HEADER IMMUNE SYSTEM 12-DEC-24 9MIC TITLE CRYSTAL STRUCTURE OF THE VRC01-CLASS ANTIBODY 4D01, DERIVED FROM GT1.1 TITLE 2 VACCINATION, IN COMPLEX WITH EOD-GT8 COMPND MOL_ID: 1; COMPND 2 MOLECULE: 4D01 FAB HEAVY CHAIN; COMPND 3 CHAIN: H; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: 4D01 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 HIV-1, GERMLINE-TARGETING VACCINATION, CD4BS MAB, IMMUNE SYSTEM EXPDTA X-RAY DIFFRACTION AUTHOR S.AGRAWAL,I.A.WILSON REVDAT 1 28-MAY-25 9MIC 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. 1.97 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) : 1.97 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 33.90 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340 REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0 REMARK 3 NUMBER OF REFLECTIONS : 60352 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.223 REMARK 3 R VALUE (WORKING SET) : 0.222 REMARK 3 FREE R VALUE : 0.252 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.950 REMARK 3 FREE R VALUE TEST SET COUNT : 2987 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 - 5.4300 1.00 2948 167 0.2138 0.2187 REMARK 3 2 5.4300 - 4.3100 1.00 2808 164 0.1819 0.1992 REMARK 3 3 4.3100 - 3.7700 1.00 2765 165 0.1870 0.2025 REMARK 3 4 3.7700 - 3.4200 1.00 2774 125 0.2044 0.2208 REMARK 3 5 3.4200 - 3.1800 1.00 2768 118 0.2117 0.2811 REMARK 3 6 3.1800 - 2.9900 1.00 2750 118 0.2185 0.2312 REMARK 3 7 2.9900 - 2.8400 1.00 2746 156 0.2218 0.2662 REMARK 3 8 2.8400 - 2.7200 1.00 2718 142 0.2231 0.3008 REMARK 3 9 2.7200 - 2.6100 1.00 2747 133 0.2267 0.2430 REMARK 3 10 2.6100 - 2.5200 1.00 2690 152 0.2250 0.2879 REMARK 3 11 2.5200 - 2.4400 1.00 2727 130 0.2390 0.2834 REMARK 3 12 2.4400 - 2.3700 1.00 2720 140 0.2395 0.2939 REMARK 3 13 2.3700 - 2.3100 1.00 2675 149 0.2445 0.2976 REMARK 3 14 2.3100 - 2.2500 1.00 2706 154 0.2466 0.2974 REMARK 3 15 2.2500 - 2.2000 1.00 2713 149 0.2545 0.2623 REMARK 3 16 2.2000 - 2.1600 1.00 2657 147 0.2632 0.2988 REMARK 3 17 2.1600 - 2.1100 1.00 2677 138 0.2766 0.3341 REMARK 3 18 2.1100 - 2.0700 1.00 2698 144 0.2892 0.3095 REMARK 3 19 2.0700 - 2.0400 1.00 2699 127 0.2904 0.3538 REMARK 3 20 2.0400 - 2.0000 1.00 2709 145 0.3121 0.3258 REMARK 3 21 2.0000 - 1.9700 1.00 2670 124 0.3130 0.3789 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) : 0.270 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.410 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 : 0.009 NULL REMARK 3 ANGLE : 1.012 NULL REMARK 3 CHIRALITY : 0.063 725 REMARK 3 PLANARITY : 0.009 811 REMARK 3 DIHEDRAL : 17.227 1700 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 9MIC COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 16-DEC-24. REMARK 100 THE DEPOSITION ID IS D_1000291033. 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 : 60382 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.970 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 : 12.90 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 5.8000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.97 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.00 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 (%): 60.82 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.14 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 1.2 M SODIUM DIHYDROGEN PHOSPHATE, REMARK 280 0.1M CAPS, 0.8M DI-POTASSIUM HYDROGEN PHOSPHATE, 25% GLYCEROL, REMARK 280 0.2M LITHIUM SULFATE, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE REMARK 280 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 26.71750 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 109.66750 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 35.64550 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 109.66750 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 26.71750 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 35.64550 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 6430 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 25010 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -16.0 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 SER H 215 REMARK 465 CYS H 216 REMARK 465 ASP H 217 REMARK 465 ASP L 1 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 144 64.67 60.32 REMARK 500 SER L 30 -124.87 60.93 REMARK 500 ALA L 51 -23.04 70.47 REMARK 500 TYR L 91 -120.99 44.47 REMARK 500 SER L 156 74.15 43.10 REMARK 500 PRO C 9 170.71 -59.52 REMARK 500 ASN C 32 90.85 69.57 REMARK 500 ASP C 44 -163.44 -117.59 REMARK 500 GLN C 61 -35.12 65.31 REMARK 500 ASP C 79 108.70 -162.15 REMARK 500 ALA C 165 81.70 -158.42 REMARK 500 REMARK 500 REMARK: NULL DBREF 9MIC H 1 217 PDB 9MIC 9MIC 1 217 DBREF 9MIC L 1 212 PDB 9MIC 9MIC 1 212 DBREF 9MIC C 1 183 PDB 9MIC 9MIC 1 183 SEQRES 1 H 224 GLN VAL GLN LEU VAL GLN SER GLY ALA GLU VAL LYS LYS SEQRES 2 H 224 PRO GLY ALA SER VAL LYS VAL SER CYS LYS THR SER GLY SEQRES 3 H 224 TYR THR PHE THR ASP PHE TYR MET HIS TRP MET ARG GLN SEQRES 4 H 224 ALA PRO GLY GLN GLY LEU GLU TRP MET GLY TRP ILE ASN SEQRES 5 H 224 PRO THR GLY GLY GLY VAL ASN TYR ALA HIS LYS PHE GLN SEQRES 6 H 224 GLY ARG VAL THR MET THR ARG ASP THR SER ILE SER THR SEQRES 7 H 224 ALA TYR MET GLU LEU SER ARG LEU THR SER ASP ASP THR SEQRES 8 H 224 GLY VAL TYR TYR CYS ALA ARG SER PRO ALA ARG GLU LEU SEQRES 9 H 224 LEU PRO LEU ASP TYR TRP GLY GLN GLY THR LEU VAL THR SEQRES 10 H 224 VAL SER SER ALA SER THR LYS GLY PRO SER VAL PHE PRO SEQRES 11 H 224 LEU ALA PRO SER SER LYS SER THR SER GLY GLY THR ALA SEQRES 12 H 224 ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU PRO SEQRES 13 H 224 VAL THR VAL SER TRP ASN SER GLY ALA LEU THR SER GLY SEQRES 14 H 224 VAL HIS THR PHE PRO ALA VAL LEU GLN SER SER GLY LEU SEQRES 15 H 224 TYR SER LEU SER SER VAL VAL THR VAL PRO SER SER SER SEQRES 16 H 224 LEU GLY THR GLN THR TYR ILE CYS ASN VAL ASN HIS LYS SEQRES 17 H 224 PRO SER ASN THR LYS VAL ASP LYS ARG VAL GLU PRO LYS SEQRES 18 H 224 SER CYS ASP SEQRES 1 L 208 ASP ILE GLN VAL THR GLN SER PRO SER SER LEU SER ALA SEQRES 2 L 208 SER VAL GLY ASP ARG VAL THR ILE THR CYS ARG ALA SER SEQRES 3 L 208 GLN GLY ILE SER ASN TYR LEU ALA TRP TYR GLN GLN LYS SEQRES 4 L 208 PRO GLY LYS VAL PRO LYS LEU LEU ILE TYR GLY ALA SER SEQRES 5 L 208 THR LEU GLN SER GLY VAL PRO SER ARG PHE SER GLY SER SEQRES 6 L 208 GLY SER GLY THR ASP PHE THR LEU THR ILE SER SER LEU SEQRES 7 L 208 GLN PRO GLU ASP PHE ALA THR TYR TYR CYS GLN ILE TYR SEQRES 8 L 208 GLU THR PHE GLY GLN GLY THR LYS VAL ASP ILE LYS ARG SEQRES 9 L 208 THR VAL ALA ALA PRO SER VAL PHE ILE PHE PRO PRO SER SEQRES 10 L 208 ASP GLU GLN LEU LYS SER GLY THR ALA SER VAL VAL CYS SEQRES 11 L 208 LEU LEU ASN ASN PHE TYR PRO ARG GLU ALA LYS VAL GLN SEQRES 12 L 208 TRP LYS VAL ASP ASN ALA LEU GLN SER GLY ASN SER GLN SEQRES 13 L 208 GLU SER VAL THR GLU GLN ASP SER LYS ASP SER THR TYR SEQRES 14 L 208 SER LEU SER SER THR LEU THR LEU SER LYS ALA ASP TYR SEQRES 15 L 208 GLU LYS HIS LYS VAL TYR ALA CYS GLU VAL THR GLN GLY SEQRES 16 L 208 THR THR SER VAL THR LYS SER PHE ASN ARG GLY GLU 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 *170(H2 O) HELIX 1 AA1 THR H 28 THR H 30 5 3 HELIX 2 AA2 HIS H 61 GLN H 64 5 4 HELIX 3 AA3 THR H 73 ILE H 75 5 3 HELIX 4 AA4 THR H 83 THR H 87 5 5 HELIX 5 AA5 SER H 156 ALA H 158 5 3 HELIX 6 AA6 SER H 187 LEU H 189 5 3 HELIX 7 AA7 LYS H 201 ASN H 204 5 4 HELIX 8 AA8 GLN L 79 PHE L 83 5 5 HELIX 9 AA9 SER L 121 SER L 127 1 7 HELIX 10 AB1 LYS L 183 GLU L 187 1 5 HELIX 11 AB2 GLY L 210 CYS L 212 5 3 HELIX 12 AB3 PRO C 12 SER C 16 5 5 HELIX 13 AB4 ASP C 44 GLN C 52 1 9 HELIX 14 AB5 ARG C 109 GLY C 128 1 20 HELIX 15 AB6 ASP C 141 ASN C 146 1 6 HELIX 16 AB7 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 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 GLY H 88 PRO H 96 -1 N GLY H 88 O VAL H 109 SHEET 4 AA2 6 PHE H 32 GLN H 39 -1 N MET 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 VAL 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 GLY H 88 PRO H 96 -1 N GLY H 88 O VAL H 109 SHEET 4 AA3 4 TYR H 102 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 LEU H 178 N VAL H 142 SHEET 4 AA4 4 VAL H 163 THR H 165 -1 N HIS H 164 O VAL H 181 SHEET 1 AA5 4 THR H 131 SER H 132 0 SHEET 2 AA5 4 THR H 135 TYR H 145 -1 O THR H 135 N SER H 132 SHEET 3 AA5 4 TYR H 176 PRO H 185 -1 O LEU H 178 N VAL H 142 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 199 N THR H 151 SHEET 3 AA6 3 THR H 205 ARG H 210 -1 O VAL H 207 N VAL H 198 SHEET 1 AA7 4 VAL L 4 SER L 7 0 SHEET 2 AA7 4 VAL L 19 ALA L 25 -1 O THR L 22 N SER L 7 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 65 -1 N SER L 63 O THR L 74 SHEET 1 AA8 6 SER L 10 ALA L 13 0 SHEET 2 AA8 6 THR L 102 ILE L 106 1 O ASP L 105 N LEU L 11 SHEET 3 AA8 6 THR L 85 ILE 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 THR L 85 SHEET 5 AA8 6 LYS L 45 TYR L 49 -1 O LYS L 45 N GLN L 37 SHEET 6 AA8 6 THR L 53 LEU L 54 -1 O THR L 53 N TYR L 49 SHEET 1 AA9 4 SER L 10 ALA L 13 0 SHEET 2 AA9 4 THR L 102 ILE L 106 1 O ASP L 105 N LEU L 11 SHEET 3 AA9 4 THR L 85 ILE 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 ILE 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 ASN L 137 N SER L 114 SHEET 3 AB1 4 TYR L 173 SER L 182 -1 O LEU L 179 N VAL L 132 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 GLU L 195 N GLN L 147 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 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 ILE C 133 N PHE C 38 SHEET 6 AB4 6 SER C 166 TRP C 168 -1 O SER C 166 N PHE C 134 SSBOND 1 CYS H 22 CYS H 92 1555 1555 2.07 SSBOND 2 CYS H 140 CYS H 196 1555 1555 2.05 SSBOND 3 CYS L 23 CYS L 88 1555 1555 2.06 SSBOND 4 CYS L 134 CYS L 194 1555 1555 2.03 SSBOND 5 CYS C 7 CYS C 158 1555 1555 2.07 SSBOND 6 CYS C 15 CYS C 151 1555 1555 2.04 SSBOND 7 CYS C 51 CYS C 88 1555 1555 1.99 SSBOND 8 CYS C 99 CYS C 105 1555 1555 2.07 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 -8.07 CISPEP 2 GLU H 148 PRO H 149 0 0.04 CISPEP 3 SER L 7 PRO L 8 0 -10.19 CISPEP 4 TYR L 140 PRO L 141 0 0.42 CISPEP 5 ARG C 8 PRO C 9 0 -12.55 CRYST1 53.435 71.291 219.335 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 0.018714 0.000000 0.000000 0.00000 SCALE2 0.000000 0.014027 0.000000 0.00000 SCALE3 0.000000 0.000000 0.004559 0.00000