HEADER IMMUNE SYSTEM 03-FEB-06 2FX7 TITLE CRYSTAL STRUCTURE OF HIV-1 NEUTRALIZING HUMAN FAB 4E10 IN TITLE 2 COMPLEX WITH A 16-RESIDUE PEPTIDE ENCOMPASSING THE 4E10 TITLE 3 EPITOPE ON GP41 COMPND MOL_ID: 1; COMPND 2 MOLECULE: FAB 4E10; COMPND 3 CHAIN: L; COMPND 4 FRAGMENT: LIGHT CHAIN; COMPND 5 ENGINEERED: YES; COMPND 6 MOL_ID: 2; COMPND 7 MOLECULE: FAB 4E10; COMPND 8 CHAIN: H; COMPND 9 FRAGMENT: HEAVY CHAIN; COMPND 10 ENGINEERED: YES; COMPND 11 MOL_ID: 3; COMPND 12 MOLECULE: FRAGMENT OF HIV GLYCOPROTEIN (GP41); COMPND 13 CHAIN: P; COMPND 14 FRAGMENT: PEPTIDE EPITOPE OF 4E10; COMPND 15 ENGINEERED: YES; COMPND 16 MUTATION: 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 MOL_ID: 2; SOURCE 7 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 8 ORGANISM_COMMON: HUMAN; SOURCE 9 EXPRESSION_SYSTEM: CRICETULUS GRISEUS; SOURCE 10 EXPRESSION_SYSTEM_COMMON: CHINESE HAMSTER; SOURCE 11 MOL_ID: 3; SOURCE 12 SYNTHETIC: YES; SOURCE 13 OTHER_DETAILS: THIS SEQUENCE INCLUDES A FRAGMENT OF THE SOURCE 14 HIV ENVELOPE PROTEIN GP41 KEYWDS IMMUNOGLOBULIN FOLD, BETA-SANDWICH, ANTIBODY-EPITOPE COMPLEX EXPDTA X-RAY DIFFRACTION AUTHOR R.M.F.CARDOSO,F.M.BRUNEL,S.FERGUSON,D.R.BURTON,P.E.DAWSON, AUTHOR 2 I.A.WILSON REVDAT 2 04-SEP-07 2FX7 1 JRNL REVDAT 1 19-DEC-06 2FX7 0 JRNL AUTH R.M.CARDOSO,F.M.BRUNEL,S.FERGUSON,M.ZWICK, JRNL AUTH 2 D.R.BURTON,P.E.DAWSON,I.A.WILSON JRNL TITL STRUCTURAL BASIS OF ENHANCED BINDING OF EXTENDED JRNL TITL 2 AND HELICALLY CONSTRAINED PEPTIDE EPITOPES OF THE JRNL TITL 3 BROADLY NEUTRALIZING HIV-1 ANTIBODY 4E10. JRNL REF J.MOL.BIOL. V. 365 1533 2007 JRNL REFN ASTM JMOBAK UK ISSN 0022-2836 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH R.M.F.CARDOSO,M.B.ZWICK,R.L.STANFIELD,R.KUNERT, REMARK 1 AUTH 2 J.M.BINLEY,H.KATINGER,D.R.BURTON,I.A.WILSON REMARK 1 TITL BROADLY NEUTRALIZING ANTI-HIV ANTIBODY 4E10 REMARK 1 TITL 2 RECOGNIZES A HELICAL CONFORMATION OF A HIGHLY REMARK 1 TITL 3 CONSERVED FUSION-ASSOCIATED MOTIF IN GP41 REMARK 1 REF IMMUNITY V. 22 163 2005 REMARK 1 REFN ASTM IUNIEH US ISSN 1074-7613 REMARK 2 REMARK 2 RESOLUTION. 1.76 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) : 1.76 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00 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) (%) : 98.7 REMARK 3 NUMBER OF REFLECTIONS : 53993 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) : 0.202 REMARK 3 FREE R VALUE : 0.222 REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL REMARK 3 FREE R VALUE TEST SET COUNT : 2689 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) : 1.76 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.77 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL REMARK 3 BIN R VALUE (WORKING SET) : 0.2770 REMARK 3 BIN FREE R VALUE : 0.3620 REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL REMARK 3 BIN FREE R VALUE TEST SET COUNT : 32 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 : 3486 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 0 REMARK 3 SOLVENT ATOMS : 343 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 18.10 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 24.60 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 2.23100 REMARK 3 B22 (A**2) : -0.36400 REMARK 3 B33 (A**2) : -1.86700 REMARK 3 B12 (A**2) : 0.00000 REMARK 3 B13 (A**2) : -0.92100 REMARK 3 B23 (A**2) : 0.00000 REMARK 3 REMARK 3 ESTIMATED COORDINATE ERROR. REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.20 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) : 0.005 REMARK 3 BOND ANGLES (DEGREES) : 1.30 REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL REMARK 3 IMPROPER ANGLES (DEGREES) : NULL REMARK 3 REMARK 3 ISOTROPIC THERMAL MODEL : ISOTROPIC REMARK 3 REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA REMARK 3 MAIN-CHAIN BOND (A**2) : 1.363 ; NULL REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.206 ; NULL REMARK 3 SIDE-CHAIN BOND (A**2) : 2.033 ; NULL REMARK 3 SIDE-CHAIN ANGLE (A**2) : 3.019 ; NULL REMARK 3 REMARK 3 BULK SOLVENT MODELING. REMARK 3 METHOD USED : NULL REMARK 3 KSOL : 0.40 REMARK 3 BSOL : 47.00 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 2FX7 COMPLIES WITH FORMAT V. 3.0, 1-DEC-2006 REMARK 4 REMARK 4 THIS IS THE REMEDIATED VERSION OF THIS PDB ENTRY. REMARK 4 REMEDIATED DATA FILE REVISION 3.102 (2007-05-29) REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB. REMARK 100 THE RCSB ID CODE IS RCSB036418. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 11-MAR-2005 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 : 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) : 0.97945 REMARK 200 MONOCHROMATOR : CURVED CRYSTAL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : QUANTUM-315 REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000 REMARK 200 DATA SCALING SOFTWARE : SCALEPACK REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 53993 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.760 REMARK 200 RESOLUTION RANGE LOW (A) : 50.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 3.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.3 REMARK 200 DATA REDUNDANCY : 3.700 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : 0.06500 REMARK 200 FOR THE DATA SET : 14.8000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.76 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.82 REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9 REMARK 200 DATA REDUNDANCY IN SHELL : 3.70 REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : 0.30200 REMARK 200 FOR SHELL : 5.200 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: AMORE REMARK 200 STARTING MODEL: PDB ENTRY 1TZG REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 55.98 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.79 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 26% PEG 8000, 0.2 M SODIUM ACETATE, REMARK 280 0.2 M SODIUM THIOCYANATE, PH 5.6, VAPOR DIFFUSION, SITTING REMARK 280 DROP, TEMPERATURE 295K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,Y,-Z REMARK 290 3555 1/2+X,1/2+Y,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 0.00000 REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 78.97000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 22.32900 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 78.97000 REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 22.32900 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: CLOSE CONTACTS REMARK 500 REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15 REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375 REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS. REMARK 500 REMARK 500 DISTANCE CUTOFF: REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE REMARK 500 O HOH 91 O HOH 219 2657 0.59 REMARK 500 O HOH 187 O HOH 330 2657 0.67 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 151 CB PRO H 151 CG 0.029 REMARK 500 PRO H 151 CG PRO H 151 CD 0.033 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. = -9.5 DEGREES REMARK 500 GLY L 99 N - CA - C ANGL. DEV. = -8.4 DEGREES REMARK 500 SER L 114 N - CA - C ANGL. DEV. =-11.1 DEGREES REMARK 500 LEU L 136 N - CA - C ANGL. DEV. =-10.3 DEGREES REMARK 500 ASN L 137 N - CA - C ANGL. DEV. = 8.3 DEGREES REMARK 500 SER H 30 N - CA - C ANGL. DEV. = 8.1 DEGREES REMARK 500 ILE H 52 N - CA - C ANGL. DEV. = -9.4 DEGREES REMARK 500 CYS H 92 N - CA - C ANGL. DEV. = -9.7 DEGREES REMARK 500 SER H 120 N - CA - C ANGL. DEV. =-12.0 DEGREES REMARK 500 LEU H 124 N - CA - C ANGL. DEV. =-12.2 DEGREES REMARK 500 LYS H 145 N - CA - C ANGL. DEV. = 9.4 DEGREES REMARK 500 LEU H 187 CA - CB - CG ANGL. DEV. = 8.1 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 -36.66 69.54 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1TZG RELATED DB: PDB REMARK 900 FAB 4E10 BOUND TO A 13-RESIDUE PEPTIDE EPITOPE REMARK 900 RELATED ID: 2FX8 RELATED DB: PDB REMARK 900 FAB 4E10 BOUND TO AN AIB-INDUCED PEPTIDE EPITOPE REMARK 900 RELATED ID: 2FX9 RELATED DB: PDB REMARK 900 FAB 4E10 BOUND TO A THIOETHER-LINKED PEPTIDE EPITOPE REMARK 999 REMARK 999 NO DATABASE REFERENCE IS CURRENTLY AVAILABLE FOR THE LIGHT REMARK 999 AND HEAVY CHAINS (CHAIN L AND H). DBREF 2FX7 P 671 686 UNP P05880 ENV_HV1W2 662 677 SEQADV 2FX7 LYS P 684 UNP P05880 ILE 675 ENGINEERED SEQADV 2FX7 LYS P 685 UNP P05880 PHE 676 ENGINEERED SEQADV 2FX7 LYS P 686 UNP P05880 ILE 677 ENGINEERED SEQRES 1 L 214 GLU ILE VAL LEU THR GLN SER PRO GLY THR GLN SER LEU SEQRES 2 L 214 SER PRO GLY GLU ARG ALA THR LEU SER CYS ARG ALA SER SEQRES 3 L 214 GLN SER VAL GLY ASN ASN LYS LEU ALA TRP TYR GLN GLN SEQRES 4 L 214 ARG PRO GLY GLN ALA PRO ARG LEU LEU ILE TYR GLY ALA SEQRES 5 L 214 SER SER ARG PRO SER GLY VAL ALA ASP ARG PHE SER GLY SEQRES 6 L 214 SER GLY SER GLY THR ASP PHE THR LEU THR ILE SER ARG SEQRES 7 L 214 LEU GLU PRO GLU ASP PHE ALA VAL TYR TYR CYS GLN GLN SEQRES 8 L 214 TYR GLY GLN SER LEU SER THR PHE GLY GLN GLY THR LYS SEQRES 9 L 214 VAL GLU VAL LYS ARG THR VAL ALA ALA PRO SER VAL PHE SEQRES 10 L 214 ILE PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR SEQRES 11 L 214 ALA SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG SEQRES 12 L 214 GLU ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SEQRES 13 L 214 SER GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER SEQRES 14 L 214 LYS ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SEQRES 15 L 214 SER LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS SEQRES 16 L 214 GLU VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SEQRES 17 L 214 SER PHE ASN ARG GLY GLU SEQRES 1 H 228 GLN VAL GLN LEU VAL GLN SER GLY ALA GLU VAL LYS ARG SEQRES 2 H 228 PRO GLY SER SER VAL THR VAL SER CYS LYS ALA SER GLY SEQRES 3 H 228 GLY SER PHE SER THR TYR ALA LEU SER TRP VAL ARG GLN SEQRES 4 H 228 ALA PRO GLY ARG GLY LEU GLU TRP MET GLY GLY VAL ILE SEQRES 5 H 228 PRO LEU LEU THR ILE THR ASN TYR ALA PRO ARG PHE GLN SEQRES 6 H 228 GLY ARG ILE THR ILE THR ALA ASP ARG SER THR SER THR SEQRES 7 H 228 ALA TYR LEU GLU LEU ASN SER LEU ARG PRO GLU ASP THR SEQRES 8 H 228 ALA VAL TYR TYR CYS ALA ARG GLU GLY THR THR GLY TRP SEQRES 9 H 228 GLY TRP LEU GLY LYS PRO ILE GLY ALA PHE ALA HIS TRP SEQRES 10 H 228 GLY GLN GLY THR LEU VAL THR VAL SER SER ALA SER THR SEQRES 11 H 228 LYS GLY PRO SER VAL PHE PRO LEU ALA PRO SER SER LYS SEQRES 12 H 228 SER THR SER GLY GLY THR ALA ALA LEU GLY CYS LEU VAL SEQRES 13 H 228 LYS ASP TYR PHE PRO GLU PRO VAL THR VAL SER TRP ASN SEQRES 14 H 228 SER GLY ALA LEU THR SER GLY VAL HIS THR PHE PRO ALA SEQRES 15 H 228 VAL LEU GLN SER SER GLY LEU TYR SER LEU SER SER VAL SEQRES 16 H 228 VAL THR VAL PRO SER SER SER LEU GLY THR GLN THR TYR SEQRES 17 H 228 ILE CYS ASN VAL ASN HIS LYS PRO SER ASN THR LYS VAL SEQRES 18 H 228 ASP LYS LYS VAL GLU PRO LYS SEQRES 1 P 16 ASN TRP PHE ASP ILE THR ASN TRP LEU TRP TYR ILE LYS SEQRES 2 P 16 LYS LYS LYS HET GOL 701 6 HETNAM GOL GLYCEROL FORMUL 4 GOL C3 H8 O3 FORMUL 5 HOH *337(H2 O) HELIX 1 1 VAL L 28 ASN L 31 5 4 HELIX 2 2 GLU L 79 PHE L 83 5 5 HELIX 3 3 SER L 121 SER L 127 1 7 HELIX 4 4 LYS L 183 GLU L 187 1 5 HELIX 5 5 PRO H 61 GLN H 64 5 4 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 SER H 196 LEU H 198 5 3 HELIX 9 9 LYS H 213 ASN H 216 5 4 HELIX 10 10 ASN P 671 PHE P 673 5 3 HELIX 11 11 ASP P 674 LYS P 686 1 13 SHEET 1 A 4 LEU L 4 THR L 5 0 SHEET 2 A 4 ALA L 19 ALA 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 LEU L 21 SHEET 4 A 4 PHE L 62 SER L 67 -1 N SER L 63 O THR L 74 SHEET 1 B 5 THR L 10 LEU L 13 0 SHEET 2 B 5 THR L 102 VAL L 106 1 O LYS L 103 N GLN L 11 SHEET 3 B 5 VAL L 85 GLN L 90 -1 N TYR L 86 O THR L 102 SHEET 4 B 5 LEU L 33 GLN L 38 -1 N ALA L 34 O GLN L 89 SHEET 5 B 5 ARG L 45 ILE L 48 -1 O LEU L 47 N TRP L 35 SHEET 1 C 4 THR L 10 LEU L 13 0 SHEET 2 C 4 THR L 102 VAL L 106 1 O LYS L 103 N GLN L 11 SHEET 3 C 4 VAL 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 179 N VAL L 132 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 ALA L 144 VAL L 150 -1 N VAL L 150 O ALA L 153 SHEET 3 E 4 VAL L 191 HIS L 198 -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 GLN H 3 GLN H 6 0 SHEET 2 F 4 VAL H 18 SER H 25 -1 O LYS H 23 N VAL H 5 SHEET 3 F 4 THR H 77 LEU H 82 -1 O ALA H 78 N CYS H 22 SHEET 4 F 4 ILE H 67 ASP H 72 -1 N ASP H 72 O THR H 77 SHEET 1 G 6 GLU H 10 LYS H 12 0 SHEET 2 G 6 THR H 107 VAL H 111 1 O THR H 110 N GLU H 10 SHEET 3 G 6 ALA H 88 THR H 97 -1 N TYR H 90 O THR H 107 SHEET 4 G 6 LEU H 34 GLN H 39 -1 N VAL H 37 O TYR H 91 SHEET 5 G 6 LEU H 45 ILE H 52 -1 O MET H 48 N TRP H 36 SHEET 6 G 6 ILE H 56 TYR H 59 -1 O ASN H 58 N GLY H 50 SHEET 1 H 4 GLU H 10 LYS H 12 0 SHEET 2 H 4 THR H 107 VAL H 111 1 O THR H 110 N GLU H 10 SHEET 3 H 4 ALA H 88 THR H 97 -1 N TYR H 90 O THR H 107 SHEET 4 H 4 PRO H 100F TRP H 103 -1 O HIS H 102 N ARG H 94 SHEET 1 I 4 SER H 120 LEU H 124 0 SHEET 2 I 4 THR H 137 TYR H 147 -1 O LEU H 143 N PHE H 122 SHEET 3 I 4 TYR H 185 PRO H 194 -1 O TYR H 185 N TYR H 147 SHEET 4 I 4 VAL H 171 THR H 173 -1 N HIS H 172 O VAL H 190 SHEET 1 J 4 SER H 120 LEU H 124 0 SHEET 2 J 4 THR H 137 TYR H 147 -1 O LEU H 143 N PHE H 122 SHEET 3 J 4 TYR H 185 PRO H 194 -1 O TYR H 185 N TYR H 147 SHEET 4 J 4 VAL H 177 LEU H 178 -1 N VAL H 177 O SER H 186 SHEET 1 K 3 THR H 153 TRP H 157 0 SHEET 2 K 3 TYR H 206 HIS H 212 -1 O ASN H 209 N SER H 156 SHEET 3 K 3 THR H 217 VAL H 225 -1 O VAL H 219 N VAL H 210 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 CISPEP 1 SER L 7 PRO L 8 0 0.02 CISPEP 2 TYR L 140 PRO L 141 0 0.14 CISPEP 3 PHE H 148 PRO H 149 0 -0.26 CISPEP 4 GLU H 150 PRO H 151 0 0.12 CRYST1 157.940 44.658 85.264 90.00 113.09 90.00 C 1 2 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 0.006332 0.000000 0.002699 0.00000 SCALE2 0.000000 0.022392 0.000000 0.00000 SCALE3 0.000000 0.000000 0.012750 0.00000