HEADER IMMUNE SYSTEM 09-JAN-25 9MS9 TITLE STRUCTURE OF HCV NEUTRALIZING ANTIBODY RM5-16 COMPND MOL_ID: 1; COMPND 2 MOLECULE: RM5-16 FAB LIGHT CHAIN; COMPND 3 CHAIN: L; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: RM5-16 FAB HEAVY CHAIN; COMPND 7 CHAIN: H; COMPND 8 ENGINEERED: YES; COMPND 9 OTHER_DETAILS: Q1(PCA) SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: MACACA MULATTA; SOURCE 3 ORGANISM_COMMON: RHESUS MONKEY; SOURCE 4 ORGANISM_TAXID: 9544; SOURCE 5 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 6 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 8 MOL_ID: 2; SOURCE 9 ORGANISM_SCIENTIFIC: MACACA MULATTA; SOURCE 10 ORGANISM_COMMON: RHESUS MONKEY; SOURCE 11 ORGANISM_TAXID: 9544; SOURCE 12 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 13 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 14 EXPRESSION_SYSTEM_TAXID: 9606 KEYWDS MONKEY ANTIBODY, IMMUNE SYSTEM EXPDTA X-RAY DIFFRACTION AUTHOR T.K.Y.NGUYEN,I.A.WILSON REVDAT 1 14-JAN-26 9MS9 0 JRNL AUTH T.K.Y.NGUYEN,I.A.WILSON JRNL TITL STRUCTURE OF HCV NEUTRALIZING ANTIBODY RM5-16 JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 1.46 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX 1.21RC1_5127 REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE, REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER, REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY, REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON, REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI, REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART REMARK 3 REMARK 3 REFINEMENT TARGET : GEOSTD + MONOMER LIBRARY + CDL V1.2 REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.46 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 42.64 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.360 REMARK 3 COMPLETENESS FOR RANGE (%) : 99.1 REMARK 3 NUMBER OF REFLECTIONS : 84877 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.145 REMARK 3 R VALUE (WORKING SET) : 0.143 REMARK 3 FREE R VALUE : 0.175 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.040 REMARK 3 FREE R VALUE TEST SET COUNT : 4275 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS). REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE REMARK 3 1 42.6400 - 4.5400 0.98 2912 158 0.1820 0.1912 REMARK 3 2 4.5400 - 3.6000 0.99 2793 146 0.1422 0.1411 REMARK 3 3 3.6000 - 3.1500 1.00 2771 153 0.1567 0.1885 REMARK 3 4 3.1500 - 2.8600 0.99 2730 148 0.1532 0.1752 REMARK 3 5 2.8600 - 2.6500 1.00 2752 136 0.1518 0.2001 REMARK 3 6 2.6500 - 2.5000 0.99 2704 154 0.1436 0.1936 REMARK 3 7 2.5000 - 2.3700 0.97 2647 133 0.1341 0.1629 REMARK 3 8 2.3700 - 2.2700 0.99 2670 157 0.1248 0.1679 REMARK 3 9 2.2700 - 2.1800 1.00 2733 147 0.1253 0.1294 REMARK 3 10 2.1800 - 2.1100 1.00 2699 148 0.1201 0.1452 REMARK 3 11 2.1100 - 2.0400 0.99 2693 135 0.1203 0.1673 REMARK 3 12 2.0400 - 1.9800 1.00 2676 158 0.1269 0.1889 REMARK 3 13 1.9800 - 1.9300 0.99 2678 156 0.1210 0.1742 REMARK 3 14 1.9300 - 1.8800 1.00 2658 144 0.1185 0.1542 REMARK 3 15 1.8800 - 1.8400 1.00 2713 146 0.1136 0.1434 REMARK 3 16 1.8400 - 1.8000 0.99 2672 127 0.1162 0.1582 REMARK 3 17 1.8000 - 1.7600 0.97 2629 125 0.1221 0.1547 REMARK 3 18 1.7600 - 1.7300 0.99 2641 145 0.1240 0.1784 REMARK 3 19 1.7300 - 1.7000 1.00 2689 162 0.1276 0.1822 REMARK 3 20 1.7000 - 1.6700 0.99 2628 152 0.1365 0.1652 REMARK 3 21 1.6700 - 1.6400 0.99 2653 139 0.1349 0.1609 REMARK 3 22 1.6400 - 1.6200 0.99 2700 133 0.1439 0.1848 REMARK 3 23 1.6200 - 1.6000 0.99 2623 141 0.1453 0.2081 REMARK 3 24 1.6000 - 1.5700 0.99 2691 159 0.1408 0.2104 REMARK 3 25 1.5700 - 1.5500 0.99 2625 141 0.1551 0.1995 REMARK 3 26 1.5500 - 1.5300 0.99 2659 122 0.1537 0.2306 REMARK 3 27 1.5300 - 1.5100 0.99 2685 129 0.1623 0.1979 REMARK 3 28 1.5100 - 1.4900 0.99 2616 135 0.1696 0.2293 REMARK 3 29 1.4900 - 1.4800 0.99 2692 119 0.1739 0.2573 REMARK 3 30 1.4800 - 1.4600 0.96 2570 127 0.1990 0.2730 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL REMARK 3 SOLVENT RADIUS : 1.10 REMARK 3 SHRINKAGE RADIUS : 0.90 REMARK 3 K_SOL : NULL REMARK 3 B_SOL : NULL REMARK 3 REMARK 3 ERROR ESTIMATES. REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.142 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 15.078 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 13.51 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 18.32 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : NULL REMARK 3 B22 (A**2) : NULL REMARK 3 B33 (A**2) : NULL REMARK 3 B12 (A**2) : NULL REMARK 3 B13 (A**2) : NULL REMARK 3 B23 (A**2) : NULL REMARK 3 REMARK 3 TWINNING INFORMATION. REMARK 3 FRACTION: NULL REMARK 3 OPERATOR: NULL REMARK 3 REMARK 3 DEVIATIONS FROM IDEAL VALUES. REMARK 3 RMSD COUNT REMARK 3 BOND : 0.008 3396 REMARK 3 ANGLE : 1.032 4660 REMARK 3 CHIRALITY : 0.087 531 REMARK 3 PLANARITY : 0.009 592 REMARK 3 DIHEDRAL : 11.642 1215 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : NULL REMARK 3 REMARK 3 NCS DETAILS REMARK 3 NUMBER OF NCS GROUPS : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 9MS9 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 10-JAN-25. REMARK 100 THE DEPOSITION ID IS D_1000291427. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 04-NOV-22 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : NULL REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : SSRL REMARK 200 BEAMLINE : BL12-2 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.979 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000 REMARK 200 DATA SCALING SOFTWARE : HKL-2000 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 85214 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.460 REMARK 200 RESOLUTION RANGE LOW (A) : 42.640 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.4 REMARK 200 DATA REDUNDANCY : 13.10 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 24.1300 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.46 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.51 REMARK 200 COMPLETENESS FOR SHELL (%) : NULL 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: PHENIX REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 52.73 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.60 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M SODIUM ACETATE, PH 4.5, 0.2 M REMARK 280 LITHIUM SULFATE, 28% W/V PEG8000, VAPOR DIFFUSION, SITTING DROP, REMARK 280 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 -X+1/2,-Y,Z+1/2 REMARK 290 3555 -X,Y+1/2,-Z+1/2 REMARK 290 4555 X+1/2,-Y+1/2,-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 21.53600 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 80.53400 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 35.08400 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 80.53400 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 21.53600 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 35.08400 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 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 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 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 3960 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 19340 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -68.0 KCAL/MOL 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 GLN L 1 REMARK 465 SER L 2 REMARK 465 THR L 210 REMARK 465 GLU L 211 REMARK 465 CYS L 212 REMARK 465 SER L 213 REMARK 465 SER H 215 REMARK 465 CYS H 216 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 PROTEIN: ENGH AND HUBER, 1999 REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996 REMARK 500 REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3 REMARK 500 CYS H 140 CA - CB - SG ANGL. DEV. = 12.5 DEGREES REMARK 500 REMARK 500 REMARK: NULL 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 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 ASN L 27B -98.38 -124.97 REMARK 500 ASP L 51 -45.79 73.44 REMARK 500 ASN L 52 13.35 -144.91 REMARK 500 ASP L 68 -118.79 56.50 REMARK 500 SER L 90 -159.09 -150.17 REMARK 500 ASP L 152 -117.81 54.70 REMARK 500 SER H 15 -8.66 86.65 REMARK 500 REMARK 500 REMARK: NULL DBREF 9MS9 L 1 213 PDB 9MS9 9MS9 1 213 DBREF 9MS9 H 1 216 PDB 9MS9 9MS9 1 216 SEQRES 1 L 216 GLN SER VAL LEU THR GLN PRO PRO SER VAL SER GLY ALA SEQRES 2 L 216 PRO GLY GLN ARG VAL THR ILE SER CYS THR GLY HIS SER SEQRES 3 L 216 SER ASN ILE GLY GLY TYR PHE VAL SER TRP TYR GLN GLN SEQRES 4 L 216 LEU PRO GLY THR THR PRO LYS LEU LEU ILE TYR GLN ASP SEQRES 5 L 216 ASN LYS ARG PRO SER GLY VAL SER ASP ARG PHE SER GLY SEQRES 6 L 216 SER LYS SER ASP THR THR ALA SER LEU THR ILE THR GLY SEQRES 7 L 216 LEU GLN THR GLU ASP GLU ALA ASP TYR TYR CYS LEU SER SEQRES 8 L 216 TYR ASP ASN SER LEU SER ALA GLN VAL PHE GLY GLY GLY SEQRES 9 L 216 THR ARG LEU THR VAL LEU GLY GLN PRO LYS ALA ALA PRO SEQRES 10 L 216 SER VAL THR LEU PHE PRO PRO SER SER GLU GLU LEU GLN SEQRES 11 L 216 ALA ASN LYS ALA THR LEU VAL CYS LEU ILE SER ASP PHE SEQRES 12 L 216 TYR PRO GLY ALA VAL THR VAL ALA TRP LYS ALA ASP SER SEQRES 13 L 216 SER PRO VAL LYS ALA GLY VAL GLU THR THR THR PRO SER SEQRES 14 L 216 LYS GLN SER ASN ASN LYS TYR ALA ALA SER SER TYR LEU SEQRES 15 L 216 SER LEU THR PRO GLU GLN TRP LYS SER HIS ARG SER TYR SEQRES 16 L 216 SER CYS GLN VAL THR HIS GLU GLY SER THR VAL GLU LYS SEQRES 17 L 216 THR VAL ALA PRO THR GLU CYS SER SEQRES 1 H 224 PCA LEU GLN LEU GLN GLU SER GLY PRO GLY LEU MET LYS SEQRES 2 H 224 PRO SER GLU THR LEU SER LEU THR CYS ALA VAL SER GLY SEQRES 3 H 224 GLY SER ILE SER SER HIS TYR TRP SER TRP ILE ARG GLN SEQRES 4 H 224 SER PRO GLY LYS GLY LEU GLU TRP ILE GLY TYR ILE TYR SEQRES 5 H 224 GLY GLY THR GLY ARG THR ASN TYR ASN PRO SER LEU LYS SEQRES 6 H 224 SER ARG VAL THR ILE SER THR ASP THR SER LYS ASN GLN SEQRES 7 H 224 PHE SER LEU ASN LEU SER SER VAL THR ALA ALA ASP THR SEQRES 8 H 224 ALA MET TYR TYR CYS ALA ARG TYR PRO GLY SER HIS TRP SEQRES 9 H 224 GLU ASN SER LEU ASP VAL TRP GLY ARG GLY VAL LEU VAL SEQRES 10 H 224 THR VAL SER SER ALA SER THR LYS GLY PRO SER VAL PHE SEQRES 11 H 224 PRO LEU ALA PRO SER SER LYS SER THR SER GLY GLY THR SEQRES 12 H 224 ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU SEQRES 13 H 224 PRO VAL THR VAL SER TRP ASN SER GLY ALA LEU THR SER SEQRES 14 H 224 GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SER SER GLY SEQRES 15 H 224 LEU TYR SER LEU SER SER VAL VAL THR VAL PRO SER SER SEQRES 16 H 224 SER LEU GLY THR GLN THR TYR ILE CYS ASN VAL ASN HIS SEQRES 17 H 224 LYS PRO SER ASN THR LYS VAL ASP LYS LYS VAL GLU PRO SEQRES 18 H 224 LYS SER CYS HET PCA H 1 14 HET SO4 L 301 5 HET SO4 L 302 5 HET SO4 L 303 5 HET SO4 H 301 5 HETNAM PCA PYROGLUTAMIC ACID HETNAM SO4 SULFATE ION FORMUL 2 PCA C5 H7 N O3 FORMUL 3 SO4 4(O4 S 2-) FORMUL 7 HOH *434(H2 O) HELIX 1 AA1 GLN L 79 GLU L 83 5 5 HELIX 2 AA2 SER L 122 ALA L 128 1 7 HELIX 3 AA3 THR L 182 HIS L 189 1 8 HELIX 4 AA4 LEU H 63 SER H 65 5 3 HELIX 5 AA5 THR H 83 THR H 87 5 5 HELIX 6 AA6 SER H 98 ASN H 100B 5 5 HELIX 7 AA7 SER H 156 ALA H 158 5 3 HELIX 8 AA8 SER H 187 LEU H 189 5 3 HELIX 9 AA9 LYS H 201 ASN H 204 5 4 SHEET 1 AA1 5 SER L 9 GLY L 13 0 SHEET 2 AA1 5 THR L 102 VAL L 106 1 O THR L 105 N VAL L 11 SHEET 3 AA1 5 ASP L 85 ASP L 92 -1 N TYR L 86 O THR L 102 SHEET 4 AA1 5 SER L 34 GLN L 38 -1 N GLN L 38 O ASP L 85 SHEET 5 AA1 5 LYS L 45 ILE L 48 -1 O LEU L 47 N TRP L 35 SHEET 1 AA2 4 SER L 9 GLY L 13 0 SHEET 2 AA2 4 THR L 102 VAL L 106 1 O THR L 105 N VAL L 11 SHEET 3 AA2 4 ASP L 85 ASP L 92 -1 N TYR L 86 O THR L 102 SHEET 4 AA2 4 ALA L 95B PHE L 98 -1 O VAL L 97 N SER L 90 SHEET 1 AA3 3 VAL L 19 THR L 24 0 SHEET 2 AA3 3 THR L 70 ILE L 75 -1 O ALA L 71 N CYS L 23 SHEET 3 AA3 3 PHE L 62 SER L 67 -1 N SER L 65 O SER L 72 SHEET 1 AA4 4 SER L 115 PHE L 119 0 SHEET 2 AA4 4 ALA L 131 PHE L 140 -1 O LEU L 136 N THR L 117 SHEET 3 AA4 4 TYR L 173 LEU L 181 -1 O SER L 177 N CYS L 135 SHEET 4 AA4 4 VAL L 160 THR L 162 -1 N GLU L 161 O TYR L 178 SHEET 1 AA5 4 SER L 115 PHE L 119 0 SHEET 2 AA5 4 ALA L 131 PHE L 140 -1 O LEU L 136 N THR L 117 SHEET 3 AA5 4 TYR L 173 LEU L 181 -1 O SER L 177 N CYS L 135 SHEET 4 AA5 4 SER L 166 LYS L 167 -1 N SER L 166 O ALA L 174 SHEET 1 AA6 4 SER L 154 VAL L 156 0 SHEET 2 AA6 4 THR L 146 ALA L 151 -1 N ALA L 151 O SER L 154 SHEET 3 AA6 4 TYR L 192 HIS L 198 -1 O GLN L 195 N ALA L 148 SHEET 4 AA6 4 SER L 201 VAL L 207 -1 O VAL L 203 N VAL L 196 SHEET 1 AA7 4 GLN H 3 SER H 7 0 SHEET 2 AA7 4 LEU H 18 SER H 25 -1 O SER H 25 N GLN H 3 SHEET 3 AA7 4 GLN H 77 LEU H 82 -1 O PHE H 78 N CYS H 22 SHEET 4 AA7 4 VAL H 67 ASP H 72 -1 N THR H 68 O ASN H 81 SHEET 1 AA8 6 LEU H 11 MET H 12 0 SHEET 2 AA8 6 VAL H 107 VAL H 111 1 O THR H 110 N MET H 12 SHEET 3 AA8 6 ALA H 88 ARG H 94 -1 N TYR H 90 O VAL H 107 SHEET 4 AA8 6 TYR H 33 SER H 40 -1 N ILE H 37 O TYR H 91 SHEET 5 AA8 6 GLY H 44 TYR H 52 -1 O GLU H 46 N ARG H 38 SHEET 6 AA8 6 THR H 57 TYR H 59 -1 O ASN H 58 N TYR H 50 SHEET 1 AA9 4 LEU H 11 MET H 12 0 SHEET 2 AA9 4 VAL H 107 VAL H 111 1 O THR H 110 N MET H 12 SHEET 3 AA9 4 ALA H 88 ARG H 94 -1 N TYR H 90 O VAL H 107 SHEET 4 AA9 4 VAL H 102 TRP H 103 -1 O VAL H 102 N ARG H 94 SHEET 1 AB1 4 SER H 120 LEU H 124 0 SHEET 2 AB1 4 THR H 135 TYR H 145 -1 O GLY H 139 N LEU H 124 SHEET 3 AB1 4 TYR H 176 PRO H 185 -1 O LEU H 178 N VAL H 142 SHEET 4 AB1 4 VAL H 163 THR H 165 -1 N HIS H 164 O VAL H 181 SHEET 1 AB2 4 SER H 120 LEU H 124 0 SHEET 2 AB2 4 THR H 135 TYR H 145 -1 O GLY H 139 N LEU H 124 SHEET 3 AB2 4 TYR H 176 PRO H 185 -1 O LEU H 178 N VAL H 142 SHEET 4 AB2 4 VAL H 169 LEU H 170 -1 N VAL H 169 O SER H 177 SHEET 1 AB3 3 THR H 151 TRP H 154 0 SHEET 2 AB3 3 ILE H 195 HIS H 200 -1 O ASN H 197 N SER H 153 SHEET 3 AB3 3 THR H 205 LYS H 210 -1 O VAL H 207 N VAL H 198 SSBOND 1 CYS L 23 CYS L 88 1555 1555 2.08 SSBOND 2 CYS L 135 CYS L 194 1555 1555 2.06 SSBOND 3 CYS H 22 CYS H 92 1555 1555 2.17 SSBOND 4 CYS H 140 CYS H 196 1555 1555 2.03 LINK C PCA H 1 N LEU H 2 1555 1555 1.33 CISPEP 1 TYR L 141 PRO L 142 0 -0.05 CISPEP 2 PHE H 146 PRO H 147 0 -7.95 CISPEP 3 GLU H 148 PRO H 149 0 2.22 CRYST1 43.072 70.168 161.068 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 0.023217 0.000000 0.000000 0.00000 SCALE2 0.000000 0.014252 0.000000 0.00000 SCALE3 0.000000 0.000000 0.006209 0.00000