HEADER VIRAL PROTEIN/IMMUNE SYSTEM 01-FEB-24 8VWE TITLE HIV-1 NEUTRALIZING ANTIBODY D5_AR BOUND TO HIV-1 GP41 COILED-COIL TITLE 2 POCKET IQN17 COMPND MOL_ID: 1; COMPND 2 MOLECULE: NEUTRALIZING ANTIBODY D5_AR HEAVY CHAIN; COMPND 3 CHAIN: H; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: TRANSMEMBRANE PROTEIN GP41 IQN17 PEPTIDE; COMPND 7 CHAIN: C; COMPND 8 ENGINEERED: YES; COMPND 9 MOL_ID: 3; COMPND 10 MOLECULE: NEUTRALIZING ANTIBODY D5_AR LIGHT CHAIN; COMPND 11 CHAIN: L; COMPND 12 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606; SOURCE 5 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 6 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 8 EXPRESSION_SYSTEM_CELL_LINE: EXPI293F; SOURCE 9 MOL_ID: 2; SOURCE 10 SYNTHETIC: YES; SOURCE 11 ORGANISM_SCIENTIFIC: HIV-1 M:B_HXB2R; SOURCE 12 ORGANISM_TAXID: 11706; SOURCE 13 MOL_ID: 3; SOURCE 14 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 15 ORGANISM_COMMON: HUMAN; SOURCE 16 ORGANISM_TAXID: 9606; SOURCE 17 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 18 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 19 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 20 EXPRESSION_SYSTEM_CELL_LINE: EXPI293F KEYWDS HIV-1 FUSION INHIBITOR, GP41, HIV-1 NEUTRALIZING ANTIBODY, PREHAIRPIN KEYWDS 2 INTERMEDIATE, VIRAL PROTEIN, VIRAL PROTEIN-IMMUNE SYSTEM COMPLEX EXPDTA X-RAY DIFFRACTION AUTHOR M.V.FILSINGER INTERRANTE,S.TANG,D.FERNANDEZ,P.S.KIM REVDAT 1 02-JUL-25 8VWE 0 JRNL AUTH M.V.FILSINGER INTERRANTE,S.TANG,S.KIM,V.R.SHANKER,B.L.HIE, JRNL AUTH 2 T.U.J.BRUUN,W.WU,J.E.PAK,D.FERNANDEZ,P.S.KIM JRNL TITL UTILIZING MACHINE LEARNING TO IMPROVE NEUTRALIZATION POTENCY JRNL TITL 2 OF AN HIV-1 ANTIBODY TARGETING THE GP41 N-HEPTAD REPEAT. JRNL REF ACS CHEM.BIOL. 2025 JRNL REFN ESSN 1554-8937 JRNL PMID 40540236 JRNL DOI 10.1021/ACSCHEMBIO.5C00035 REMARK 2 REMARK 2 RESOLUTION. 2.20 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX 1.20.1_4487 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) : 2.20 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 41.48 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 177.98 REMARK 3 COMPLETENESS FOR RANGE (%) : 92.0 REMARK 3 NUMBER OF REFLECTIONS : 30323 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.215 REMARK 3 R VALUE (WORKING SET) : 0.205 REMARK 3 FREE R VALUE : 0.257 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 6.760 REMARK 3 FREE R VALUE TEST SET COUNT : 2050 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 41.4800 - 5.3000 0.93 2189 159 0.1680 0.2391 REMARK 3 2 5.2900 - 4.2100 0.93 2199 156 0.1530 0.1833 REMARK 3 3 4.2100 - 3.6700 0.93 2181 156 0.1926 0.2384 REMARK 3 4 3.6700 - 3.3400 0.93 2205 155 0.2283 0.2692 REMARK 3 5 3.3400 - 3.1000 0.93 2195 147 0.2377 0.2884 REMARK 3 6 3.1000 - 2.9200 0.93 2174 153 0.2601 0.2848 REMARK 3 7 2.9200 - 2.7700 0.93 2197 154 0.2719 0.3477 REMARK 3 8 2.7700 - 2.6500 0.93 2190 156 0.3109 0.3153 REMARK 3 9 2.6500 - 2.5500 0.92 2157 153 0.2709 0.3173 REMARK 3 10 2.5500 - 2.4600 0.90 2131 152 0.2971 0.3086 REMARK 3 11 2.4600 - 2.3800 0.90 2085 146 0.3022 0.3172 REMARK 3 12 2.3800 - 2.3200 0.84 1989 143 0.3330 0.3431 REMARK 3 13 2.3100 - 2.2500 0.60 1425 101 0.4236 0.4443 REMARK 3 14 2.2500 - 2.2000 0.42 1003 72 0.6339 0.6725 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) : NULL REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 34.000 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 75.08 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 : 0.004 3405 REMARK 3 ANGLE : 0.865 4660 REMARK 3 CHIRALITY : 0.054 544 REMARK 3 PLANARITY : 0.006 605 REMARK 3 DIHEDRAL : 10.049 1149 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 8VWE COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-FEB-24. REMARK 100 THE DEPOSITION ID IS D_1000281245. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 14-NOV-20 REMARK 200 TEMPERATURE (KELVIN) : 80 REMARK 200 PH : 8.5 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : SSRL REMARK 200 BEAMLINE : BL9-2 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-3000 REMARK 200 DATA SCALING SOFTWARE : HKL-3000 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 32536 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.200 REMARK 200 RESOLUTION RANGE LOW (A) : 41.480 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 92.1 REMARK 200 DATA REDUNDANCY : 19.70 REMARK 200 R MERGE (I) : 0.06700 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 29.2000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.41 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.45 REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0 REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : 1.61900 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 2.200 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: PHENIX 1.20.1_4487 REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 61.73 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.21 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 10% PEG 2000 MME 100MM TMAO 100MM TRIS REMARK 280 PH 8.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: H 3 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -Y,X-Y,Z REMARK 290 3555 -X+Y,-X,Z REMARK 290 4555 X+2/3,Y+1/3,Z+1/3 REMARK 290 5555 -Y+2/3,X-Y+1/3,Z+1/3 REMARK 290 6555 -X+Y+2/3,-X+1/3,Z+1/3 REMARK 290 7555 X+1/3,Y+2/3,Z+2/3 REMARK 290 8555 -Y+1/3,X-Y+2/3,Z+2/3 REMARK 290 9555 -X+Y+1/3,-X+2/3,Z+2/3 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 -0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 79.98300 REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 46.17821 REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 22.65633 REMARK 290 SMTRY1 5 -0.500000 -0.866025 0.000000 79.98300 REMARK 290 SMTRY2 5 0.866025 -0.500000 0.000000 46.17821 REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 22.65633 REMARK 290 SMTRY1 6 -0.500000 0.866025 0.000000 79.98300 REMARK 290 SMTRY2 6 -0.866025 -0.500000 0.000000 46.17821 REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 22.65633 REMARK 290 SMTRY1 7 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 92.35641 REMARK 290 SMTRY3 7 0.000000 0.000000 1.000000 45.31267 REMARK 290 SMTRY1 8 -0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 8 0.866025 -0.500000 0.000000 92.35641 REMARK 290 SMTRY3 8 0.000000 0.000000 1.000000 45.31267 REMARK 290 SMTRY1 9 -0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 9 -0.866025 -0.500000 0.000000 92.35641 REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 45.31267 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: NONAMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: NONAMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 21120 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 58760 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -185.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: H, C, L 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 350 BIOMT1 2 -0.500000 -0.866025 0.000000 0.00000 REMARK 350 BIOMT2 2 0.866025 -0.500000 0.000000 0.00000 REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000 REMARK 350 BIOMT1 3 -0.500000 0.866025 0.000000 0.00000 REMARK 350 BIOMT2 3 -0.866025 -0.500000 0.000000 0.00000 REMARK 350 BIOMT3 3 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 H 1 REMARK 465 VAL H 2 REMARK 465 SER H 130 REMARK 465 SER H 131 REMARK 465 LYS H 132 REMARK 465 SER H 133 REMARK 465 THR H 134 REMARK 465 SER H 135 REMARK 465 SER H 191 REMARK 465 LEU H 192 REMARK 465 GLY H 193 REMARK 465 CYS H 219 REMARK 465 ARG C 1 REMARK 465 PHE L 208 REMARK 465 ASN L 209 REMARK 465 ARG L 210 REMARK 465 GLY L 211 REMARK 465 GLU L 212 REMARK 465 CYS L 213 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 LYS H 13 CD CE NZ REMARK 470 LYS H 23 CD CE NZ REMARK 470 SER H 31 OG REMARK 470 LYS H 63 CG CD CE NZ REMARK 470 LYS H 108 CG CD CE NZ REMARK 470 SER H 118 OG REMARK 470 LYS H 120 CG CD CE NZ REMARK 470 LEU H 141 CG CD1 CD2 REMARK 470 LYS H 146 CG CD CE NZ REMARK 470 PHE H 149 CG CD1 CD2 CE1 CE2 CZ REMARK 470 THR H 163 OG1 CG2 REMARK 470 SER H 164 OG REMARK 470 VAL H 185 CG1 CG2 REMARK 470 THR H 194 OG1 CG2 REMARK 470 GLN H 195 CB CG CD OE1 NE2 REMARK 470 VAL H 201 CG1 CG2 REMARK 470 ASN H 207 CG OD1 ND2 REMARK 470 LYS H 209 CG CD CE NZ REMARK 470 VAL H 210 CG1 CG2 REMARK 470 LYS H 212 CG CD CE NZ REMARK 470 LYS H 213 CG CD CE NZ REMARK 470 VAL H 214 CG1 CG2 REMARK 470 GLU H 215 CG CD OE1 OE2 REMARK 470 LYS H 217 CG CD CE NZ REMARK 470 SER H 218 OG REMARK 470 MET C 2 CG SD CE REMARK 470 LYS C 3 CG CD CE NZ REMARK 470 GLN C 4 CG CD OE1 NE2 REMARK 470 ASP C 7 CG OD1 OD2 REMARK 470 LYS C 8 CD CE NZ REMARK 470 GLU C 10 CG CD OE1 OE2 REMARK 470 GLU C 11 CG CD OE1 OE2 REMARK 470 SER C 14 OG REMARK 470 LYS C 15 CG CD CE NZ REMARK 470 LYS C 17 CD CE NZ REMARK 470 LYS C 18 CG CD CE NZ REMARK 470 GLU C 20 CG CD OE1 OE2 REMARK 470 LYS C 27 CD CE NZ REMARK 470 LYS C 28 CE NZ REMARK 470 ARG C 43 NE CZ NH1 NH2 REMARK 470 ARG L 24 CD NE CZ NH1 NH2 REMARK 470 TYR L 30 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 LYS L 39 CG CD CE NZ REMARK 470 LYS L 103 CG CD CE NZ REMARK 470 ARG L 107 CG CD NE CZ NH1 NH2 REMARK 470 ILE L 116 CG1 CG2 CD1 REMARK 470 GLU L 122 CG CD OE1 OE2 REMARK 470 LEU L 124 CG CD1 CD2 REMARK 470 LYS L 144 CE NZ REMARK 470 VAL L 145 CG1 CG2 REMARK 470 LYS L 148 CG CD CE NZ REMARK 470 ASN L 151 CG OD1 ND2 REMARK 470 LEU L 153 CG CD1 CD2 REMARK 470 LYS L 168 CG CD CE NZ REMARK 470 LEU L 180 CG CD1 CD2 REMARK 470 SER L 181 OG REMARK 470 LYS L 187 CG CD CE NZ REMARK 470 LYS L 189 CG CD CE NZ REMARK 470 VAL L 204 CG1 CG2 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 PHE H 29 0.14 -69.90 REMARK 500 SER H 31 35.44 73.07 REMARK 500 TYR L 30 -141.34 56.75 REMARK 500 ALA L 51 -18.17 72.38 REMARK 500 ASN L 137 61.98 62.92 REMARK 500 PRO L 140 -162.00 -79.96 REMARK 500 ASP L 150 -138.51 44.32 REMARK 500 REMARK 500 REMARK: NULL DBREF 8VWE H 1 219 PDB 8VWE 8VWE 1 219 DBREF 8VWE C 1 45 PDB 8VWE 8VWE 1 45 DBREF 8VWE L 1 213 PDB 8VWE 8VWE 1 213 SEQRES 1 H 222 GLN VAL GLN LEU VAL GLN SER GLY ALA GLU VAL ARG LYS SEQRES 2 H 222 PRO GLY ALA SER VAL LYS VAL SER CYS LYS ALA SER GLY SEQRES 3 H 222 ASP THR PHE SER SER TYR ALA ILE SER TRP VAL ARG GLN SEQRES 4 H 222 ALA PRO GLY GLN GLY LEU GLU TRP MET GLY SER ILE ILE SEQRES 5 H 222 PRO LEU PHE GLY THR ALA ALA TYR ALA GLN LYS PHE GLN SEQRES 6 H 222 GLY ARG VAL THR ILE THR ALA ASP GLU SER THR SER THR SEQRES 7 H 222 ALA TYR MET GLU LEU SER SER LEU ARG SER GLU ASP THR SEQRES 8 H 222 ALA ILE TYR TYR CYS ALA ARG ASP ASN PRO THR PHE GLY SEQRES 9 H 222 ALA ALA ASP SER TRP GLY LYS GLY THR LEU VAL THR VAL SEQRES 10 H 222 SER SER ALA SER THR LYS GLY PRO SER VAL PHE PRO LEU SEQRES 11 H 222 ALA PRO SER SER LYS SER THR SER GLY GLY THR ALA ALA SEQRES 12 H 222 LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU PRO VAL SEQRES 13 H 222 THR VAL SER TRP ASN SER GLY ALA LEU THR SER GLY VAL SEQRES 14 H 222 HIS THR PHE PRO ALA VAL LEU GLN SER SER GLY LEU TYR SEQRES 15 H 222 SER LEU SER SER VAL VAL THR VAL PRO SER SER SER LEU SEQRES 16 H 222 GLY THR GLN THR TYR ILE CYS ASN VAL ASN HIS LYS PRO SEQRES 17 H 222 SER ASN THR LYS VAL ASP LYS LYS VAL GLU PRO LYS SER SEQRES 18 H 222 CYS SEQRES 1 C 45 ARG MET LYS GLN ILE GLU ASP LYS ILE GLU GLU ILE GLU SEQRES 2 C 45 SER LYS GLN LYS LYS ILE GLU ASN GLU ILE ALA ARG ILE SEQRES 3 C 45 LYS LYS LEU LEU GLN LEU THR VAL TRP GLY ILE LYS GLN SEQRES 4 C 45 LEU GLN ALA ARG ILE LEU SEQRES 1 L 214 ASP ILE GLN MET THR GLN SER PRO SER THR LEU SER ALA SEQRES 2 L 214 SER ILE GLY ASP ARG VAL THR ILE THR CYS ARG ALA SER SEQRES 3 L 214 GLU GLY ILE TYR HIS TRP LEU ALA TRP TYR GLN GLN LYS SEQRES 4 L 214 PRO GLY LYS ALA PRO LYS LEU LEU ILE TYR LYS ALA SER SEQRES 5 L 214 SER LEU ALA SER GLY ALA PRO SER ARG PHE SER GLY SER SEQRES 6 L 214 GLY SER GLY THR ASP PHE THR LEU THR ILE SER SER LEU SEQRES 7 L 214 GLN PRO ASP ASP PHE ALA THR TYR TYR CYS GLN GLN TYR SEQRES 8 L 214 SER ASN TYR PRO LEU THR PHE GLY GLY GLY THR LYS LEU SEQRES 9 L 214 GLU ILE LYS 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 CYS FORMUL 4 HOH *48(H2 O) HELIX 1 AA1 ARG H 84 THR H 88 5 5 HELIX 2 AA2 LYS C 3 LEU C 45 1 43 HELIX 3 AA3 GLN L 79 PHE L 83 5 5 HELIX 4 AA4 SER L 120 LYS L 125 1 6 HELIX 5 AA5 LYS L 182 HIS L 188 1 7 SHEET 1 AA1 4 VAL H 5 GLN H 6 0 SHEET 2 AA1 4 VAL H 18 LYS H 23 -1 O LYS H 23 N VAL H 5 SHEET 3 AA1 4 THR H 78 LEU H 83 -1 O ALA H 79 N CYS H 22 SHEET 4 AA1 4 VAL H 68 ASP H 73 -1 N THR H 69 O GLU H 82 SHEET 1 AA2 6 GLU H 10 ARG H 12 0 SHEET 2 AA2 6 THR H 110 VAL H 114 1 O THR H 113 N ARG H 12 SHEET 3 AA2 6 ALA H 89 ASN H 97 -1 N TYR H 91 O THR H 110 SHEET 4 AA2 6 ALA H 33 GLN H 39 -1 N VAL H 37 O TYR H 92 SHEET 5 AA2 6 LEU H 45 ILE H 51 -1 O GLY H 49 N TRP H 36 SHEET 6 AA2 6 ALA H 58 TYR H 60 -1 O ALA H 59 N SER H 50 SHEET 1 AA3 4 GLU H 10 ARG H 12 0 SHEET 2 AA3 4 THR H 110 VAL H 114 1 O THR H 113 N ARG H 12 SHEET 3 AA3 4 ALA H 89 ASN H 97 -1 N TYR H 91 O THR H 110 SHEET 4 AA3 4 ALA H 102 TRP H 106 -1 O ALA H 102 N ASN H 97 SHEET 1 AA4 4 SER H 123 LEU H 127 0 SHEET 2 AA4 4 ALA H 139 TYR H 148 -1 O GLY H 142 N LEU H 127 SHEET 3 AA4 4 TYR H 179 VAL H 187 -1 O LEU H 181 N VAL H 145 SHEET 4 AA4 4 HIS H 167 THR H 168 -1 N HIS H 167 O VAL H 184 SHEET 1 AA5 4 SER H 123 LEU H 127 0 SHEET 2 AA5 4 ALA H 139 TYR H 148 -1 O GLY H 142 N LEU H 127 SHEET 3 AA5 4 TYR H 179 VAL H 187 -1 O LEU H 181 N VAL H 145 SHEET 4 AA5 4 VAL H 172 LEU H 173 -1 N VAL H 172 O SER H 180 SHEET 1 AA6 3 THR H 154 TRP H 157 0 SHEET 2 AA6 3 TYR H 197 HIS H 203 -1 O ASN H 200 N SER H 156 SHEET 3 AA6 3 THR H 208 VAL H 214 -1 O THR H 208 N HIS H 203 SHEET 1 AA7 4 MET L 4 SER L 7 0 SHEET 2 AA7 4 VAL L 19 ALA L 25 -1 O ARG L 24 N THR L 5 SHEET 3 AA7 4 ASP L 70 ILE L 75 -1 O LEU L 73 N ILE L 21 SHEET 4 AA7 4 PHE L 62 SER L 67 -1 N SER L 63 O THR L 74 SHEET 1 AA8 6 THR L 10 ALA L 13 0 SHEET 2 AA8 6 THR L 102 ILE L 106 1 O GLU L 105 N LEU L 11 SHEET 3 AA8 6 THR L 85 GLN L 89 -1 N TYR L 86 O THR L 102 SHEET 4 AA8 6 ALA L 34 GLN L 38 -1 N ALA L 34 O GLN L 89 SHEET 5 AA8 6 LYS L 45 TYR L 49 -1 O LYS L 45 N GLN L 37 SHEET 6 AA8 6 SER L 53 LEU L 54 -1 O SER L 53 N TYR L 49 SHEET 1 AA9 4 PHE L 115 PHE L 117 0 SHEET 2 AA9 4 THR L 128 PHE L 138 -1 O VAL L 132 N PHE L 117 SHEET 3 AA9 4 TYR L 172 SER L 181 -1 O LEU L 178 N VAL L 131 SHEET 4 AA9 4 SER L 158 VAL L 162 -1 N SER L 161 O SER L 175 SHEET 1 AB1 3 LYS L 144 VAL L 149 0 SHEET 2 AB1 3 TYR L 191 THR L 196 -1 O GLU L 194 N GLN L 146 SHEET 3 AB1 3 VAL L 204 THR L 205 -1 O VAL L 204 N VAL L 195 SSBOND 1 CYS H 22 CYS H 93 1555 1555 2.03 SSBOND 2 CYS H 143 CYS H 199 1555 1555 2.03 SSBOND 3 CYS L 23 CYS L 88 1555 1555 2.03 SSBOND 4 CYS L 133 CYS L 193 1555 1555 2.03 CISPEP 1 PHE H 149 PRO H 150 0 -2.46 CISPEP 2 GLU H 151 PRO H 152 0 -4.47 CISPEP 3 SER L 7 PRO L 8 0 -1.01 CISPEP 4 TYR L 94 PRO L 95 0 0.93 CISPEP 5 TYR L 139 PRO L 140 0 3.14 CRYST1 159.966 159.966 67.969 90.00 90.00 120.00 H 3 9 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 0.006251 0.003609 0.000000 0.00000 SCALE2 0.000000 0.007218 0.000000 0.00000 SCALE3 0.000000 0.000000 0.014713 0.00000