HEADER IMMUNE SYSTEM 12-SEP-14 4RBP TITLE CRYSTAL STRUCTURE OF HIV NEUTRALIZING ANTIBODY 2G12 IN COMPLEX WITH A TITLE 2 BACTERIAL OLIGOSACCHARIDE ANALOG OF MAMMALIAN OLIGOMANOSE COMPND MOL_ID: 1; COMPND 2 MOLECULE: FAB 2G12 LIGHT CHAIN; COMPND 3 CHAIN: L, K; COMPND 4 MOL_ID: 2; COMPND 5 MOLECULE: FAB 2G12 HEAVY CHAIN; COMPND 6 CHAIN: H, M SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606; SOURCE 5 MOL_ID: 2; SOURCE 6 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 7 ORGANISM_COMMON: HUMAN; SOURCE 8 ORGANISM_TAXID: 9606 KEYWDS IMMUNOGLOBULIN FOLD, HIV NEUTRALIZING, HIV-1 GP120, IMMUNE SYSTEM EXPDTA X-RAY DIFFRACTION AUTHOR R.L.STANFIELD,I.A.WILSON,C.DE CASTRO,A.M.MARZAIOLI,R.PANTOPHLET REVDAT 1 26-NOV-14 4RBP 0 JRNL AUTH R.L.STANFIELD,C.DE CASTRO,A.M.MARZAIOLI,I.A.WILSON, JRNL AUTH 2 R.PANTOPHLET JRNL TITL CRYSTAL STRUCTURE OF THE HIV NEUTRALIZING ANTIBODY 2G12 IN JRNL TITL 2 COMPLEX WITH A BACTERIAL OLIGOSACCHARIDE ANALOG OF MAMMALIAN JRNL TITL 3 OLIGOMANNOSE. JRNL REF GLYCOBIOLOGY 2014 JRNL REFN ESSN 1460-2423 JRNL PMID 25380763 JRNL DOI 10.1093/GLYCOB/CWU123 REMARK 2 REMARK 2 RESOLUTION. 1.85 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.8.4_1496) REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE- REMARK 3 : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO, REMARK 3 : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL REMARK 3 : MORIARTY,REETAL PAI,RANDY READ,JANE REMARK 3 : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM REMARK 3 : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH, REMARK 3 : LAURENT STORONI,TOM TERWILLIGER,PETER REMARK 3 : ZWART REMARK 3 REMARK 3 REFINEMENT TARGET : ML REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.85 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 43.77 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.000 REMARK 3 COMPLETENESS FOR RANGE (%) : 87.9 REMARK 3 NUMBER OF REFLECTIONS : 76919 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 : 0.252 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 2.600 REMARK 3 FREE R VALUE TEST SET COUNT : 1999 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 43.7865 - 4.4574 0.99 6370 169 0.1697 0.1946 REMARK 3 2 4.4574 - 3.5384 0.98 6041 162 0.1579 0.1834 REMARK 3 3 3.5384 - 3.0913 0.96 5890 157 0.1998 0.2428 REMARK 3 4 3.0913 - 2.8087 0.94 5745 152 0.2230 0.2914 REMARK 3 5 2.8087 - 2.6074 0.93 5678 153 0.2398 0.3151 REMARK 3 6 2.6074 - 2.4537 0.92 5555 147 0.2556 0.2912 REMARK 3 7 2.4537 - 2.3308 0.89 5366 143 0.2553 0.2799 REMARK 3 8 2.3308 - 2.2294 0.86 5181 139 0.2446 0.2714 REMARK 3 9 2.2294 - 2.1436 0.84 5026 134 0.2414 0.3282 REMARK 3 10 2.1436 - 2.0696 0.82 4915 131 0.2408 0.3214 REMARK 3 11 2.0696 - 2.0049 0.81 4886 131 0.2380 0.2743 REMARK 3 12 2.0049 - 1.9476 0.81 4846 130 0.2396 0.3165 REMARK 3 13 1.9476 - 1.8963 0.80 4742 126 0.2496 0.3302 REMARK 3 14 1.8963 - 1.8500 0.78 4679 125 0.2629 0.3309 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) : 0.210 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 27.180 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 : 0.008 6974 REMARK 3 ANGLE : 1.251 9482 REMARK 3 CHIRALITY : 0.080 1111 REMARK 3 PLANARITY : 0.005 1177 REMARK 3 DIHEDRAL : 13.747 2543 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 4RBP COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-SEP-14. REMARK 100 THE RCSB ID CODE IS RCSB087146. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 08-MAR-12 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 5.5 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-D REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.03318 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 300 MM CCD REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO REMARK 200 DATA SCALING SOFTWARE : SCALA REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 77021 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.850 REMARK 200 RESOLUTION RANGE LOW (A) : 45.300 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 88.0 REMARK 200 DATA REDUNDANCY : NULL REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : NULL REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.85 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.90 REMARK 200 COMPLETENESS FOR SHELL (%) : 88.0 REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : 0.57600 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: 1OP5 REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 54.09 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.68 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 33% PEG 600, 0.2M IMIDAZOLE MALATE, PH REMARK 280 5.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 298K 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 22.65000 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 85.05000 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 65.44000 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 85.05000 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 22.65000 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 65.44000 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: TETRAMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 13060 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 39080 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -36.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: K, L, H, M 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 127A REMARK 465 LYS H 127B REMARK 465 SER H 127C REMARK 465 THR H 127D 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 NH1 ARG L 142 O HOH L 434 2.06 REMARK 500 O LYS H 222 O HOH H 498 2.10 REMARK 500 O ALA K 112 O HOH K 496 2.10 REMARK 500 O HOH K 450 O HOH K 509 2.12 REMARK 500 OE2 GLU H 1 O HOH H 505 2.15 REMARK 500 OD1 ASP H 61 NZ LYS H 64 2.18 REMARK 500 OG SER M 134 O1 GOL L 301 2.18 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 GLU L 30 -118.17 47.61 REMARK 500 ALA L 51 -42.85 75.65 REMARK 500 ALA L 84 -177.42 -175.96 REMARK 500 ASN L 152 -2.02 72.60 REMARK 500 PHE H 148 135.50 -172.21 REMARK 500 SER H 163 20.70 49.47 REMARK 500 THR H 200 -66.06 149.97 REMARK 500 GLU K 30 -120.28 50.45 REMARK 500 ALA K 51 -36.21 71.52 REMARK 500 ALA K 84 -179.31 -178.35 REMARK 500 ASP M 76 60.43 63.61 REMARK 500 REMARK 500 REMARK: NULL REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL L 301 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL L 302 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE KDO H 301 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN H 302 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN H 303 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN H 304 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN H 305 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC8 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN H 306 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC9 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL H 307 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL H 308 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL H 309 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL K 301 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL K 302 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL K 303 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE KDO M 301 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN M 302 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC8 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN M 303 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC9 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN M 304 REMARK 800 REMARK 800 SITE_IDENTIFIER: CC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN M 305 REMARK 800 REMARK 800 SITE_IDENTIFIER: CC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN M 306 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1OM3 RELATED DB: PDB REMARK 900 RELATED ID: 1OP3 RELATED DB: PDB REMARK 900 RELATED ID: 1OP5 RELATED DB: PDB REMARK 900 RELATED ID: 1ZLS RELATED DB: PDB REMARK 900 RELATED ID: 1ZLU RELATED DB: PDB REMARK 900 RELATED ID: 1ZLV RELATED DB: PDB REMARK 900 RELATED ID: 1ZLW RELATED DB: PDB REMARK 900 RELATED ID: 2OQJ RELATED DB: PDB REMARK 900 RELATED ID: 3OAU RELATED DB: PDB REMARK 900 RELATED ID: 3OAY RELATED DB: PDB REMARK 900 RELATED ID: 3OAZ RELATED DB: PDB REMARK 900 RELATED ID: 3OB0 RELATED DB: PDB DBREF 4RBP L 1 213 PDB 4RBP 4RBP 1 213 DBREF 4RBP K 1 213 PDB 4RBP 4RBP 1 213 DBREF 4RBP H 1 228 PDB 4RBP 4RBP 1 228 DBREF 4RBP M 1 228 PDB 4RBP 4RBP 1 228 SEQRES 1 L 213 ALA VAL VAL MET THR GLN SER PRO SER THR LEU SER ALA SEQRES 2 L 213 SER VAL GLY ASP THR ILE THR ILE THR CYS ARG ALA SER SEQRES 3 L 213 GLN SER ILE GLU THR TRP LEU ALA TRP TYR GLN GLN LYS SEQRES 4 L 213 PRO GLY LYS ALA PRO LYS LEU LEU ILE TYR LYS ALA SER SEQRES 5 L 213 THR LEU LYS THR GLY VAL PRO SER ARG PHE SER GLY SER SEQRES 6 L 213 GLY SER GLY THR GLU PHE THR LEU THR ILE SER GLY LEU SEQRES 7 L 213 GLN PHE ASP ASP PHE ALA THR TYR HIS CYS GLN HIS TYR SEQRES 8 L 213 ALA GLY TYR SER ALA THR PHE GLY GLN GLY THR ARG VAL SEQRES 9 L 213 GLU ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE ILE SEQRES 10 L 213 PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR ALA SEQRES 11 L 213 SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG GLU SEQRES 12 L 213 ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SER SEQRES 13 L 213 GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER LYS SEQRES 14 L 213 ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SER SEQRES 15 L 213 LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS GLU SEQRES 16 L 213 VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SER SEQRES 17 L 213 PHE ASN ARG GLY GLU SEQRES 1 H 224 GLU VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL LYS SEQRES 2 H 224 ALA GLY GLY SER LEU ILE LEU SER CYS GLY VAL SER ASN SEQRES 3 H 224 PHE ARG ILE SER ALA HIS THR MET ASN TRP VAL ARG ARG SEQRES 4 H 224 VAL PRO GLY GLY GLY LEU GLU TRP VAL ALA SER ILE SER SEQRES 5 H 224 THR SER SER THR TYR ARG ASP TYR ALA ASP ALA VAL LYS SEQRES 6 H 224 GLY ARG PHE THR VAL SER ARG ASP ASP LEU GLU ASP PHE SEQRES 7 H 224 VAL TYR LEU GLN MET HIS LYS MET ARG VAL GLU ASP THR SEQRES 8 H 224 ALA ILE TYR TYR CYS ALA ARG LYS GLY SER ASP ARG LEU SEQRES 9 H 224 SER ASP ASN ASP PRO PHE ASP ALA TRP GLY PRO GLY THR SEQRES 10 H 224 VAL VAL THR VAL SER PRO ALA SER THR LYS GLY PRO SER SEQRES 11 H 224 VAL PHE PRO LEU ALA PRO SER SER LYS SER THR SER GLY SEQRES 12 H 224 GLY THR ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE SEQRES 13 H 224 PRO GLU PRO VAL THR VAL SER TRP ASN SER GLY ALA LEU SEQRES 14 H 224 THR SER GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SER SEQRES 15 H 224 SER GLY LEU TYR SER LEU SER SER VAL VAL THR VAL PRO SEQRES 16 H 224 SER SER SER LEU GLY THR GLN THR TYR ILE CYS ASN VAL SEQRES 17 H 224 ASN HIS LYS PRO SER ASN THR LYS VAL ASP LYS LYS VAL SEQRES 18 H 224 GLU PRO LYS SEQRES 1 K 213 ALA VAL VAL MET THR GLN SER PRO SER THR LEU SER ALA SEQRES 2 K 213 SER VAL GLY ASP THR ILE THR ILE THR CYS ARG ALA SER SEQRES 3 K 213 GLN SER ILE GLU THR TRP LEU ALA TRP TYR GLN GLN LYS SEQRES 4 K 213 PRO GLY LYS ALA PRO LYS LEU LEU ILE TYR LYS ALA SER SEQRES 5 K 213 THR LEU LYS THR GLY VAL PRO SER ARG PHE SER GLY SER SEQRES 6 K 213 GLY SER GLY THR GLU PHE THR LEU THR ILE SER GLY LEU SEQRES 7 K 213 GLN PHE ASP ASP PHE ALA THR TYR HIS CYS GLN HIS TYR SEQRES 8 K 213 ALA GLY TYR SER ALA THR PHE GLY GLN GLY THR ARG VAL SEQRES 9 K 213 GLU ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE ILE SEQRES 10 K 213 PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR ALA SEQRES 11 K 213 SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG GLU SEQRES 12 K 213 ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SER SEQRES 13 K 213 GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER LYS SEQRES 14 K 213 ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SER SEQRES 15 K 213 LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS GLU SEQRES 16 K 213 VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SER SEQRES 17 K 213 PHE ASN ARG GLY GLU SEQRES 1 M 224 GLU VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL LYS SEQRES 2 M 224 ALA GLY GLY SER LEU ILE LEU SER CYS GLY VAL SER ASN SEQRES 3 M 224 PHE ARG ILE SER ALA HIS THR MET ASN TRP VAL ARG ARG SEQRES 4 M 224 VAL PRO GLY GLY GLY LEU GLU TRP VAL ALA SER ILE SER SEQRES 5 M 224 THR SER SER THR TYR ARG ASP TYR ALA ASP ALA VAL LYS SEQRES 6 M 224 GLY ARG PHE THR VAL SER ARG ASP ASP LEU GLU ASP PHE SEQRES 7 M 224 VAL TYR LEU GLN MET HIS LYS MET ARG VAL GLU ASP THR SEQRES 8 M 224 ALA ILE TYR TYR CYS ALA ARG LYS GLY SER ASP ARG LEU SEQRES 9 M 224 SER ASP ASN ASP PRO PHE ASP ALA TRP GLY PRO GLY THR SEQRES 10 M 224 VAL VAL THR VAL SER PRO ALA SER THR LYS GLY PRO SER SEQRES 11 M 224 VAL PHE PRO LEU ALA PRO SER SER LYS SER THR SER GLY SEQRES 12 M 224 GLY THR ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE SEQRES 13 M 224 PRO GLU PRO VAL THR VAL SER TRP ASN SER GLY ALA LEU SEQRES 14 M 224 THR SER GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SER SEQRES 15 M 224 SER GLY LEU TYR SER LEU SER SER VAL VAL THR VAL PRO SEQRES 16 M 224 SER SER SER LEU GLY THR GLN THR TYR ILE CYS ASN VAL SEQRES 17 M 224 ASN HIS LYS PRO SER ASN THR LYS VAL ASP LYS LYS VAL SEQRES 18 M 224 GLU PRO LYS HET GOL L 301 14 HET GOL L 302 14 HET KDO H 301 16 HET MAN H 302 11 HET MAN H 303 11 HET MAN H 304 11 HET MAN H 305 11 HET MAN H 306 11 HET GOL H 307 14 HET GOL H 308 14 HET GOL H 309 14 HET GOL K 301 14 HET GOL K 302 14 HET GOL K 303 14 HET KDO M 301 16 HET MAN M 302 11 HET MAN M 303 11 HET MAN M 304 11 HET MAN M 305 11 HET MAN M 306 11 HETNAM GOL GLYCEROL HETNAM KDO 3-DEOXY-D-MANNO-OCT-2-ULOSONIC ACID HETNAM MAN ALPHA-D-MANNOSE HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL FORMUL 5 GOL 8(C3 H8 O3) FORMUL 7 KDO 2(C8 H14 O8) FORMUL 7 MAN 10(C6 H12 O6) FORMUL 15 HOH *495(H2 O) HELIX 1 1 GLN L 79 PHE L 83 5 5 HELIX 2 2 SER L 121 SER L 127 1 7 HELIX 3 3 LYS L 183 GLU L 187 1 5 HELIX 4 4 THR H 52A THR H 55 5 4 HELIX 5 5 ASP H 61 LYS H 64 5 4 HELIX 6 6 ARG H 83 THR H 87 5 5 HELIX 7 7 SER H 163 ALA H 165 5 3 HELIX 8 8 LYS H 213 ASN H 216 5 4 HELIX 9 9 GLN K 79 PHE K 83 5 5 HELIX 10 10 SER K 121 SER K 127 1 7 HELIX 11 11 LYS K 183 HIS K 189 1 7 HELIX 12 12 ARG M 28 HIS M 32 5 5 HELIX 13 13 THR M 52A THR M 55 5 4 HELIX 14 14 ARG M 83 THR M 87 5 5 HELIX 15 15 SER M 127 LYS M 129 5 3 HELIX 16 16 SER M 163 ALA M 165 5 3 HELIX 17 17 SER M 196 LEU M 198 5 3 HELIX 18 18 LYS M 213 ASN M 216 5 4 SHEET 1 A 4 MET L 4 SER L 7 0 SHEET 2 A 4 THR L 18 ALA L 25 -1 O THR L 22 N SER L 7 SHEET 3 A 4 GLU L 70 SER L 76 -1 O LEU L 73 N ILE L 21 SHEET 4 A 4 PHE L 62 SER L 67 -1 N SER L 63 O THR L 74 SHEET 1 B 6 THR L 10 ALA L 13 0 SHEET 2 B 6 THR L 102 ILE L 106 1 O ARG L 103 N LEU L 11 SHEET 3 B 6 THR L 85 ALA L 92 -1 N TYR L 86 O THR L 102 SHEET 4 B 6 LEU L 33 GLN L 38 -1 N GLN L 38 O THR L 85 SHEET 5 B 6 LYS L 45 TYR L 49 -1 O LYS L 45 N GLN L 37 SHEET 6 B 6 THR L 53 LEU L 54 -1 O THR L 53 N TYR L 49 SHEET 1 C 4 THR L 10 ALA L 13 0 SHEET 2 C 4 THR L 102 ILE L 106 1 O ARG L 103 N LEU L 11 SHEET 3 C 4 THR L 85 ALA L 92 -1 N TYR L 86 O THR L 102 SHEET 4 C 4 SER L 95 PHE L 98 -1 O SER L 95 N ALA L 92 SHEET 1 D 4 SER L 114 PHE L 118 0 SHEET 2 D 4 THR L 129 PHE L 139 -1 O LEU L 135 N PHE L 116 SHEET 3 D 4 TYR L 173 SER L 182 -1 O SER L 177 N CYS L 134 SHEET 4 D 4 SER L 159 VAL L 163 -1 N SER L 162 O SER L 176 SHEET 1 E 4 ALA L 153 LEU L 154 0 SHEET 2 E 4 LYS L 145 VAL L 150 -1 N VAL L 150 O ALA L 153 SHEET 3 E 4 VAL L 191 THR L 197 -1 O GLU L 195 N GLN L 147 SHEET 4 E 4 VAL L 205 ASN L 210 -1 O VAL L 205 N VAL L 196 SHEET 1 F 4 GLN H 3 SER H 7 0 SHEET 2 F 4 LEU H 18 SER H 25 -1 O GLY H 23 N VAL H 5 SHEET 3 F 4 PHE H 77 MET H 82 -1 O LEU H 80 N LEU H 20 SHEET 4 F 4 PHE H 67 ASP H 72 -1 N ASP H 72 O PHE H 77 SHEET 1 G 6 GLY H 10 LYS H 13 0 SHEET 2 G 6 THR H 107 SER H 112 1 O THR H 110 N VAL H 12 SHEET 3 G 6 ALA H 88 LYS H 95 -1 N TYR H 90 O THR H 107 SHEET 4 G 6 MET H 34 ARG H 39 -1 N VAL H 37 O TYR H 91 SHEET 5 G 6 LEU H 45 ILE H 51 -1 O GLU H 46 N ARG H 38 SHEET 6 G 6 ARG H 57 TYR H 59 -1 O ASP H 58 N SER H 50 SHEET 1 H 4 GLY H 10 LYS H 13 0 SHEET 2 H 4 THR H 107 SER H 112 1 O THR H 110 N VAL H 12 SHEET 3 H 4 ALA H 88 LYS H 95 -1 N TYR H 90 O THR H 107 SHEET 4 H 4 PHE H 100F TRP H 103 -1 O ALA H 102 N ARG H 94 SHEET 1 I 4 SER H 120 LEU H 124 0 SHEET 2 I 4 THR H 137 TYR H 147 -1 O GLY H 141 N LEU H 124 SHEET 3 I 4 TYR H 185 PRO H 194 -1 O VAL H 193 N ALA H 138 SHEET 4 I 4 VAL H 171 THR H 173 -1 N HIS H 172 O VAL H 190 SHEET 1 J 4 SER H 120 LEU H 124 0 SHEET 2 J 4 THR H 137 TYR H 147 -1 O GLY H 141 N LEU H 124 SHEET 3 J 4 TYR H 185 PRO H 194 -1 O VAL H 193 N ALA H 138 SHEET 4 J 4 VAL H 177 LEU H 178 -1 N VAL H 177 O SER H 186 SHEET 1 K 3 THR H 153 TRP H 157 0 SHEET 2 K 3 ILE H 207 HIS H 212 -1 O ASN H 209 N SER H 156 SHEET 3 K 3 THR H 217 LYS H 222 -1 O THR H 217 N HIS H 212 SHEET 1 L 4 MET K 4 SER K 7 0 SHEET 2 L 4 THR K 18 ALA K 25 -1 O ARG K 24 N THR K 5 SHEET 3 L 4 GLU K 70 SER K 76 -1 O LEU K 73 N ILE K 21 SHEET 4 L 4 PHE K 62 SER K 67 -1 N SER K 63 O THR K 74 SHEET 1 M 6 THR K 10 ALA K 13 0 SHEET 2 M 6 THR K 102 ILE K 106 1 O ARG K 103 N LEU K 11 SHEET 3 M 6 ALA K 84 TYR K 91 -1 N ALA K 84 O VAL K 104 SHEET 4 M 6 LEU K 33 GLN K 38 -1 N TYR K 36 O HIS K 87 SHEET 5 M 6 LYS K 45 TYR K 49 -1 O LEU K 47 N TRP K 35 SHEET 6 M 6 THR K 53 LEU K 54 -1 O THR K 53 N TYR K 49 SHEET 1 N 4 THR K 10 ALA K 13 0 SHEET 2 N 4 THR K 102 ILE K 106 1 O ARG K 103 N LEU K 11 SHEET 3 N 4 ALA K 84 TYR K 91 -1 N ALA K 84 O VAL K 104 SHEET 4 N 4 ALA K 96 PHE K 98 -1 O THR K 97 N HIS K 90 SHEET 1 O 4 SER K 114 PHE K 118 0 SHEET 2 O 4 THR K 129 PHE K 139 -1 O ASN K 137 N SER K 114 SHEET 3 O 4 TYR K 173 SER K 182 -1 O SER K 177 N CYS K 134 SHEET 4 O 4 SER K 159 VAL K 163 -1 N GLN K 160 O THR K 178 SHEET 1 P 4 ALA K 153 LEU K 154 0 SHEET 2 P 4 LYS K 145 VAL K 150 -1 N VAL K 150 O ALA K 153 SHEET 3 P 4 VAL K 191 THR K 197 -1 O GLU K 195 N GLN K 147 SHEET 4 P 4 VAL K 205 ASN K 210 -1 O VAL K 205 N VAL K 196 SHEET 1 Q 4 GLN M 3 SER M 7 0 SHEET 2 Q 4 LEU M 18 SER M 25 -1 O GLY M 23 N VAL M 5 SHEET 3 Q 4 PHE M 77 MET M 82 -1 O LEU M 80 N LEU M 20 SHEET 4 Q 4 PHE M 67 ASP M 72 -1 N THR M 68 O GLN M 81 SHEET 1 R 6 GLY M 10 LYS M 13 0 SHEET 2 R 6 THR M 107 SER M 112 1 O THR M 110 N VAL M 12 SHEET 3 R 6 ALA M 88 LYS M 95 -1 N TYR M 90 O THR M 107 SHEET 4 R 6 MET M 34 ARG M 39 -1 N VAL M 37 O TYR M 91 SHEET 5 R 6 LEU M 45 ILE M 51 -1 O ALA M 49 N TRP M 36 SHEET 6 R 6 ARG M 57 TYR M 59 -1 O ASP M 58 N SER M 50 SHEET 1 S 4 GLY M 10 LYS M 13 0 SHEET 2 S 4 THR M 107 SER M 112 1 O THR M 110 N VAL M 12 SHEET 3 S 4 ALA M 88 LYS M 95 -1 N TYR M 90 O THR M 107 SHEET 4 S 4 PHE M 100F TRP M 103 -1 O ALA M 102 N ARG M 94 SHEET 1 T 4 SER M 120 LEU M 124 0 SHEET 2 T 4 THR M 137 TYR M 147 -1 O LEU M 143 N PHE M 122 SHEET 3 T 4 TYR M 185 PRO M 194 -1 O LEU M 187 N VAL M 144 SHEET 4 T 4 VAL M 171 THR M 173 -1 N HIS M 172 O VAL M 190 SHEET 1 U 4 THR M 133 SER M 134 0 SHEET 2 U 4 THR M 137 TYR M 147 -1 O THR M 137 N SER M 134 SHEET 3 U 4 TYR M 185 PRO M 194 -1 O LEU M 187 N VAL M 144 SHEET 4 U 4 VAL M 177 LEU M 178 -1 N VAL M 177 O SER M 186 SHEET 1 V 3 THR M 153 TRP M 157 0 SHEET 2 V 3 ILE M 207 HIS M 212 -1 O ASN M 209 N SER M 156 SHEET 3 V 3 THR M 217 LYS M 222 -1 O THR M 217 N HIS M 212 SSBOND 1 CYS L 23 CYS L 88 1555 1555 2.06 SSBOND 2 CYS L 134 CYS L 194 1555 1555 2.04 SSBOND 3 CYS H 22 CYS H 92 1555 1555 2.06 SSBOND 4 CYS H 142 CYS H 208 1555 1555 2.04 SSBOND 5 CYS K 23 CYS K 88 1555 1555 2.07 SSBOND 6 CYS K 134 CYS K 194 1555 1555 2.04 SSBOND 7 CYS M 22 CYS M 92 1555 1555 2.06 SSBOND 8 CYS M 142 CYS M 208 1555 1555 2.05 LINK O2 MAN H 305 C1 MAN H 306 1555 1555 1.43 LINK O5 KDO M 301 C1 MAN M 302 1555 1555 1.44 LINK O3 MAN H 302 C1 MAN H 303 1555 1555 1.44 LINK O2 MAN H 303 C1 MAN H 305 1555 1555 1.44 LINK O5 KDO H 301 C1 MAN H 302 1555 1555 1.44 LINK O3 MAN M 302 C1 MAN M 303 1555 1555 1.44 LINK O2 MAN M 305 C1 MAN M 306 1555 1555 1.44 LINK O2 MAN M 303 C1 MAN M 305 1555 1555 1.44 LINK O6 MAN M 302 C1 MAN M 304 1555 1555 1.45 LINK O6 MAN H 302 C1 MAN H 304 1555 1555 1.45 CISPEP 1 SER L 7 PRO L 8 0 -2.98 CISPEP 2 TYR L 140 PRO L 141 0 7.26 CISPEP 3 PHE H 148 PRO H 149 0 -3.72 CISPEP 4 GLU H 150 PRO H 151 0 3.27 CISPEP 5 SER K 7 PRO K 8 0 -0.36 CISPEP 6 TYR K 140 PRO K 141 0 4.98 CISPEP 7 PHE M 148 PRO M 149 0 -2.70 CISPEP 8 GLU M 150 PRO M 151 0 1.80 SITE 1 AC1 7 SER K 52 HOH K 491 SER L 114 VAL L 115 SITE 2 AC1 7 LYS L 207 HOH L 412 SER M 134 SITE 1 AC2 3 ARG L 24 ARG L 108 LYS L 169 SITE 1 AC3 2 MAN H 302 LYS K 145 SITE 1 AC4 5 ASP H 100B KDO H 301 MAN H 303 MAN H 304 SITE 2 AC4 5 MAN H 305 SITE 1 AC5 7 MAN H 302 MAN H 305 MAN H 306 HOH H 406 SITE 2 AC5 7 HOH H 444 HOH H 473 TYR L 94 SITE 1 AC6 2 ASP H 100B MAN H 302 SITE 1 AC7 8 ALA H 31 LEU H 100 SER H 100A ASP H 100B SITE 2 AC7 8 MAN H 302 MAN H 303 MAN H 306 HOH H 447 SITE 1 AC8 12 ALA H 31 HIS H 32 THR H 33 LYS H 95 SITE 2 AC8 12 GLY H 96 SER H 100A ASP H 100B ASN H 100C SITE 3 AC8 12 ASP H 100D MAN H 303 MAN H 305 GLY L 93 SITE 1 AC9 1 GLU H 85 SITE 1 BC1 5 LEU H 74 GLU H 75 HOH H 508 SER M 54 SITE 2 BC1 5 ARG M 57 SITE 1 BC2 7 HOH H 447 GLU K 143 THR K 197 HIS K 198 SITE 2 BC2 7 GLN K 199 HOH K 478 HOH K 481 SITE 1 BC3 3 GLU K 30 THR K 31 ASN L 152 SITE 1 BC4 10 PHE H 174 PRO H 175 VAL H 177 LEU H 187 SITE 2 BC4 10 SER H 188 GLN K 160 SER K 162 SER K 176 SITE 3 BC4 10 SER K 177 THR K 178 SITE 1 BC5 5 GLN K 37 GLY K 57 PRO K 59 ASP K 81 SITE 2 BC5 5 HOH K 534 SITE 1 BC6 1 MAN M 302 SITE 1 BC7 7 ASP M 100B KDO M 301 MAN M 303 MAN M 304 SITE 2 BC7 7 MAN M 305 HOH M 432 HOH M 450 SITE 1 BC8 5 TYR K 94 MAN M 302 MAN M 305 HOH M 411 SITE 2 BC8 5 HOH M 487 SITE 1 BC9 4 GLU L 213 ASP M 100B MAN M 302 HOH M 497 SITE 1 CC1 8 ALA M 31 SER M 100A ASP M 100B MAN M 302 SITE 2 CC1 8 MAN M 303 MAN M 306 HOH M 451 HOH M 497 SITE 1 CC2 13 GLY K 93 ALA M 31 HIS M 32 THR M 33 SITE 2 CC2 13 LYS M 95 GLY M 96 LEU M 100 SER M 100A SITE 3 CC2 13 ASP M 100B ASN M 100C ASP M 100D MAN M 305 SITE 4 CC2 13 HOH M 411 CRYST1 45.300 130.880 170.100 90.00 90.00 90.00 P 21 21 21 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 0.022075 0.000000 0.000000 0.00000 SCALE2 0.000000 0.007641 0.000000 0.00000 SCALE3 0.000000 0.000000 0.005879 0.00000