HEADER IMMUNE SYSTEM 21-APR-25 9OAO TITLE CRYSTAL STRUCTURE OF ANTIBODY FAB G001-0087 FROM IAVI G001 HUMAN TRIAL TITLE 2 IN COMPLEX WITH A GERMLINE-TARGETING GP120 ENGINEERED OUTER DOMAIN TITLE 3 EOD-GT8-MINGLY COMPND MOL_ID: 1; COMPND 2 MOLECULE: G001-0087 FAB HEAVY CHAIN; COMPND 3 CHAIN: H; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: G001-0087 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; 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 9OAO 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. 2.58 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) : 2.58 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 47.74 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.330 REMARK 3 COMPLETENESS FOR RANGE (%) : 97.5 REMARK 3 NUMBER OF REFLECTIONS : 33110 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.239 REMARK 3 R VALUE (WORKING SET) : 0.238 REMARK 3 FREE R VALUE : 0.253 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.930 REMARK 3 FREE R VALUE TEST SET COUNT : 1631 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 47.7400 - 5.9100 1.00 2840 143 0.2326 0.2455 REMARK 3 2 5.9100 - 4.6900 1.00 2742 133 0.2053 0.1930 REMARK 3 3 4.6900 - 4.1000 1.00 2670 138 0.1960 0.2126 REMARK 3 4 4.1000 - 3.7200 1.00 2700 144 0.2149 0.2540 REMARK 3 5 3.7200 - 3.4600 1.00 2674 133 0.2365 0.2446 REMARK 3 6 3.4600 - 3.2500 1.00 2685 122 0.2434 0.2309 REMARK 3 7 3.2500 - 3.0900 1.00 2639 142 0.2635 0.2574 REMARK 3 8 3.0900 - 2.9600 0.99 2658 142 0.2918 0.3399 REMARK 3 9 2.9600 - 2.8400 0.98 2588 124 0.2870 0.3417 REMARK 3 10 2.8400 - 2.7400 0.98 2601 153 0.2962 0.3093 REMARK 3 11 2.7400 - 2.6600 0.97 2538 148 0.2985 0.3287 REMARK 3 12 2.6600 - 2.5800 0.80 2144 109 0.3388 0.3674 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) : 0.312 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.428 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 44.32 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 48.13 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 : 0.003 4649 REMARK 3 ANGLE : 0.550 6322 REMARK 3 CHIRALITY : 0.045 710 REMARK 3 PLANARITY : 0.005 813 REMARK 3 DIHEDRAL : 11.827 1689 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 9OAO 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_1000295198. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 22-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 : APS REMARK 200 BEAMLINE : 23-ID-B REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.0332 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 : 33387 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.580 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 (%) : 99.3 REMARK 200 DATA REDUNDANCY : 10.50 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 12.3000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.58 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.64 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 (%): 69.33 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.01 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 20% (W/V) PEG 3000, 0.1 M SODIUM REMARK 280 CITRATE PH 5.5, WITH ADDITION OF 10% (V/V) ETHYLENE GLYCOL, REMARK 280 VAPOR DIFFUSION, SITTING DROP, 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 51.25000 REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 68.08550 REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 76.47200 REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 51.25000 REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 68.08550 REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 76.47200 REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 51.25000 REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 68.08550 REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 76.47200 REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 51.25000 REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 68.08550 REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 76.47200 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 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 132 REMARK 465 GLY H 133 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 HIS 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 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 GLN H 98 -71.21 -160.93 REMARK 500 PHE H 100A 86.52 -65.68 REMARK 500 SER H 127 -156.34 -137.37 REMARK 500 ASP H 144 83.10 56.97 REMARK 500 ALA L 51 -39.69 68.59 REMARK 500 TYR L 91 -119.54 57.63 REMARK 500 ASN L 138 75.24 56.45 REMARK 500 ASP C 44 -146.95 -128.48 REMARK 500 GLN C 61 -59.34 64.11 REMARK 500 GLU C 71 -59.79 -122.28 REMARK 500 ALA C 165 58.97 -157.21 REMARK 500 REMARK 500 REMARK: NULL REMARK 525 REMARK 525 SOLVENT REMARK 525 REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER; REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE REMARK 525 NUMBER; I=INSERTION CODE): REMARK 525 REMARK 525 M RES CSSEQI REMARK 525 HOH L 370 DISTANCE = 7.89 ANGSTROMS DBREF 9OAO H 1 216 PDB 9OAO 9OAO 1 216 DBREF 9OAO L 1 214 PDB 9OAO 9OAO 1 214 DBREF 9OAO C -2 180 PDB 9OAO 9OAO -2 180 SEQRES 1 H 221 GLN VAL GLN LEU VAL GLN SER GLY ALA GLU VAL LYS LYS SEQRES 2 H 221 PRO GLY ALA SER VAL LYS VAL SER CYS LYS ALA SER GLY SEQRES 3 H 221 TYR THR PHE THR GLY ASN TYR ILE HIS TRP VAL ARG GLN SEQRES 4 H 221 ALA PRO GLY GLN GLY LEU GLU TRP VAL GLY TRP LEU ASN SEQRES 5 H 221 PRO ASN SER GLY GLY THR ASN TYR ALA GLN GLN PHE GLN SEQRES 6 H 221 GLY ARG VAL THR MET THR ARG ASP THR SER ILE SER THR SEQRES 7 H 221 ALA TYR MET GLU LEU ASN ARG LEU ARG SER ASP ASP THR SEQRES 8 H 221 ALA VAL PHE TYR CYS ALA ARG GLY LEU TRP GLN TRP GLU SEQRES 9 H 221 PHE ARG TYR TRP GLY GLN GLY THR LEU VAL THR VAL SER SEQRES 10 H 221 SER ALA SER THR LYS GLY PRO SER VAL PHE PRO LEU ALA SEQRES 11 H 221 PRO SER SER LYS SER THR SER GLY GLY THR ALA ALA LEU SEQRES 12 H 221 GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU PRO VAL THR SEQRES 13 H 221 VAL SER TRP ASN SER GLY ALA LEU THR SER GLY VAL HIS SEQRES 14 H 221 THR PHE PRO ALA VAL LEU GLN SER SER GLY LEU TYR SER SEQRES 15 H 221 LEU SER SER VAL VAL THR VAL PRO SER SER SER LEU GLY SEQRES 16 H 221 THR GLN THR TYR ILE CYS ASN VAL ASN HIS LYS PRO SER SEQRES 17 H 221 ASN THR LYS VAL ASP LYS LYS VAL GLU PRO LYS SER CYS SEQRES 1 L 211 ASP ILE VAL LEU THR GLN SER PRO GLY THR LEU SER LEU SEQRES 2 L 211 SER PRO GLY GLU ARG ALA THR LEU SER CYS ARG ALA SER SEQRES 3 L 211 GLN SER VAL SER SER SER ASN LEU ALA TRP TYR GLN GLN SEQRES 4 L 211 LYS PRO GLY GLN ALA PRO ARG LEU LEU ILE TYR GLY ALA SEQRES 5 L 211 SER SER ARG ALA THR GLY ILE PRO ASP ARG PHE SER GLY SEQRES 6 L 211 SER GLY SER GLY THR ASP PHE THR LEU THR ILE SER ARG SEQRES 7 L 211 LEU GLU PRO GLU ASP CYS ALA VAL TYR TYR CYS GLN GLN SEQRES 8 L 211 TYR GLU GLY PHE GLY GLY GLY THR LYS VAL GLU ILE LYS SEQRES 9 L 211 ARG THR VAL ALA ALA PRO SER VAL PHE ILE PHE PRO PRO SEQRES 10 L 211 SER ASP GLU GLN LEU LYS SER GLY THR ALA SER VAL VAL SEQRES 11 L 211 CYS LEU LEU ASN ASN PHE TYR PRO ARG GLU ALA LYS VAL SEQRES 12 L 211 GLN TRP LYS VAL ASP ASN ALA LEU GLN SER GLY ASN SER SEQRES 13 L 211 GLN GLU SER VAL THR GLU GLN ASP SER LYS ASP SER THR SEQRES 14 L 211 TYR SER LEU SER SER THR LEU THR LEU SER LYS ALA ASP SEQRES 15 L 211 TYR GLU LYS HIS LYS VAL TYR ALA CYS GLU VAL THR HIS SEQRES 16 L 211 GLN GLY LEU SER SER PRO VAL THR LYS SER PHE ASN ARG SEQRES 17 L 211 GLY GLU CYS SEQRES 1 C 183 GLU THR GLY ASP THR ILE THR LEU PRO CYS ARG PRO ALA SEQRES 2 C 183 PRO PRO PRO HIS CYS SER SER ASN ILE THR GLY LEU ILE SEQRES 3 C 183 LEU THR ARG GLN GLY GLY TYR SER ASN ALA ASN THR VAL SEQRES 4 C 183 ILE PHE ARG PRO SER GLY GLY ASP TRP ARG ASP ILE ALA SEQRES 5 C 183 ARG CYS GLN ILE ALA GLY THR VAL VAL SER THR GLN LEU SEQRES 6 C 183 PHE LEU ASN GLY SER LEU ALA GLU GLU GLU VAL VAL ILE SEQRES 7 C 183 ARG SER GLU ASP TRP ARG ASP ASN ALA LYS SER ILE CYS SEQRES 8 C 183 VAL GLN LEU ALA THR SER VAL GLU ILE ALA CYS THR GLY SEQRES 9 C 183 ALA GLY HIS CYS ALA ILE SER ARG ALA LYS TRP ALA ASN SEQRES 10 C 183 THR LEU LYS GLN ILE ALA SER LYS LEU ARG GLU GLN TYR SEQRES 11 C 183 GLY ALA LYS THR ILE ILE PHE LYS PRO SER SER GLY GLY SEQRES 12 C 183 ASP PRO GLU PHE VAL ASN HIS SER PHE ASN CYS GLY GLY SEQRES 13 C 183 GLU PHE PHE TYR CYS ALA SER THR GLN LEU PHE ALA SER SEQRES 14 C 183 THR TRP PHE ALA SER THR GLY THR HIS HIS HIS HIS HIS SEQRES 15 C 183 HIS HET NAG C 201 14 HET NAG C 202 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 2(C8 H15 N O6) FORMUL 6 HOH *152(H2 O) HELIX 1 AA1 THR H 28 ASN H 32 5 5 HELIX 2 AA2 GLN H 61 GLN H 64 5 4 HELIX 3 AA3 ARG H 83 THR H 87 5 5 HELIX 4 AA4 SER H 156 ALA H 158 5 3 HELIX 5 AA5 SER H 187 LEU H 189 5 3 HELIX 6 AA6 SER L 29 SER L 31 5 3 HELIX 7 AA7 GLU L 79 CYS L 83 5 5 HELIX 8 AA8 SER L 121 SER L 127 1 7 HELIX 9 AA9 LYS L 183 GLU L 187 1 5 HELIX 10 AB1 PRO C 12 SER C 16 5 5 HELIX 11 AB2 ASP C 44 ARG C 50 1 7 HELIX 12 AB3 ARG C 109 GLY C 128 1 20 HELIX 13 AB4 ASP C 141 ASN C 146 1 6 HELIX 14 AB5 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 ALA H 78 N CYS H 22 SHEET 4 AA1 4 VAL H 67 ASP H 72 -1 N THR H 70 O TYR H 79 SHEET 1 AA2 6 GLU H 10 LYS H 12 0 SHEET 2 AA2 6 THR H 107 VAL H 111 1 O LEU H 108 N GLU H 10 SHEET 3 AA2 6 ALA H 88 GLY H 95 -1 N ALA H 88 O VAL H 109 SHEET 4 AA2 6 ILE H 34 GLN H 39 -1 N VAL H 37 O TYR H 91 SHEET 5 AA2 6 GLU H 46 LEU H 51 -1 O GLU H 46 N ARG H 38 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 LEU H 108 N GLU H 10 SHEET 3 AA3 4 ALA H 88 GLY H 95 -1 N ALA H 88 O VAL H 109 SHEET 4 AA3 4 PHE H 100A 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 ILE H 195 HIS H 200 -1 O ASN H 197 N SER H 153 SHEET 3 AA6 3 THR H 205 LYS H 210 -1 O VAL H 207 N VAL H 198 SHEET 1 AA7 3 LEU L 4 SER L 7 0 SHEET 2 AA7 3 ALA L 19 VAL L 28 -1 O ARG L 24 N THR L 5 SHEET 3 AA7 3 PHE L 62 ILE L 75 -1 O LEU L 73 N LEU L 21 SHEET 1 AA8 6 THR L 10 LEU 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 LEU L 33 GLN L 38 -1 N GLN L 38 O VAL L 85 SHEET 5 AA8 6 ARG L 45 TYR L 49 -1 O ILE L 48 N TRP L 35 SHEET 6 AA8 6 SER L 53 ARG L 54 -1 O SER L 53 N TYR L 49 SHEET 1 AA9 4 THR L 10 LEU 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 GLY L 97 PHE L 98 -1 O GLY 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 181 N ALA L 130 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 LYS L 145 VAL L 150 -1 N VAL L 150 O ALA L 153 SHEET 3 AB2 4 VAL L 191 THR L 197 -1 O ALA L 193 N LYS L 149 SHEET 4 AB2 4 VAL L 205 ASN L 210 -1 O VAL L 205 N VAL L 196 SHEET 1 AB3 7 LEU C 62 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 SER C 166 TRP C 168 -1 O TRP C 168 N ILE C 132 SSBOND 1 CYS H 22 CYS H 92 1555 1555 2.04 SSBOND 2 CYS H 140 CYS H 196 1555 1555 2.04 SSBOND 3 CYS L 23 CYS L 88 1555 1555 2.04 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 CISPEP 1 PHE H 146 PRO H 147 0 -4.69 CISPEP 2 GLU H 148 PRO H 149 0 0.94 CISPEP 3 SER L 7 PRO L 8 0 -1.94 CISPEP 4 TYR L 140 PRO L 141 0 3.34 CISPEP 5 ARG C 8 PRO C 9 0 -1.53 CRYST1 102.500 136.171 152.944 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 0.009756 0.000000 0.000000 0.00000 SCALE2 0.000000 0.007344 0.000000 0.00000 SCALE3 0.000000 0.000000 0.006538 0.00000