IPA 664 4 HET IPA 665 4 HET IPA 666 4 HETNAM YCM S-(2-AMINO-2-OXOETHYL)-L-CYSTEINE HETNAM ACE ACETYL GROUP HETNAM NH2 AMINO GROUP 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 ACE C2 H4 O FORMUL 5 NH2 H2 N FORMUL 6 EDO 2(C2 H6 O2) FORMUL 8 IPA 6(C3 H8 O) FORMUL 14 HOH *486(H2 O) HELIX 1 1 ARG L 79 PHE L 83 5 5 HELIX 2 2 SER L 121 SER L 127 1 7 HELIX 3 3 LYS L 183 GLU L 187 1 5 HELIX 4 4 SER H 83 THR H 87 5 5 HELIX 5 5 ARG H 100H ASN H 100L 5 5 HELIX 6 6 SER H 127 LYS H 129 5 3 HELIX 7 7 SER H 156 ALA H 158 5 3 HELIX 8 8 SER H 187 LEU H 189 5 3 HELIX 9 9 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 GLY L 66 -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 2 PHE L 93 TYR L 94 0 SHEET 2 D 2 GLU P 662 LEU P 663 -1 O GLU P 662 N TYR L 94 SHEET 1 E 4 SER L 114 PHE L 118 0 SHEET 2 E 4 THR L 129 PHE L 139 -1 O LEU L 135 N PHE L 116 SHEET 3 E 4 TYR L 173 SER L 182 -1 O LEU L 179 N VAL L 132 SHEET 4 E 4 SER L 159 VAL L 163 -1 N GLN L 160 O THR L 178 SHEET 1 F 4 ALA L 153 GLN L 155 0 SHEET 2 F 4 LYS L 145 VAL L 150 -1 N TRP L 148 O GLN L 155 SHEET 3 F 4 VAL L 191 THR L 197 -1 O ALA L 193 N LYS L 149 SHEET 4 F 4 VAL L 205 ASN L 210 -1 O VAL L 205 N VAL L 196 SHEET 1 G 4 THR H 3 SER H 7 0 SHEET 2 G 4 LEU H 18 SER H 25 -1 O SER H 23 N LYS H 5 SHEET 3 G 4 GLN H 77 MET H 82 -1 O MET H 82 N LEU H 18 SHEET 4 G 4 LEU H 67 ASP H 72 -1 N THR H 68 O VAL H 81 SHEET 1 H 6 LEU H 11 VAL H 12 0 SHEET 2 H 6 ILE H 107 ILE H 111 1 O THR H 110 N VAL H 12 SHEET 3 H 6 ALA H 88 ARG H 95 -1 N TYR H 90 O ILE H 107 SHEET 4 H 6 GLY H 35 GLN H 39 -1 N ILE H 37 O PHE H 91 SHEET 5 H 6 GLU H 46 TYR H 52 -1 O GLU H 46 N ARG H 38 SHEET 6 H 6 LYS H 57 TYR H 59 -1 O ARG H 58 N ILE H 50 SHEET 1 I 4 LEU H 11 VAL H 12 0 SHEET 2 I 4 ILE H 107 ILE H 111 1 O THR H 110 N VAL H 12 SHEET 3 I 4 ALA H 88 ARG H 95 -1 N TYR H 90 O ILE H 107 SHEET 4 I 4 VAL H 102 TRP H 103 -1 O VAL H 102 N HIS H 94 SHEET 1 J 2 THR H 99 LEU H 100A 0 SHEET 2 J 2 VAL H 100D ALA H 100G-1 O VAL H 100D N LEU H 100A SHEET 1 K 4 SER H 120 LEU H 124 0 SHEET 2 K 4 THR H 135 TYR H 145 -1 O GLY H 139 N LEU H 124 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 163 THR H 165 -1 N HIS H 164 O VAL H 181 SHEET 1 L 4 THR H 131 SER H 132 0 SHEET 2 L 4 THR H 135 TYR H 145 -1 O THR H 135 N SER H 132 SHEET 3 L 4 TYR H 176 PRO H 185 -1 O VAL H 184 N ALA H 136 SHEET 4 L 4 VAL H 169 LEU H 170 -1 N VAL H 169 O SER H 177 SHEET 1 M 3 THR H 151 TRP H 154 0 SHEET 2 M 3 ILE H 195 HIS H 200 -1 O ASN H 197 N SER H 153 SHEET 3 M 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 LINK C ACE P 659 N LEU P 660 LINK C TRP P 670 N NH2 P 671 CISPEP 1 SER L 7 PRO L 8 0 -0.12 CISPEP 2 TYR L 94 PRO L 95 0 -0.38 CISPEP 3 TYR L 140 PRO L 141 0 0.06 CISPEP 4 PHE H 146 PRO H 147 0 0.01 CISPEP 5 GLU H 148 PRO H 149 0 0.18 CRYST1 58.286 63.522 178.935 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 0.017157 0.000000 0.000000 0.00000 SCALE2 0.000000 0.015743 0.000000 0.00000 SCALE3 0.000000 0.000000 0.005589 0.00000