HEADER IMMUNE SYSTEM 12-DEC-24 9MID TITLE CRYSTAL STRUCTURE OF THE VRC01-CLASS ANTIBODY 3G08, DERIVED FROM GT1.1 TITLE 2 VACCINATION, IN COMPLEX WITH EOD-GT8 COMPND MOL_ID: 1; COMPND 2 MOLECULE: 3G08 FAB HEAVY CHAIN; COMPND 3 CHAIN: H; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: 3G08 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 GENE: ENV; SOURCE 15 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 16 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 9MID 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. 1.74 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) : 1.74 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 34.70 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340 REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0 REMARK 3 NUMBER OF REFLECTIONS : 58131 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.208 REMARK 3 R VALUE (WORKING SET) : 0.206 REMARK 3 FREE R VALUE : 0.247 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.960 REMARK 3 FREE R VALUE TEST SET COUNT : 2884 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 34.7000 - 4.7900 1.00 2779 140 0.2046 0.2436 REMARK 3 2 4.7900 - 3.8000 1.00 2679 127 0.1752 0.2083 REMARK 3 3 3.8000 - 3.3200 1.00 2659 150 0.1977 0.2284 REMARK 3 4 3.3200 - 3.0200 1.00 2617 152 0.2016 0.2364 REMARK 3 5 3.0200 - 2.8000 1.00 2632 147 0.2040 0.2261 REMARK 3 6 2.8000 - 2.6400 1.00 2618 110 0.2023 0.2540 REMARK 3 7 2.6400 - 2.5100 1.00 2684 139 0.2060 0.2313 REMARK 3 8 2.5100 - 2.4000 1.00 2608 141 0.2017 0.2629 REMARK 3 9 2.4000 - 2.3000 1.00 2599 136 0.2008 0.2710 REMARK 3 10 2.3000 - 2.2300 1.00 2622 133 0.2031 0.2603 REMARK 3 11 2.2300 - 2.1600 1.00 2645 130 0.2005 0.2313 REMARK 3 12 2.1600 - 2.0900 1.00 2613 139 0.2025 0.2678 REMARK 3 13 2.0900 - 2.0400 1.00 2607 140 0.2010 0.2675 REMARK 3 14 2.0400 - 1.9900 1.00 2622 136 0.2027 0.2364 REMARK 3 15 1.9900 - 1.9400 1.00 2602 128 0.2143 0.2568 REMARK 3 16 1.9400 - 1.9000 1.00 2616 137 0.2332 0.2754 REMARK 3 17 1.9000 - 1.8600 1.00 2586 146 0.2417 0.3035 REMARK 3 18 1.8600 - 1.8300 1.00 2639 131 0.2529 0.2982 REMARK 3 19 1.8300 - 1.8000 1.00 2593 149 0.2696 0.3359 REMARK 3 20 1.8000 - 1.7700 1.00 2572 138 0.2773 0.3070 REMARK 3 21 1.7700 - 1.7400 1.00 2655 135 0.2926 0.3342 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) : 0.190 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 23.820 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 : 0.005 NULL REMARK 3 ANGLE : 0.768 NULL REMARK 3 CHIRALITY : 0.054 692 REMARK 3 PLANARITY : 0.007 789 REMARK 3 DIHEDRAL : 14.866 1629 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 9MID 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_1000291043. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 30-OCT-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 EIGER2 X 9M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : AUTOPROC REMARK 200 DATA SCALING SOFTWARE : AIMLESS REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 58145 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.740 REMARK 200 RESOLUTION RANGE LOW (A) : 34.700 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9 REMARK 200 DATA REDUNDANCY : 7.000 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 6.8000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.74 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.77 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 (%): 42.35 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.13 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M AMMONIUM FORMATE, 10% ETHYLENE REMARK 280 GLYCOL, 20% POLYETHYLENE GLYCOL 3350, VAPOR DIFFUSION, SITTING REMARK 280 DROP, TEMPERATURE 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1 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+1/2,Y+1/2,Z 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 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 70.55250 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 22.23700 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 70.55250 REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 22.23700 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: 4230 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 25950 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -12.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 350 APPLY THE FOLLOWING TO CHAINS: H, L REMARK 350 BIOMT1 2 1.000000 0.000000 0.000000 -18.73697 REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 22.23700 REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 -90.14637 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 126 REMARK 465 SER H 127 REMARK 465 LYS H 128 REMARK 465 SER H 129 REMARK 465 THR H 130 REMARK 465 SER H 131 REMARK 465 GLY H 132 REMARK 465 GLY H 133 REMARK 465 THR H 134 REMARK 465 SER H 186 REMARK 465 LYS H 213 REMARK 465 SER H 214 REMARK 465 CYS H 215 REMARK 465 GLN L 1 REMARK 465 SER L 2 REMARK 465 THR L 25A REMARK 465 SER L 25B REMARK 465 SER L 25C REMARK 465 ASP L 25D REMARK 465 VAL L 25E REMARK 465 GLY L 25F REMARK 465 GLY L 25G REMARK 465 TYR L 25H REMARK 465 GLU L 211 REMARK 465 CYS L 212 REMARK 465 SER L 213 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: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT REMARK 500 REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT. REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE REMARK 500 O ASP L 152 O HOH L 301 1.91 REMARK 500 REMARK 500 REMARK: NULL 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 THR H 76 56.65 37.87 REMARK 500 ASP H 97 -166.63 -162.76 REMARK 500 ASP H 143 66.88 62.74 REMARK 500 VAL L 51 -50.03 73.94 REMARK 500 TYR L 91 -126.35 52.77 REMARK 500 SER L 153 -3.23 68.02 REMARK 500 ASN L 171 -4.78 76.64 REMARK 500 GLN C 61 -28.20 70.56 REMARK 500 ASP C 79 110.25 -162.76 REMARK 500 ALA C 129 -178.16 57.87 REMARK 500 LYS C 130 -54.97 -120.98 REMARK 500 ALA C 165 88.68 -156.03 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 H 391 DISTANCE = 6.03 ANGSTROMS REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 9MIC RELATED DB: PDB DBREF 9MID H 1 215 PDB 9MID 9MID 1 215 DBREF 9MID L 1 213 PDB 9MID 9MID 1 213 DBREF 9MID C 1 183 PDB 9MID 9MID 1 183 SEQRES 1 H 223 GLN VAL GLN LEU VAL GLN SER GLY ALA GLU VAL LYS LYS SEQRES 2 H 223 PRO GLY ALA SER VAL LYS VAL SER CYS LYS ALA SER GLY SEQRES 3 H 223 TYR THR PHE THR GLY HIS TYR MET 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 TYR SER SER GLY THR ASN TYR ALA GLN ASN PHE GLN SEQRES 6 H 223 GLY ARG VAL THR MET THR ARG ASP THR SER ILE THR THR SEQRES 7 H 223 ALA TYR MET GLU LEU SER ARG LEU ARG SER ASP ASP THR SEQRES 8 H 223 ALA VAL TYR TYR CYS ALA ARG ALA PRO ASP TYR GLY ASP SEQRES 9 H 223 ARG TRP ASP PHE ASP TYR TRP GLY GLN GLY THR LEU VAL SEQRES 10 H 223 THR VAL PHE ASN GLN ILE 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 211 GLN SER ALA LEU THR GLN PRO PRO SER ALA SER GLY SER SEQRES 2 L 211 PRO GLY GLN SER VAL THR ILE SER CYS THR GLY THR SER SEQRES 3 L 211 SER ASP VAL GLY GLY TYR ASN TYR VAL SER TRP TYR GLN SEQRES 4 L 211 GLN HIS PRO GLY LYS ALA PRO LYS VAL ILE ILE TYR GLU SEQRES 5 L 211 VAL SER LYS ARG PRO SER GLY VAL PRO ASP ARG PHE SER SEQRES 6 L 211 GLY SER LYS SER GLY ASN THR ALA SER LEU THR VAL SER SEQRES 7 L 211 GLY LEU GLN ALA ASP ASP GLU ALA ASP TYR TYR CYS SER SEQRES 8 L 211 SER TYR GLU VAL PHE GLY THR GLY THR LYS VAL THR VAL SEQRES 9 L 211 LEU GLY GLN PRO LYS ALA ALA PRO SER VAL THR LEU PHE SEQRES 10 L 211 PRO PRO SER SER GLU GLU LEU GLN ALA ASN LYS ALA THR SEQRES 11 L 211 LEU VAL CYS LEU ILE SER ASP PHE TYR PRO GLY ALA VAL SEQRES 12 L 211 THR VAL ALA TRP LYS ALA ASP SER SER PRO VAL LYS ALA SEQRES 13 L 211 GLY VAL GLU THR THR THR PRO SER LYS GLN SER ASN ASN SEQRES 14 L 211 LYS TYR ALA ALA SER SER TYR LEU SER LEU THR PRO GLU SEQRES 15 L 211 GLN TRP LYS SER HIS ARG SER TYR SER CYS GLN VAL THR SEQRES 16 L 211 HIS GLU GLY SER THR VAL GLU LYS THR VAL ALA PRO THR SEQRES 17 L 211 GLU CYS SER 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 *244(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 THR H 73 ILE H 75 5 3 HELIX 4 AA4 ARG H 83 THR H 87 5 5 HELIX 5 AA5 SER H 155 ALA H 157 5 3 HELIX 6 AA6 LYS H 200 ASN H 203 5 4 HELIX 7 AA7 GLN L 79 GLU L 83 5 5 HELIX 8 AA8 SER L 122 ALA L 128 1 7 HELIX 9 AA9 THR L 182 HIS L 189 1 8 HELIX 10 AB1 PRO C 12 SER C 16 5 5 HELIX 11 AB2 ASP C 44 GLN C 52 1 9 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 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 LEU H 108 N GLU H 10 SHEET 3 AA2 6 ALA H 88 ARG H 94 -1 N ALA H 88 O VAL H 109 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 THR H 57 TYR H 59 -1 O ASN H 58 N TRP H 50 SHEET 1 AA3 4 SER H 119 LEU H 123 0 SHEET 2 AA3 4 ALA H 136 TYR H 144 -1 O LYS H 142 N SER H 119 SHEET 3 AA3 4 TYR H 175 THR H 182 -1 O TYR H 175 N TYR H 144 SHEET 4 AA3 4 VAL H 162 THR H 164 -1 N HIS H 163 O VAL H 180 SHEET 1 AA4 4 SER H 119 LEU H 123 0 SHEET 2 AA4 4 ALA H 136 TYR H 144 -1 O LYS H 142 N SER H 119 SHEET 3 AA4 4 TYR H 175 THR H 182 -1 O TYR H 175 N TYR H 144 SHEET 4 AA4 4 VAL H 168 LEU H 169 -1 N VAL H 168 O SER H 176 SHEET 1 AA5 3 THR H 150 TRP H 153 0 SHEET 2 AA5 3 ILE H 194 HIS H 199 -1 O ASN H 196 N SER H 152 SHEET 3 AA5 3 THR H 204 LYS H 209 -1 O THR H 204 N HIS H 199 SHEET 1 AA6 5 SER L 9 GLY L 13 0 SHEET 2 AA6 5 THR L 102 VAL L 106 1 O THR L 105 N ALA L 11 SHEET 3 AA6 5 ALA L 84 SER L 90 -1 N ALA L 84 O VAL L 104 SHEET 4 AA6 5 SER L 34 GLN L 38 -1 N TYR L 36 O TYR L 87 SHEET 5 AA6 5 LYS L 45 ILE L 48 -1 O LYS L 45 N GLN L 37 SHEET 1 AA7 4 SER L 9 GLY L 13 0 SHEET 2 AA7 4 THR L 102 VAL L 106 1 O THR L 105 N ALA L 11 SHEET 3 AA7 4 ALA L 84 SER L 90 -1 N ALA L 84 O VAL L 104 SHEET 4 AA7 4 VAL L 97 PHE L 98 -1 O VAL L 97 N SER L 90 SHEET 1 AA8 3 VAL L 19 THR L 24 0 SHEET 2 AA8 3 THR L 70 VAL L 75 -1 O LEU L 73 N ILE L 21 SHEET 3 AA8 3 PHE L 62 SER L 67 -1 N SER L 67 O THR L 70 SHEET 1 AA9 4 SER L 115 PHE L 119 0 SHEET 2 AA9 4 ALA L 131 PHE L 140 -1 O LEU L 136 N THR L 117 SHEET 3 AA9 4 TYR L 173 LEU L 181 -1 O SER L 177 N CYS L 135 SHEET 4 AA9 4 VAL L 160 THR L 162 -1 N GLU L 161 O TYR L 178 SHEET 1 AB1 4 SER L 115 PHE L 119 0 SHEET 2 AB1 4 ALA L 131 PHE L 140 -1 O LEU L 136 N THR L 117 SHEET 3 AB1 4 TYR L 173 LEU L 181 -1 O SER L 177 N CYS L 135 SHEET 4 AB1 4 SER L 166 LYS L 167 -1 N SER L 166 O ALA L 174 SHEET 1 AB2 4 SER L 154 PRO L 155 0 SHEET 2 AB2 4 THR L 146 ALA L 151 -1 N ALA L 151 O SER L 154 SHEET 3 AB2 4 TYR L 192 HIS L 198 -1 O GLN L 195 N ALA L 148 SHEET 4 AB2 4 SER L 201 VAL L 207 -1 O SER L 201 N HIS L 198 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 ILE C 97 N SER C 17 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 LEU C 5 O CYS C 105 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 PHE C 149 O PHE C 156 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 SER C 17 O ILE C 97 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 TRP C 168 N ILE C 132 SSBOND 1 CYS H 22 CYS H 92 1555 1555 2.04 SSBOND 2 CYS H 139 CYS H 195 1555 1555 2.03 SSBOND 3 CYS L 23 CYS L 88 1555 1555 2.05 SSBOND 4 CYS L 135 CYS L 194 1555 1555 2.04 SSBOND 5 CYS C 7 CYS C 158 1555 1555 2.04 SSBOND 6 CYS C 15 CYS C 151 1555 1555 2.02 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 145 PRO H 146 0 -1.92 CISPEP 2 GLU H 147 PRO H 148 0 -2.30 CISPEP 3 TYR L 141 PRO L 142 0 2.96 CISPEP 4 ARG C 8 PRO C 9 0 -7.07 CRYST1 141.105 44.474 103.977 90.00 119.89 90.00 C 1 2 1 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 0.007087 0.000000 0.004074 0.00000 SCALE2 0.000000 0.022485 0.000000 0.00000 SCALE3 0.000000 0.000000 0.011094 0.00000