HEADER IMMUNE SYSTEM 24-DEC-03 1RZF TITLE CRYSTAL STRUCTURE OF HUMAN ANTI-HIV-1 GP120-REACTIVE TITLE 2 ANTIBODY E51 COMPND MOL_ID: 1; COMPND 2 MOLECULE: FAB E51 LIGHT CHAIN; COMPND 3 CHAIN: L; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: FAB E51 HEAVY CHAIN; COMPND 7 CHAIN: H; COMPND 8 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 EXPRESSION_SYSTEM: HUMAN HERPESVIRUS TYPE 4; SOURCE 5 EXPRESSION_SYSTEM_COMMON: EPSTEIN-BARR VIRUS; SOURCE 6 EXPRESSION_SYSTEM_CELL: IMMORTALIZED B-CELL CLONE FUSED SOURCE 7 WITH A MURINE B-CELL FUSION PARTNER; SOURCE 8 MOL_ID: 2; SOURCE 9 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 10 ORGANISM_COMMON: HUMAN; SOURCE 11 EXPRESSION_SYSTEM: HUMAN HERPESVIRUS TYPE 4; SOURCE 12 EXPRESSION_SYSTEM_COMMON: EPSTEIN-BARR VIRUS; SOURCE 13 EXPRESSION_SYSTEM_CELL: IMMORTALIZED B-CELL CLONE FUSED SOURCE 14 WITH A MURINE B-CELL FUSION PARTNER KEYWDS HIV-1; GP120; CD4I; ANTIBODIES; TYROSINE SULFATION; VH-GENE KEYWDS 2 USAGE EXPDTA X-RAY DIFFRACTION AUTHOR C.C.HUANG,M.VENTURI,S.MAJEED,M.J.MOORE,S.PHOGAT,M.-Y.ZHANG, AUTHOR 2 D.S.DIMITROV,W.A.HENDRICKSON,J.ROBINSON,J.SODROSKI,R.WYATT, AUTHOR 3 H.CHOE,M.FARZAN,P.D.KWONG REVDAT 4 01-FEB-05 1RZF 1 SOURCE REMARK REVDAT 3 16-MAR-04 1RZF 1 JRNL REVDAT 2 09-MAR-04 1RZF 1 JRNL REVDAT 1 03-FEB-04 1RZF 0 JRNL AUTH C.C.HUANG,M.VENTURI,S.MAJEED,M.J.MOORE,S.PHOGAT, JRNL AUTH 2 M.-Y.ZHANG,D.S.DIMITROV,W.A.HENDRICKSON,J.ROBINSON, JRNL AUTH 3 J.SODROSKI,R.WYATT,H.CHOE,M.FARZAN,P.D.KWONG JRNL TITL STRUCTURAL BASIS OF TYROSINE SULFATION AND VH-GENE JRNL TITL 2 USAGE IN ANTIBODIES THAT RECOGNIZE THE HIV TYPE 1 JRNL TITL 3 CORECEPTOR-BINDING SITE ON GP120 JRNL REF PROC.NATL.ACAD.SCI.USA V. 101 2706 2004 JRNL REFN ASTM PNASA6 US ISSN 0027-8424 REMARK 1 REMARK 2 REMARK 2 RESOLUTION. 1.70 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) : 1.70 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000 REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 703888.750 REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000 REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 97.7 REMARK 3 NUMBER OF REFLECTIONS : 50304 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 : 0.232 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.100 REMARK 3 FREE R VALUE TEST SET COUNT : 5064 REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.003 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) : 1.70 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.81 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 93.60 REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 7111 REMARK 3 BIN R VALUE (WORKING SET) : 0.2370 REMARK 3 BIN FREE R VALUE : 0.2810 REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 10.00 REMARK 3 BIN FREE R VALUE TEST SET COUNT : 793 REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.010 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 3217 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 0 REMARK 3 SOLVENT ATOMS : 419 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 18.40 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 25.50 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : -0.59000 REMARK 3 B22 (A**2) : -5.40000 REMARK 3 B33 (A**2) : 5.98000 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) : 0.19 REMARK 3 ESD FROM SIGMAA (A) : 0.13 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) : 0.23 REMARK 3 ESD FROM C-V SIGMAA (A) : 0.16 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. REMARK 3 BOND LENGTHS (A) : 0.005 REMARK 3 BOND ANGLES (DEGREES) : 1.40 REMARK 3 DIHEDRAL ANGLES (DEGREES) : 27.30 REMARK 3 IMPROPER ANGLES (DEGREES) : 0.83 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) : 1.310 ; 1.500 REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.050 ; 2.000 REMARK 3 SIDE-CHAIN BOND (A**2) : 2.060 ; 2.000 REMARK 3 SIDE-CHAIN ANGLE (A**2) : 3.010 ; 2.500 REMARK 3 REMARK 3 BULK SOLVENT MODELING. REMARK 3 METHOD USED : FLAT MODEL REMARK 3 KSOL : 0.42 REMARK 3 BSOL : 59.25 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 : GCL.PAR REMARK 3 PARAMETER FILE 4 : ISO.PAR 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 : GCL.TOP REMARK 3 TOPOLOGY FILE 4 : ISO.TOP REMARK 3 TOPOLOGY FILE 5 : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1RZF 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 RCSB021176. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 04-NOV-2002 REMARK 200 TEMPERATURE (KELVIN) : 100.0 REMARK 200 PH : 7.50 REMARK 200 NUMBER OF CRYSTALS USED : NULL REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : NSLS REMARK 200 BEAMLINE : X4A REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.9793 REMARK 200 MONOCHROMATOR : KOHZU DOUBLE CRYSTAL REMARK 200 MONOCHROMATOR WITH A REMARK 200 SAGITTALLY FOCUSED SECOND REMARK 200 CRYSTAL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4 REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO REMARK 200 DATA SCALING SOFTWARE : SCALEPACK REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 60893 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.600 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 (%) : NULL REMARK 200 DATA REDUNDANCY : NULL REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : 0.06700 REMARK 200 FOR THE DATA SET : NULL REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.66 REMARK 200 COMPLETENESS FOR SHELL (%) : 89.5 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: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: AMORE REMARK 200 STARTING MODEL: 1RZ7 REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 45.20 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.26 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 14% PEG 4000, 7% ISOPROPANOL, 0.07M REMARK 280 HEPES, PH 7.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K 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 32.38500 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 49.64000 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 35.80400 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 49.64000 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 32.38500 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 35.80400 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 2 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 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 GLU H 1 REMARK 465 GLY H 98A REMARK 465 VAL H 98B REMARK 465 ALA H 98C REMARK 465 ALA H 98D REMARK 465 ALA H 98E REMARK 465 GLY H 98F REMARK 465 ASP H 98G REMARK 465 TYR H 98H REMARK 465 ALA H 98I REMARK 465 ASP H 98J REMARK 465 TYR H 98K REMARK 465 ASP H 98L REMARK 465 SER H 127 REMARK 465 SER H 128 REMARK 465 LYS H 129 REMARK 465 SER H 130 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 TYR H 100M CG CD1 CD2 CE1 CE2 CZ OH 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 CYS L 194 C GLN L 195 N -0.041 REMARK 500 CYS L 194 C GLN L 195 N -0.040 REMARK 500 TYR H 91 C CYS H 92 N -0.033 REMARK 500 TYR H 91 C CYS H 92 N -0.041 REMARK 500 CYS H 92 C ALA H 93 N 0.045 REMARK 500 CYS H 92 C ALA H 93 N 0.047 REMARK 500 PRO H 147 CG PRO H 147 CD 0.038 REMARK 500 PRO H 149 CG PRO H 149 CD 0.032 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 GLY L 99 N - CA - C ANGL. DEV. = -9.6 DEGREES REMARK 500 SER L 115 N - CA - C ANGL. DEV. = -8.7 DEGREES REMARK 500 ALA L 151 N - CA - C ANGL. DEV. =-14.5 DEGREES REMARK 500 CYS L 194 CA - CB - SG ANGL. DEV. = 10.1 DEGREES REMARK 500 ALA H 33 N - CA - C ANGL. DEV. = -9.7 DEGREES REMARK 500 ASP H 100P N - CA - C ANGL. DEV. =-12.3 DEGREES REMARK 500 SER H 120 N - CA - C ANGL. DEV. =-10.6 DEGREES REMARK 500 LYS H 143 N - CA - C ANGL. DEV. = 8.9 DEGREES REMARK 500 ASP H 208 N - CA - C ANGL. DEV. = -9.0 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 ASN L 51 -48.54 71.91 REMARK 500 ASP L 152 -111.02 65.02 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1RZ7 RELATED DB: PDB REMARK 900 RELATED ID: 1RZ8 RELATED DB: PDB REMARK 900 RELATED ID: 1RZG RELATED DB: PDB REMARK 900 RELATED ID: 1RZI RELATED DB: PDB REMARK 900 RELATED ID: 1RZJ RELATED DB: PDB REMARK 900 RELATED ID: 1RZK RELATED DB: PDB SEQRES 1 L 213 GLN SER ILE LEU THR GLN PRO PRO SER VAL SER ALA ALA SEQRES 2 L 213 PRO GLY GLN LYS VAL THR ILE SER CYS SER GLY SER SER SEQRES 3 L 213 SER ASN ILE GLY ASN ASN ASP VAL SER TRP TYR GLN GLN SEQRES 4 L 213 PHE PRO GLY THR VAL PRO LYS LEU VAL ILE TYR GLU ASN SEQRES 5 L 213 ASN GLU ARG PRO SER GLY ILE PRO ASP ARG PHE SER GLY SEQRES 6 L 213 SER LYS SER GLY THR SER ALA THR LEU GLY ILE THR GLY SEQRES 7 L 213 LEU GLN THR GLY ASP GLU ALA ASP TYR TYR CYS GLY THR SEQRES 8 L 213 TRP ASP SER SER LEU SER ALA VAL VAL PHE GLY GLY GLY SEQRES 9 L 213 SER LYS VAL THR VAL LEU GLY GLN PRO LYS ALA ALA PRO SEQRES 10 L 213 SER VAL THR LEU PHE PRO PRO SER SER GLU GLU LEU GLN SEQRES 11 L 213 ALA ASN LYS ALA THR LEU VAL CYS LEU ILE SER ASP PHE SEQRES 12 L 213 TYR PRO GLY ALA VAL THR VAL ALA TRP LYS ALA ASP SER SEQRES 13 L 213 SER PRO VAL LYS ALA GLY VAL GLU THR THR THR PRO SER SEQRES 14 L 213 LYS GLN SER ASN ASN LYS TYR ALA ALA SER SER TYR LEU SEQRES 15 L 213 SER LEU THR PRO GLU GLN TRP LYS SER HIS ARG SER TYR SEQRES 16 L 213 SER CYS GLN VAL THR HIS GLU GLY SER THR VAL GLU LYS SEQRES 17 L 213 THR VAL ALA PRO THR SEQRES 1 H 235 GLU VAL GLN LEU VAL GLN SER GLY ALA GLU VAL ASN LYS SEQRES 2 H 235 PRO GLY SER SER VAL LYS VAL SER CYS GLN ALA SER GLY SEQRES 3 H 235 ALA THR LEU ASN SER HIS ALA PHE SER TRP VAL ARG GLN SEQRES 4 H 235 ALA PRO GLY GLN GLY LEU GLU TRP MET ALA GLY ILE ILE SEQRES 5 H 235 PRO ILE PHE GLY SER SER HIS TYR ALA GLN LYS PHE ARG SEQRES 6 H 235 GLY ARG VAL THR ILE SER ALA ASP GLU SER THR ARG THR SEQRES 7 H 235 VAL TYR LEU HIS LEU ARG GLY LEU ARG SER ASP ASP THR SEQRES 8 H 235 ALA VAL TYR TYR CYS ALA SER ASN SER ILE ALA GLY VAL SEQRES 9 H 235 ALA ALA ALA GLY ASP TYR ALA ASP TYR ASP GLY GLY TYR SEQRES 10 H 235 TYR TYR ASP MET ASP VAL TRP GLY GLN GLY THR THR VAL SEQRES 11 H 235 THR VAL SER SER ALA SER THR LYS GLY PRO SER VAL PHE SEQRES 12 H 235 PRO LEU ALA PRO SER SER LYS SER THR SER GLY GLY THR SEQRES 13 H 235 ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU SEQRES 14 H 235 PRO VAL THR VAL SER TRP ASN SER GLY ALA LEU THR SER SEQRES 15 H 235 GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SER SER GLY SEQRES 16 H 235 LEU TYR SER LEU SER SER VAL VAL THR VAL PRO SER SER SEQRES 17 H 235 SER LEU GLY THR GLN THR TYR ILE CYS ASN VAL ASN HIS SEQRES 18 H 235 LYS PRO SER ASN THR LYS VAL ASP LYS ARG VAL GLU PRO SEQRES 19 H 235 LYS HET GOL 9001 6 HET GOL 9002 6 HET GOL 9003 6 HET GOL 9004 6 HET GOL 9005 6 HET GOL 9006 6 HET GOL 9007 6 HET GOL 9008 6 HET GOL 9009 6 HET GOL 9010 6 HET GOL 9011 6 HET GOL 9012 6 HET GOL 9013 6 HET IPA 7001 4 HET IPA 7002 4 HETNAM GOL GLYCEROL HETNAM IPA ISOPROPYL ALCOHOL FORMUL 3 GOL 13(C3 H8 O3) FORMUL 16 IPA 2(C3 H8 O) FORMUL 18 HOH *333(H2 O) HELIX 1 1 GLN L 79 GLU L 83 5 5 HELIX 2 2 SER L 122 ALA L 128 1 7 HELIX 3 3 THR L 182 HIS L 189 1 8 HELIX 4 4 PRO H 52A GLY H 55 5 4 HELIX 5 5 GLN H 61 ARG H 64 5 4 HELIX 6 6 ARG H 83 THR H 87 5 5 HELIX 7 7 SER H 156 ALA H 158 5 3 HELIX 8 8 SER H 187 THR H 191 5 5 HELIX 9 9 LYS H 201 ASN H 204 5 4 SHEET 1 A 5 SER L 10 ALA L 13 0 SHEET 2 A 5 SER L 102 VAL L 106 1 O LYS L 103 N VAL L 11 SHEET 3 A 5 ASP L 85 ASP L 92 -1 N TYR L 86 O SER L 102 SHEET 4 A 5 VAL L 33 GLN L 38 -1 N TYR L 36 O TYR L 87 SHEET 5 A 5 LYS L 45 ILE L 48 -1 O LYS L 45 N GLN L 37 SHEET 1 B 4 SER L 10 ALA L 13 0 SHEET 2 B 4 SER L 102 VAL L 106 1 O LYS L 103 N VAL L 11 SHEET 3 B 4 ASP L 85 ASP L 92 -1 N TYR L 86 O SER L 102 SHEET 4 B 4 ALA L 95B PHE L 98 -1 O VAL L 97 N THR L 90 SHEET 1 C 3 VAL L 19 SER L 24 0 SHEET 2 C 3 SER L 70 ILE L 75 -1 O ALA L 71 N CYS L 23 SHEET 3 C 3 PHE L 62 SER L 67 -1 N SER L 63 O GLY L 74 SHEET 1 D 4 SER L 115 PHE L 119 0 SHEET 2 D 4 ALA L 131 PHE L 140 -1 O LEU L 136 N THR L 117 SHEET 3 D 4 TYR L 173 LEU L 181 -1 O SER L 177 N CYS L 135 SHEET 4 D 4 VAL L 160 THR L 162 -1 N GLU L 161 O TYR L 178 SHEET 1 E 4 SER L 115 PHE L 119 0 SHEET 2 E 4 ALA L 131 PHE L 140 -1 O LEU L 136 N THR L 117 SHEET 3 E 4 TYR L 173 LEU L 181 -1 O SER L 177 N CYS L 135 SHEET 4 E 4 SER L 166 LYS L 167 -1 N SER L 166 O ALA L 174 SHEET 1 F 4 SER L 154 PRO L 155 0 SHEET 2 F 4 THR L 146 ALA L 151 -1 N ALA L 151 O SER L 154 SHEET 3 F 4 TYR L 192 HIS L 198 -1 O GLN L 195 N ALA L 148 SHEET 4 F 4 SER L 201 VAL L 207 -1 O SER L 201 N HIS L 198 SHEET 1 G 4 LEU H 4 GLN H 6 0 SHEET 2 G 4 VAL H 18 ALA H 24 -1 O GLN H 23 N VAL H 5 SHEET 3 G 4 THR H 77 LEU H 82 -1 O VAL H 78 N CYS H 22 SHEET 4 G 4 VAL H 67 ASP H 72 -1 N ASP H 72 O THR H 77 SHEET 1 H 6 GLU H 10 ASN H 12 0 SHEET 2 H 6 THR H 107 VAL H 111 1 O THR H 110 N ASN H 12 SHEET 3 H 6 ALA H 88 SER H 96 -1 N TYR H 90 O THR H 107 SHEET 4 H 6 HIS H 32 GLN H 39 -1 N VAL H 37 O TYR H 91 SHEET 5 H 6 LEU H 45 ILE H 52 -1 O ILE H 51 N PHE H 34 SHEET 6 H 6 SER H 56 TYR H 59 -1 O SER H 56 N ILE H 52 SHEET 1 I 4 GLU H 10 ASN H 12 0 SHEET 2 I 4 THR H 107 VAL H 111 1 O THR H 110 N ASN H 12 SHEET 3 I 4 ALA H 88 SER H 96 -1 N TYR H 90 O THR H 107 SHEET 4 I 4 VAL H 102 TRP H 103 -1 O VAL H 102 N SER H 94 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 182 N LEU H 138 SHEET 4 J 4 VAL H 163 THR H 165 -1 N HIS H 164 O VAL H 181 SHEET 1 K 4 SER H 120 LEU H 124 0 SHEET 2 K 4 THR H 135 TYR H 145 -1 O LEU H 141 N PHE H 122 SHEET 3 K 4 TYR H 176 PRO H 185 -1 O VAL H 182 N LEU H 138 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 ARG H 210 -1 O VAL H 207 N VAL H 198 SSBOND 1 CYS L 23 CYS L 88 SSBOND 2 CYS L 135 CYS L 194 SSBOND 3 CYS H 22 CYS H 92 SSBOND 4 CYS H 140 CYS H 196 CISPEP 1 TYR L 141 PRO L 142 0 0.13 CISPEP 2 PHE H 146 PRO H 147 0 -0.24 CISPEP 3 GLU H 148 PRO H 149 0 0.28 CRYST1 64.770 71.608 99.280 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 0.015439 0.000000 0.000000 0.00000 SCALE2 0.000000 0.013965 0.000000 0.00000 SCALE3 0.000000 0.000000 0.010073 0.00000