HEADER IMMUNE SYSTEM 13-DEC-24 9MJ3 TITLE CRYSTAL STRUCTURE OF THE VRC01-CLASS ANTIBODY 12A01, DERIVED FROM TITLE 2 GT1.1 VACCINATION, IN COMPLEX WITH EOD-GT8 COMPND MOL_ID: 1; COMPND 2 MOLECULE: 12A01 FAB HEAVY CHAIN; COMPND 3 CHAIN: H; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: 12A01 FAB LIGHT CHAIN; COMPND 7 CHAIN: L; COMPND 8 ENGINEERED: YES; COMPND 9 MOL_ID: 3; COMPND 10 MOLECULE: EOD-GT8 ENGINEERED MUTANT OF GP120; COMPND 11 CHAIN: C; COMPND 12 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_TAXID: 9606; SOURCE 4 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 5 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 6 MOL_ID: 2; SOURCE 7 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 8 ORGANISM_TAXID: 9606; SOURCE 9 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 10 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 11 MOL_ID: 3; SOURCE 12 ORGANISM_SCIENTIFIC: HUMAN IMMUNODEFICIENCY VIRUS 1; SOURCE 13 ORGANISM_TAXID: 11676; SOURCE 14 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 15 EXPRESSION_SYSTEM_TAXID: 9606 KEYWDS FAB, GERMLINE-TARGETING VACCINATION, CD4BS MAB, HIV-1, IMMUNE SYSTEM EXPDTA X-RAY DIFFRACTION AUTHOR S.AGRAWAL,I.A.WILSON REVDAT 1 28-MAY-25 9MJ3 0 JRNL AUTH T.G.CANIELS,M.PRABHAKARAN,G.OZOROWSKI,K.J.MACPHEE,W.WU, JRNL AUTH 2 K.VAN DER STRATEN,S.AGRAWAL,R.DERKING,E.I.M.M.REISS, JRNL AUTH 3 K.MILLARD,M.TURROJA,A.DESROSIERS,J.BETHONY,E.MALKIN, JRNL AUTH 4 M.H.LIESDEK,A.VAN DER VEEN,M.KLOUWENS,J.L.SNITSELAAR, JRNL AUTH 5 J.H.BOUHUIJS,R.BRONSON,J.JEAN-BAPTISTE,S.GAJJALA, JRNL AUTH 6 Z.RIKHTEGARAN TEHRANI,A.BENNER,M.RAMASWAMI,M.O.DUFF,Y.W.LIU, JRNL AUTH 7 A.H.SATO,J.Y.KIM,I.J.L.BAKEN,C.MENDES SILVA,T.P.L.BIJL, JRNL AUTH 8 J.VAN RIJSWIJK,J.A.BURGER,A.CUPO,A.YASMEEN,S.PHULERA, JRNL AUTH 9 W.H.LEE,K.N.RANDALL,S.ZHANG,M.M.CORCORAN,I.REGADAS, JRNL AUTH10 A.C.SULLIVAN,D.M.BROWN,J.A.BOHL,K.M.GREENE,H.GAO,N.L.YATES, JRNL AUTH11 S.SAWANT,J.M.PRINS,N.A.KOOTSTRA,S.M.KAMINSKY,B.BARIN, JRNL AUTH12 F.RAHAMAN,M.MELLER,V.PHILIPONIS,D.S.LAUFER,A.LOMBARDO, JRNL AUTH13 L.MWOGA,S.SHOTORBANI,D.HOLMAN,R.A.KOUP,P.J.KLASSE, JRNL AUTH14 G.B.KARLSSON HEDESTAM,G.D.TOMARAS,M.J.VAN GILS, JRNL AUTH15 D.C.MONTEFIORI,A.B.MCDERMOTT,O.HYRIEN,J.P.MOORE,I.A.WILSON, JRNL AUTH16 A.B.WARD,D.J.DIEMERT,G.J.DE BREE,S.F.ANDREWS,M.CASKEY, JRNL AUTH17 R.W.SANDERS JRNL TITL PRECISE TARGETING OF HIV BROADLY NEUTRALIZING ANTIBODY JRNL TITL 2 PRECURSORS IN HUMANS JRNL REF SCIENCE 2025 JRNL REFN ESSN 1095-9203 JRNL DOI 10.1126/SCIENCE.ADV5572 REMARK 2 REMARK 2 RESOLUTION. 2.20 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 : ML REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 33.90 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340 REMARK 3 COMPLETENESS FOR RANGE (%) : 99.4 REMARK 3 NUMBER OF REFLECTIONS : 44147 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.218 REMARK 3 R VALUE (WORKING SET) : 0.217 REMARK 3 FREE R VALUE : 0.246 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.540 REMARK 3 FREE R VALUE TEST SET COUNT : 1998 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 33.9000 - 6.5900 1.00 2934 141 0.2071 0.2091 REMARK 3 2 6.5800 - 5.2300 1.00 2959 142 0.1977 0.2101 REMARK 3 3 5.2300 - 4.5700 1.00 2966 139 0.1642 0.2154 REMARK 3 4 4.5700 - 4.1600 1.00 2931 144 0.1651 0.1655 REMARK 3 5 4.1600 - 3.8600 1.00 2944 141 0.1742 0.2026 REMARK 3 6 3.8600 - 3.6300 0.99 2933 141 0.1988 0.2439 REMARK 3 7 3.6300 - 3.4500 1.00 2958 138 0.2120 0.2454 REMARK 3 8 3.4500 - 3.3000 1.00 2936 142 0.2157 0.1944 REMARK 3 9 3.3000 - 3.1700 1.00 2970 137 0.2123 0.2675 REMARK 3 10 3.1700 - 3.0600 1.00 2984 141 0.2224 0.2611 REMARK 3 11 3.0600 - 2.9700 1.00 2925 140 0.2279 0.2418 REMARK 3 12 2.9700 - 2.8800 1.00 2915 141 0.2301 0.2868 REMARK 3 13 2.8800 - 2.8100 1.00 2892 133 0.2323 0.2860 REMARK 3 14 2.8100 - 2.7400 1.00 3010 146 0.2452 0.2711 REMARK 3 15 2.7400 - 2.6800 0.99 2868 133 0.2554 0.2995 REMARK 3 16 2.6800 - 2.6200 0.99 3004 147 0.2543 0.2752 REMARK 3 17 2.6200 - 2.5700 0.99 2880 134 0.2597 0.3378 REMARK 3 18 2.5700 - 2.5200 0.99 2954 140 0.2555 0.2588 REMARK 3 19 2.5200 - 2.4700 0.99 2983 143 0.2614 0.3081 REMARK 3 20 2.4700 - 2.4300 0.99 2876 137 0.2582 0.3238 REMARK 3 21 2.4300 - 2.3900 0.99 2961 140 0.2757 0.3336 REMARK 3 22 2.3900 - 2.3600 0.99 2877 137 0.2829 0.2910 REMARK 3 23 2.3600 - 2.3200 0.99 2878 137 0.2734 0.2916 REMARK 3 24 2.3200 - 2.2900 0.99 3001 140 0.2756 0.2953 REMARK 3 25 2.2900 - 2.2600 0.99 2846 136 0.2768 0.3352 REMARK 3 26 2.2600 - 2.2300 0.99 2924 142 0.2873 0.3280 REMARK 3 27 2.2300 - 2.2000 0.98 2876 137 0.2935 0.3135 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) : 0.280 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.220 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL 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 NULL REMARK 3 ANGLE : 0.527 NULL REMARK 3 CHIRALITY : 0.044 710 REMARK 3 PLANARITY : 0.004 816 REMARK 3 DIHEDRAL : 15.294 1702 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 9MJ3 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-DEC-24. REMARK 100 THE DEPOSITION ID IS D_1000291072. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 25-SEP-24 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 : NSLS-II REMARK 200 BEAMLINE : 17-ID-1 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.920 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 9M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : AUTOPROC REMARK 200 DATA SCALING SOFTWARE : AIMLESS REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 44221 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.200 REMARK 200 RESOLUTION RANGE LOW (A) : 33.900 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9 REMARK 200 DATA REDUNDANCY : 13.80 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 10.6000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.24 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 (%): 61.07 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.16 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 1.2M SODIUM DIHYDROGEN PHOSPHATE, 0.1M REMARK 280 CAPS, 0.8M DI-POTASSIUM HYDROGEN PHOSPHATE, 25% GLYCEROL, 0.2M REMARK 280 LITHIUM SULFATE, VAPOR DIFFUSION, SITTING 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 -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 26.84350 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 109.30900 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 36.18200 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 109.30900 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 26.84350 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 36.18200 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: 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 GLN H 1 REMARK 465 SER H 128 REMARK 465 LYS H 129 REMARK 465 SER H 130 REMARK 465 SER H 215 REMARK 465 CYS H 216 REMARK 465 VAL L 1 REMARK 465 SER L 2 REMARK 465 CYS L 212 REMARK 465 TYR C 30 REMARK 465 SER C 31 REMARK 465 ASN C 32 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 GLY C 175 REMARK 465 THR C 176 REMARK 465 LYS C 177 REMARK 465 HIS C 178 REMARK 465 HIS C 179 REMARK 465 HIS C 180 REMARK 465 HIS C 181 REMARK 465 HIS C 182 REMARK 465 HIS C 183 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 ASP H 100C 57.21 -97.21 REMARK 500 ASP H 144 61.20 62.09 REMARK 500 SER L 26 -62.44 -91.19 REMARK 500 GLN L 27 59.44 -97.55 REMARK 500 SER L 52 11.30 -140.60 REMARK 500 ALA L 84 -165.36 -160.08 REMARK 500 TYR L 91 -125.71 57.43 REMARK 500 GLN C 61 -11.80 71.59 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 9MIF RELATED DB: PDB REMARK 900 RELATED ID: 9MID RELATED DB: PDB REMARK 900 RELATED ID: 9MIC RELATED DB: PDB DBREF 9MJ3 H 1 216 PDB 9MJ3 9MJ3 1 216 DBREF 9MJ3 L 1 212 PDB 9MJ3 9MJ3 1 212 DBREF 9MJ3 C 1 183 PDB 9MJ3 9MJ3 1 183 SEQRES 1 H 226 GLN VAL GLN LEU VAL GLN SER GLY ALA GLU VAL LYS GLN SEQRES 2 H 226 PRO GLY ALA SER VAL LYS VAL SER CYS LYS ALA SER GLY SEQRES 3 H 226 TYR THR PHE SER ASP HIS PHE MET HIS TRP VAL ARG GLN SEQRES 4 H 226 ALA PRO GLY GLN GLY LEU GLU TRP MET GLY TRP ILE ASN SEQRES 5 H 226 PRO LYS SER GLY GLY PRO ASN TYR ALA GLN LYS PHE GLN SEQRES 6 H 226 GLY ARG VAL THR MET THR ARG ASP ARG SER ILE SER THR SEQRES 7 H 226 ALA TYR MET GLU LEU ARG GLY LEU ARG SER ASP ASP THR SEQRES 8 H 226 ALA ILE TYR TYR CYS ALA ARG PRO MET HIS ASP TYR ASP SEQRES 9 H 226 ASP HIS ASP TRP TYR PHE ASP LEU TRP GLY ARG GLY THR SEQRES 10 H 226 LEU VAL THR VAL SER SER ALA SER THR LYS GLY PRO SER SEQRES 11 H 226 VAL PHE PRO LEU ALA PRO SER SER LYS SER THR SER GLY SEQRES 12 H 226 GLY THR ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE SEQRES 13 H 226 PRO GLU PRO VAL THR VAL SER TRP ASN SER GLY ALA LEU SEQRES 14 H 226 THR SER GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SER SEQRES 15 H 226 SER GLY LEU TYR SER LEU SER SER VAL VAL THR VAL PRO SEQRES 16 H 226 SER SER SER LEU GLY THR GLN THR TYR ILE CYS ASN VAL SEQRES 17 H 226 ASN HIS LYS PRO SER ASN THR LYS VAL ASP LYS ARG VAL SEQRES 18 H 226 GLU PRO LYS SER CYS SEQRES 1 L 209 VAL SER VAL LEU THR GLN SER PRO GLY THR LEU SER LEU SEQRES 2 L 209 SER PRO GLY GLU ARG ALA THR LEU SER CYS ARG ALA SER SEQRES 3 L 209 GLN THR VAL GLY SER SER TYR LEU ALA TRP TYR GLN GLN SEQRES 4 L 209 LYS PRO GLY GLN ALA PRO ARG LEU LEU ILE TYR GLY ALA SEQRES 5 L 209 SER SER ARG ALA THR GLY ILE PRO ASP ARG PHE SER GLY SEQRES 6 L 209 SER GLY SER GLY THR ASP PHE THR LEU THR ILE SER ARG SEQRES 7 L 209 LEU GLU PRO GLU ASP PHE ALA VAL TYR TYR CYS GLN GLN SEQRES 8 L 209 TYR GLU ALA PHE GLY GLN GLY THR LYS VAL GLU ILE LYS SEQRES 9 L 209 ARG THR VAL ALA ALA PRO SER VAL PHE ILE PHE PRO PRO SEQRES 10 L 209 SER ASP GLU GLN LEU LYS SER GLY THR ALA SER VAL VAL SEQRES 11 L 209 CYS LEU LEU ASN ASN PHE TYR PRO ARG GLU ALA LYS VAL SEQRES 12 L 209 GLN TRP LYS VAL ASP ASN ALA LEU GLN SER GLY ASN SER SEQRES 13 L 209 GLN GLU SER VAL THR GLU GLN ASP SER LYS ASP SER THR SEQRES 14 L 209 TYR SER LEU SER SER THR LEU THR LEU SER LYS ALA ASP SEQRES 15 L 209 TYR GLU LYS HIS LYS VAL TYR ALA CYS GLU VAL THR GLN SEQRES 16 L 209 GLY THR THR SER VAL THR LYS SER PHE ASN ARG GLY GLU SEQRES 17 L 209 CYS SEQRES 1 C 183 ASP THR ILE THR LEU PRO CYS ARG PRO ALA PRO PRO PRO SEQRES 2 C 183 HIS CYS SER SER ASN ILE THR GLY LEU ILE LEU THR ARG SEQRES 3 C 183 GLN GLY GLY TYR SER ASN ALA ASN THR VAL ILE PHE ARG SEQRES 4 C 183 PRO SER GLY GLY ASP TRP ARG ASP ILE ALA ARG CYS GLN SEQRES 5 C 183 ILE ALA GLY THR VAL VAL SER THR GLN LEU PHE LEU ASN SEQRES 6 C 183 GLY SER LEU ALA GLU GLU GLU VAL VAL ILE ARG SER GLU SEQRES 7 C 183 ASP TRP ARG ASP ASN ALA LYS SER ILE CYS VAL GLN LEU SEQRES 8 C 183 ALA THR SER VAL GLU ILE ALA CYS THR GLY ALA GLY HIS SEQRES 9 C 183 CYS ALA ILE SER ARG ALA LYS TRP ALA ASN THR LEU LYS SEQRES 10 C 183 GLN ILE ALA SER LYS LEU ARG GLU GLN TYR GLY ALA LYS SEQRES 11 C 183 THR ILE ILE PHE LYS PRO SER SER GLY GLY ASP PRO GLU SEQRES 12 C 183 PHE VAL ASN HIS SER PHE ASN CYS GLY GLY GLU PHE PHE SEQRES 13 C 183 TYR CYS ALA SER THR GLN LEU PHE ALA SER THR TRP PHE SEQRES 14 C 183 ALA SER THR GLY THR GLY THR LYS 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 *162(H2 O) HELIX 1 AA1 THR H 28 HIS 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 LYS H 201 ASN H 204 5 4 HELIX 7 AA7 GLU L 79 PHE L 83 5 5 HELIX 8 AA8 SER L 121 LYS L 126 1 6 HELIX 9 AA9 LYS L 183 LYS L 188 1 6 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 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 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 PRO H 95 -1 N TYR H 90 O THR H 107 SHEET 4 AA2 6 MET H 34 GLN H 39 -1 N VAL H 37 O TYR H 91 SHEET 5 AA2 6 GLU H 46 ILE H 51 -1 O MET H 48 N TRP H 36 SHEET 6 AA2 6 PRO 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 PRO H 95 -1 N TYR H 90 O THR H 107 SHEET 4 AA3 4 PHE H 100F TRP H 103 -1 O LEU 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 TYR H 176 N TYR H 145 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 TYR H 176 N TYR H 145 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 ARG H 210 -1 O THR H 205 N HIS H 200 SHEET 1 AA7 4 LEU 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 ASP L 70 ILE L 75 -1 O LEU L 73 N LEU L 21 SHEET 4 AA7 4 PHE L 62 SER L 65 -1 N SER L 63 O THR L 74 SHEET 1 AA8 6 THR L 10 LEU 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 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 GLN L 38 O VAL L 85 SHEET 5 AA8 6 ARG L 45 TYR L 49 -1 O ARG L 45 N GLN L 37 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 GLU L 105 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 ALA L 97 PHE L 98 -1 O ALA 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 TYR L 173 N PHE L 139 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 SER L 202 ASN L 208 -1 O VAL L 203 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 THR C 20 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 GLN C 90 N VAL C 74 SHEET 3 AB4 6 SER C 17 ARG C 26 -1 N ILE C 19 O VAL C 95 SHEET 4 AB4 6 VAL C 36 PRO C 40 -1 O ARG C 39 N THR C 25 SHEET 5 AB4 6 ILE C 132 PHE C 134 1 O ILE C 133 N PHE C 38 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 2.03 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 2.04 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 -5.98 CISPEP 2 GLU H 148 PRO H 149 0 -3.25 CISPEP 3 SER L 7 PRO L 8 0 -2.55 CISPEP 4 TYR L 140 PRO L 141 0 1.41 CISPEP 5 ARG C 8 PRO C 9 0 -2.58 CRYST1 53.687 72.364 218.618 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 0.018626 0.000000 0.000000 0.00000 SCALE2 0.000000 0.013819 0.000000 0.00000 SCALE3 0.000000 0.000000 0.004574 0.00000