HEADER IMMUNE SYSTEM 21-APR-25 9OAQ TITLE CRYSTAL STRUCTURE OF ANTIBODY FAB G001-59 FROM IAVI G001 HUMAN TRIAL TITLE 2 IN COMPLEX WITH A GERMLINE-TARGETING GP120 ENGINEERED OUTER DOMAIN TITLE 3 EOD-GT8-MINGLY-N276 COMPND MOL_ID: 1; COMPND 2 MOLECULE: G001-59 FAB HEAVY CHAIN; COMPND 3 CHAIN: H; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: G001-59 FAB LIGHT CHAIN; COMPND 7 CHAIN: L; COMPND 8 ENGINEERED: YES; COMPND 9 MOL_ID: 3; COMPND 10 MOLECULE: GERMLINE-TARGETING HIV-1 GP120 ENGINEERED OUTER DOMAIN EOD- COMPND 11 GT8-MINGLY-N276; COMPND 12 CHAIN: C; COMPND 13 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 MOL_ID: 2; SOURCE 9 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 10 ORGANISM_COMMON: HUMAN; SOURCE 11 ORGANISM_TAXID: 9606; SOURCE 12 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 13 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 14 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 15 MOL_ID: 3; SOURCE 16 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 17 ORGANISM_COMMON: HUMAN; SOURCE 18 ORGANISM_TAXID: 9606; SOURCE 19 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 20 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 21 EXPRESSION_SYSTEM_TAXID: 9606 KEYWDS HIV-1 ENVELOPE ANTIBODY, HIV CD4 BINDING SITE ANTIBODY, IAVI G001 KEYWDS 2 CLINICAL TRIAL, GERMLINE-TARGETING IMMUNOGEN, IMMUNE SYSTEM EXPDTA X-RAY DIFFRACTION AUTHOR X.LIN,I.A.WILSON REVDAT 1 25-JUN-25 9OAQ 0 JRNL AUTH X.LIN,C.A.COTTRELL,O.KALYUZHNIY,R.TINGLE,M.KUBITZ,D.LU, JRNL AUTH 2 M.YUAN,W.R.SCHIEF,I.A.WILSON JRNL TITL STRUCTURAL INSIGHTS INTO VRC01-CLASS BNAB PRECURSORS WITH JRNL TITL 2 DIVERSE LIGHT CHAINS ELICITED IN THE IAVI G001 HUMAN VACCINE JRNL TITL 3 TRIAL. JRNL REF BIORXIV 2025 JRNL REFN ISSN 2692-8205 JRNL PMID 40501797 JRNL DOI 10.1101/2025.05.22.655646 REMARK 2 REMARK 2 RESOLUTION. 2.54 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX 1.21.2_5419 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) : 2.54 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 38.50 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340 REMARK 3 COMPLETENESS FOR RANGE (%) : 98.3 REMARK 3 NUMBER OF REFLECTIONS : 34672 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.209 REMARK 3 R VALUE (WORKING SET) : 0.208 REMARK 3 FREE R VALUE : 0.230 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.810 REMARK 3 FREE R VALUE TEST SET COUNT : 1668 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 38.5000 - 5.8200 0.97 2879 143 0.1834 0.1984 REMARK 3 2 5.8200 - 4.6200 1.00 2832 135 0.1528 0.1602 REMARK 3 3 4.6200 - 4.0400 1.00 2798 159 0.1517 0.1709 REMARK 3 4 4.0400 - 3.6700 1.00 2754 163 0.1883 0.2053 REMARK 3 5 3.6700 - 3.4000 0.96 2703 127 0.2038 0.2477 REMARK 3 6 3.4000 - 3.2000 0.99 2743 138 0.2156 0.2558 REMARK 3 7 3.2000 - 3.0400 1.00 2785 145 0.2767 0.3105 REMARK 3 8 3.0400 - 2.9100 0.99 2731 135 0.2689 0.3062 REMARK 3 9 2.9100 - 2.8000 0.98 2718 133 0.2650 0.2893 REMARK 3 10 2.8000 - 2.7000 0.98 2715 126 0.3047 0.3529 REMARK 3 11 2.7000 - 2.6200 0.98 2743 128 0.3775 0.3998 REMARK 3 12 2.6200 - 2.5400 0.95 2603 136 0.4791 0.5730 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL REMARK 3 SOLVENT RADIUS : 1.11 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) : 0.455 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 27.821 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 56.08 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 57.52 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 : 0.002 4693 REMARK 3 ANGLE : 0.538 6385 REMARK 3 CHIRALITY : 0.045 724 REMARK 3 PLANARITY : 0.004 812 REMARK 3 DIHEDRAL : 12.354 1710 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 9OAQ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-APR-25. REMARK 100 THE DEPOSITION ID IS D_1000295185. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 24-JUL-21 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 : BL12-1 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.9795 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 16M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : XDS REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 34890 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.540 REMARK 200 RESOLUTION RANGE LOW (A) : 50.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.0 REMARK 200 DATA REDUNDANCY : 11.40 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 14.5000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.54 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.58 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: PHASER REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 68.93 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.96 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: IN 20% (W/V) PEG 3350 AND 0.2 M REMARK 280 MAGNESIUM SULFATE AT PH 5.9, VAPOR DIFFUSION, SITTING DROP, REMARK 280 TEMPERATURE 293.15K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 2 2 2 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 -X,Y,-Z REMARK 290 4555 X,-Y,-Z REMARK 290 5555 X+1/2,Y+1/2,Z+1/2 REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2 REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2 REMARK 290 8555 X+1/2,-Y+1/2,-Z+1/2 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 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 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 0.00000 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 51.34250 REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 66.98650 REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 77.00700 REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 51.34250 REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 66.98650 REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 77.00700 REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 51.34250 REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 66.98650 REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 77.00700 REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 51.34250 REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 66.98650 REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 77.00700 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: TRIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 6210 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 26170 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -9.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: H, L, C 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 LYS H 129 REMARK 465 SER H 130 REMARK 465 THR H 131 REMARK 465 SER H 215 REMARK 465 CYS H 216 REMARK 465 CYS L 214 REMARK 465 GLU C -2 REMARK 465 THR C -1 REMARK 465 GLY C 0 REMARK 465 ALA C 170 REMARK 465 SER C 171 REMARK 465 THR C 172 REMARK 465 GLY C 173 REMARK 465 THR C 174 REMARK 465 LYS C 175 REMARK 465 HIS C 176 REMARK 465 HIS C 177 REMARK 465 HIS C 178 REMARK 465 HIS C 179 REMARK 465 HIS C 180 REMARK 465 HIS C 181 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 ILE H 98 -73.64 -8.63 REMARK 500 ASP H 144 62.91 61.61 REMARK 500 THR L 51 -15.45 73.13 REMARK 500 ALA L 84 -167.86 -162.56 REMARK 500 TYR L 91 -124.80 58.78 REMARK 500 ASP C 44 -166.72 -126.57 REMARK 500 GLN C 61 -9.88 71.29 REMARK 500 REMARK 500 REMARK: NULL DBREF 9OAQ H 1 216 PDB 9OAQ 9OAQ 1 216 DBREF 9OAQ L 1 214 PDB 9OAQ 9OAQ 1 214 DBREF 9OAQ C -2 181 PDB 9OAQ 9OAQ -2 181 SEQRES 1 H 223 GLN VAL GLN LEU VAL GLN SER GLY ALA GLU VAL LYS LYS SEQRES 2 H 223 PRO GLY THR SER VAL LYS VAL SER CYS LYS ALA SER GLU SEQRES 3 H 223 TYR THR PHE THR GLY TYR TYR VAL HIS TRP VAL ARG GLN SEQRES 4 H 223 ALA PRO GLY GLN GLY LEU GLU TRP MET GLY TRP ILE ASN SEQRES 5 H 223 PRO ASN SER GLY GLY THR ASN TYR ALA GLN LYS PHE GLN SEQRES 6 H 223 GLY TRP VAL THR MET THR ARG ASP THR SER ILE SER THR SEQRES 7 H 223 ALA TYR MET GLU LEU SER ARG LEU LYS SER ASP ASP THR SEQRES 8 H 223 ALA VAL TYR TYR CYS ALA ARG SER ASP TYR ILE SER SER SEQRES 9 H 223 TRP TYR PHE GLY TYR TRP GLY GLN GLY THR LEU VAL THR SEQRES 10 H 223 VAL SER SER ALA SER THR LYS GLY PRO SER VAL PHE PRO SEQRES 11 H 223 LEU ALA PRO SER SER LYS SER THR SER GLY GLY THR ALA SEQRES 12 H 223 ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU PRO SEQRES 13 H 223 VAL THR VAL SER TRP ASN SER GLY ALA LEU THR SER GLY SEQRES 14 H 223 VAL HIS THR PHE PRO ALA VAL LEU GLN SER SER GLY LEU SEQRES 15 H 223 TYR SER LEU SER SER VAL VAL THR VAL PRO SER SER SER SEQRES 16 H 223 LEU GLY THR GLN THR TYR ILE CYS ASN VAL ASN HIS LYS SEQRES 17 H 223 PRO SER ASN THR LYS VAL ASP LYS LYS VAL GLU PRO LYS SEQRES 18 H 223 SER CYS SEQRES 1 L 210 GLU ILE VAL MET THR GLN SER PRO ALA THR LEU SER VAL SEQRES 2 L 210 SER PRO GLY GLU ARG ALA THR LEU SER CYS ARG ALA SER SEQRES 3 L 210 GLN SER VAL SER SER ASN LEU ALA TRP TYR GLN GLN LYS SEQRES 4 L 210 PRO GLY GLN ALA PRO ARG LEU LEU ILE TYR GLY THR SER SEQRES 5 L 210 THR ARG ALA THR GLY ILE PRO ALA ARG PHE SER GLY SER SEQRES 6 L 210 GLY SER GLY THR GLU PHE THR LEU THR ILE SER SER LEU SEQRES 7 L 210 GLN SER GLU ASP PHE ALA VAL TYR TYR CYS GLN GLN TYR SEQRES 8 L 210 GLU THR PHE GLY GLN GLY THR LYS VAL GLU ILE LYS ARG SEQRES 9 L 210 THR VAL ALA ALA PRO SER VAL PHE ILE PHE PRO PRO SER SEQRES 10 L 210 ASP GLU GLN LEU LYS SER GLY THR ALA SER VAL VAL CYS SEQRES 11 L 210 LEU LEU ASN ASN PHE TYR PRO ARG GLU ALA LYS VAL GLN SEQRES 12 L 210 TRP LYS VAL ASP ASN ALA LEU GLN SER GLY ASN SER GLN SEQRES 13 L 210 GLU SER VAL THR GLU GLN ASP SER LYS ASP SER THR TYR SEQRES 14 L 210 SER LEU SER SER THR LEU THR LEU SER LYS ALA ASP TYR SEQRES 15 L 210 GLU LYS HIS LYS VAL TYR ALA CYS GLU VAL THR HIS GLN SEQRES 16 L 210 GLY LEU SER SER PRO VAL THR LYS SER PHE ASN ARG GLY SEQRES 17 L 210 GLU CYS SEQRES 1 C 184 GLU THR GLY ASP THR ILE THR LEU PRO CYS ARG PRO ALA SEQRES 2 C 184 PRO PRO PRO HIS CYS SER SER ASN ILE THR GLY LEU ILE SEQRES 3 C 184 LEU THR ARG GLN GLY GLY TYR SER ASN ALA ASN THR VAL SEQRES 4 C 184 ILE PHE ARG PRO SER GLY GLY ASP TRP ARG ASP ILE ALA SEQRES 5 C 184 ARG CYS GLN ILE ALA GLY THR VAL VAL SER THR GLN LEU SEQRES 6 C 184 PHE LEU ASN GLY SER LEU ALA GLU GLU GLU VAL VAL ILE SEQRES 7 C 184 ARG SER GLU ASN TRP THR ASP ASN ALA LYS SER ILE CYS SEQRES 8 C 184 VAL GLN LEU ALA THR SER VAL GLU ILE ALA CYS THR GLY SEQRES 9 C 184 ALA GLY HIS CYS ALA ILE SER ARG ALA LYS TRP ALA ASN SEQRES 10 C 184 THR LEU LYS GLN ILE ALA SER LYS LEU ARG GLU GLN TYR SEQRES 11 C 184 GLY ALA LYS THR ILE ILE PHE LYS PRO SER SER GLY GLY SEQRES 12 C 184 ASP PRO GLU PHE VAL ASN HIS SER PHE ASN CYS GLY GLY SEQRES 13 C 184 GLU PHE PHE TYR CYS ALA SER THR GLN LEU PHE ALA SER SEQRES 14 C 184 THR TRP PHE ALA SER THR GLY THR LYS HIS HIS HIS HIS SEQRES 15 C 184 HIS HIS HET NAG C 201 14 HET NAG C 202 14 HET NAG C 203 14 HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE HETSYN NAG N-ACETYL-BETA-D-GLUCOSAMINE; 2-ACETAMIDO-2-DEOXY-BETA- HETSYN 2 NAG D-GLUCOSE; 2-ACETAMIDO-2-DEOXY-D-GLUCOSE; 2-ACETAMIDO- HETSYN 3 NAG 2-DEOXY-GLUCOSE; N-ACETYL-D-GLUCOSAMINE FORMUL 4 NAG 3(C8 H15 N O6) FORMUL 7 HOH *134(H2 O) HELIX 1 AA1 THR H 28 TYR H 32 5 5 HELIX 2 AA2 LYS H 83 THR H 87 5 5 HELIX 3 AA3 SER H 156 ALA H 158 5 3 HELIX 4 AA4 SER H 187 LEU H 189 5 3 HELIX 5 AA5 GLN L 79 PHE L 83 5 5 HELIX 6 AA6 SER L 121 SER L 127 1 7 HELIX 7 AA7 LYS L 183 GLU L 187 1 5 HELIX 8 AA8 PRO C 12 SER C 16 5 5 HELIX 9 AA9 ASP C 44 GLN C 52 1 9 HELIX 10 AB1 ARG C 109 GLY C 128 1 20 HELIX 11 AB2 ASP C 141 ASN C 146 1 6 HELIX 12 AB3 SER C 160 PHE C 164 5 5 SHEET 1 AA1 4 GLN H 3 GLN H 6 0 SHEET 2 AA1 4 VAL H 18 SER H 25 -1 O LYS H 23 N VAL H 5 SHEET 3 AA1 4 THR H 77 LEU H 82 -1 O MET H 80 N VAL H 20 SHEET 4 AA1 4 VAL H 67 ASP H 72 -1 N THR H 68 O GLU H 81 SHEET 1 AA2 6 GLU H 10 LYS H 12 0 SHEET 2 AA2 6 THR H 107 VAL H 111 1 O THR H 110 N LYS H 12 SHEET 3 AA2 6 ALA H 88 SER H 95 -1 N TYR H 90 O THR H 107 SHEET 4 AA2 6 VAL H 34 GLN H 39 -1 N VAL H 37 O TYR H 91 SHEET 5 AA2 6 LEU H 45 ILE H 51 -1 O MET H 48 N TRP H 36 SHEET 6 AA2 6 THR H 57 TYR H 59 -1 O ASN H 58 N TRP H 50 SHEET 1 AA3 4 GLU H 10 LYS H 12 0 SHEET 2 AA3 4 THR H 107 VAL H 111 1 O THR H 110 N LYS H 12 SHEET 3 AA3 4 ALA H 88 SER H 95 -1 N TYR H 90 O THR H 107 SHEET 4 AA3 4 PHE H 100C TRP H 103 -1 O TYR H 102 N ARG H 94 SHEET 1 AA4 4 SER H 120 LEU H 124 0 SHEET 2 AA4 4 THR H 135 TYR H 145 -1 O LEU H 141 N PHE H 122 SHEET 3 AA4 4 TYR H 176 PRO H 185 -1 O VAL H 184 N ALA H 136 SHEET 4 AA4 4 VAL H 163 THR H 165 -1 N HIS H 164 O VAL H 181 SHEET 1 AA5 4 SER H 120 LEU H 124 0 SHEET 2 AA5 4 THR H 135 TYR H 145 -1 O LEU H 141 N PHE H 122 SHEET 3 AA5 4 TYR H 176 PRO H 185 -1 O VAL H 184 N ALA H 136 SHEET 4 AA5 4 VAL H 169 LEU H 170 -1 N VAL H 169 O SER H 177 SHEET 1 AA6 3 THR H 151 TRP H 154 0 SHEET 2 AA6 3 TYR H 194 HIS H 200 -1 O ASN H 197 N SER H 153 SHEET 3 AA6 3 THR H 205 VAL H 211 -1 O VAL H 207 N VAL H 198 SHEET 1 AA7 4 MET L 4 SER L 7 0 SHEET 2 AA7 4 ALA L 19 ALA L 25 -1 O ARG L 24 N THR L 5 SHEET 3 AA7 4 GLU L 70 ILE L 75 -1 O LEU L 73 N LEU L 21 SHEET 4 AA7 4 PHE L 62 SER L 67 -1 N SER L 65 O THR L 72 SHEET 1 AA8 6 THR L 10 VAL L 13 0 SHEET 2 AA8 6 THR L 102 ILE L 106 1 O LYS L 103 N LEU L 11 SHEET 3 AA8 6 VAL L 85 GLN L 90 -1 N TYR L 86 O THR L 102 SHEET 4 AA8 6 ALA L 34 GLN L 38 -1 N TYR L 36 O TYR L 87 SHEET 5 AA8 6 ARG L 45 TYR L 49 -1 O ARG L 45 N GLN L 37 SHEET 6 AA8 6 THR L 53 ARG L 54 -1 O THR L 53 N TYR L 49 SHEET 1 AA9 4 THR L 10 VAL L 13 0 SHEET 2 AA9 4 THR L 102 ILE L 106 1 O LYS L 103 N LEU L 11 SHEET 3 AA9 4 VAL L 85 GLN L 90 -1 N TYR L 86 O THR L 102 SHEET 4 AA9 4 THR L 97 PHE L 98 -1 O THR L 97 N GLN L 90 SHEET 1 AB1 4 SER L 114 PHE L 118 0 SHEET 2 AB1 4 THR L 129 PHE L 139 -1 O LEU L 135 N PHE L 116 SHEET 3 AB1 4 TYR L 173 SER L 182 -1 O LEU L 175 N LEU L 136 SHEET 4 AB1 4 SER L 159 VAL L 163 -1 N GLN L 160 O THR L 178 SHEET 1 AB2 4 ALA L 153 LEU L 154 0 SHEET 2 AB2 4 ALA L 144 VAL L 150 -1 N VAL L 150 O ALA L 153 SHEET 3 AB2 4 VAL L 191 HIS L 198 -1 O THR L 197 N LYS L 145 SHEET 4 AB2 4 VAL L 205 ASN L 210 -1 O VAL L 205 N VAL L 196 SHEET 1 AB3 7 PHE C 63 LEU C 64 0 SHEET 2 AB3 7 SER C 17 ARG C 26 -1 N GLY C 21 O PHE C 63 SHEET 3 AB3 7 ILE C 87 CYS C 99 -1 O VAL C 95 N ILE C 19 SHEET 4 AB3 7 HIS C 104 SER C 108 -1 O ALA C 106 N ALA C 98 SHEET 5 AB3 7 THR C 2 ARG C 8 -1 N ILE C 3 O ILE C 107 SHEET 6 AB3 7 GLU C 154 CYS C 158 -1 O TYR C 157 N ARG C 8 SHEET 7 AB3 7 HIS C 147 CYS C 151 -1 N HIS C 147 O CYS C 158 SHEET 1 AB4 6 VAL C 74 ARG C 76 0 SHEET 2 AB4 6 ILE C 87 CYS C 99 -1 O CYS C 88 N ARG C 76 SHEET 3 AB4 6 SER C 17 ARG C 26 -1 N ILE C 19 O VAL C 95 SHEET 4 AB4 6 THR C 35 PRO C 40 -1 O ARG C 39 N THR C 25 SHEET 5 AB4 6 THR C 131 PHE C 134 1 O THR C 131 N VAL C 36 SHEET 6 AB4 6 THR C 167 TRP C 168 -1 O TRP C 168 N ILE C 132 SSBOND 1 CYS H 22 CYS H 92 1555 1555 2.03 SSBOND 2 CYS H 140 CYS H 196 1555 1555 2.03 SSBOND 3 CYS L 23 CYS L 88 1555 1555 2.03 SSBOND 4 CYS L 134 CYS L 194 1555 1555 2.04 SSBOND 5 CYS C 7 CYS C 158 1555 1555 2.03 SSBOND 6 CYS C 15 CYS C 151 1555 1555 2.03 SSBOND 7 CYS C 51 CYS C 88 1555 1555 2.03 SSBOND 8 CYS C 99 CYS C 105 1555 1555 2.03 LINK ND2 ASN C 18 C1 NAG C 201 1555 1555 1.44 LINK ND2 ASN C 65 C1 NAG C 202 1555 1555 1.44 LINK ND2 ASN C 79 C1 NAG C 203 1555 1555 1.44 CISPEP 1 PHE H 146 PRO H 147 0 -6.30 CISPEP 2 GLU H 148 PRO H 149 0 0.66 CISPEP 3 SER L 7 PRO L 8 0 -4.48 CISPEP 4 TYR L 140 PRO L 141 0 1.48 CISPEP 5 ARG C 8 PRO C 9 0 -2.54 CRYST1 102.685 133.973 154.014 90.00 90.00 90.00 I 2 2 2 8 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 0.009739 0.000000 0.000000 0.00000 SCALE2 0.000000 0.007464 0.000000 0.00000 SCALE3 0.000000 0.000000 0.006493 0.00000