HEADER IMMUNE SYSTEM 22-FEB-18 6CH8 TITLE CRYSTAL STRUCTURE OF A NATIVELY-GLYCOSYLATED BG505 SOSIP.664 HIV-1 TITLE 2 ENVELOPE TRIMER IN COMPLEX WITH THE BROADLY-NEUTRALIZING ANTIBODIES TITLE 3 BG18 AND 35O22 COMPND MOL_ID: 1; COMPND 2 MOLECULE: ENVELOPE GLYCOPROTEIN GP41; COMPND 3 CHAIN: B; COMPND 4 SYNONYM: ENV POLYPROTEIN; COMPND 5 ENGINEERED: YES; COMPND 6 MOL_ID: 2; COMPND 7 MOLECULE: 35O22 HEAVY CHAIN; COMPND 8 CHAIN: D; COMPND 9 ENGINEERED: YES; COMPND 10 MOL_ID: 3; COMPND 11 MOLECULE: 35O22 LIGHT CHAIN; COMPND 12 CHAIN: E; COMPND 13 ENGINEERED: YES; COMPND 14 MOL_ID: 4; COMPND 15 MOLECULE: ENVELOPE GLYCOPROTEIN GP120; COMPND 16 CHAIN: G; COMPND 17 SYNONYM: ENV POLYPROTEIN; COMPND 18 ENGINEERED: YES; COMPND 19 MOL_ID: 5; COMPND 20 MOLECULE: BG18 HEAVY CHAIN; COMPND 21 CHAIN: Q; COMPND 22 ENGINEERED: YES; COMPND 23 MOL_ID: 6; COMPND 24 MOLECULE: BG18 LIGHT CHAIN; COMPND 25 CHAIN: R; COMPND 26 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HUMAN IMMUNODEFICIENCY VIRUS 1; SOURCE 3 ORGANISM_TAXID: 11676; SOURCE 4 GENE: ENV; SOURCE 5 EXPRESSION_SYSTEM: CRICETULUS GRISEUS; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 10029; SOURCE 7 EXPRESSION_SYSTEM_CELL_LINE: K1; SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: FLP-IN PLASMID; SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PAM/C; SOURCE 10 MOL_ID: 2; SOURCE 11 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 12 ORGANISM_COMMON: HUMAN; SOURCE 13 ORGANISM_TAXID: 9606; SOURCE 14 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 15 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 16 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 17 EXPRESSION_SYSTEM_CELL_LINE: HEK293-6E; SOURCE 18 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 19 EXPRESSION_SYSTEM_PLASMID: PTT5; SOURCE 20 MOL_ID: 3; SOURCE 21 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 22 ORGANISM_COMMON: HUMAN; SOURCE 23 ORGANISM_TAXID: 9606; SOURCE 24 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 25 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 26 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 27 EXPRESSION_SYSTEM_CELL_LINE: HEK293-6E; SOURCE 28 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 29 EXPRESSION_SYSTEM_PLASMID: PTT5; SOURCE 30 MOL_ID: 4; SOURCE 31 ORGANISM_SCIENTIFIC: HUMAN IMMUNODEFICIENCY VIRUS 1; SOURCE 32 ORGANISM_TAXID: 11676; SOURCE 33 GENE: ENV; SOURCE 34 EXPRESSION_SYSTEM: CRICETULUS GRISEUS; SOURCE 35 EXPRESSION_SYSTEM_TAXID: 10029; SOURCE 36 EXPRESSION_SYSTEM_CELL_LINE: K1; SOURCE 37 EXPRESSION_SYSTEM_VECTOR_TYPE: FLP-IN PLASMID; SOURCE 38 EXPRESSION_SYSTEM_PLASMID: PAM/C; SOURCE 39 MOL_ID: 5; SOURCE 40 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 41 ORGANISM_COMMON: HUMAN; SOURCE 42 ORGANISM_TAXID: 9606; SOURCE 43 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 44 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 45 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 46 MOL_ID: 6; SOURCE 47 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 48 ORGANISM_COMMON: HUMAN; SOURCE 49 ORGANISM_TAXID: 9606; SOURCE 50 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 51 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 52 EXPRESSION_SYSTEM_TAXID: 9606 KEYWDS ENV GLYCOPROTEIN, BROADLY NEUTRALIZING ANTIBODIES, IMMUNE SYSTEM EXPDTA X-RAY DIFFRACTION AUTHOR C.O.BARNES,P.J.BJORKMAN REVDAT 1 02-MAY-18 6CH8 0 JRNL AUTH C.O.BARNES,H.B.GRISTICK,N.T.FREUND,A.ESCOLANO,A.Y.LYUBIMOV, JRNL AUTH 2 H.HARTWEGER,A.P.WEST,A.E.COHEN,M.C.NUSSENZWEIG,P.J.BJORKMAN JRNL TITL STRUCTURAL CHARACTERIZATION OF A HIGHLY-POTENT V3-GLYCAN JRNL TITL 2 BROADLY NEUTRALIZING ANTIBODY BOUND TO NATIVELY-GLYCOSYLATED JRNL TITL 3 HIV-1 ENVELOPE. JRNL REF NAT COMMUN V. 9 1251 2018 JRNL REFN ESSN 2041-1723 JRNL PMID 29593217 JRNL DOI 10.1038/S41467-018-03632-Y REMARK 2 REMARK 2 RESOLUTION. 4.10 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : BUSTER 2.10.2 REMARK 3 AUTHORS : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER, REMARK 3 : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN, REMARK 3 : WOMACK,MATTHEWS,TEN EYCK,TRONRUD REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 4.10 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 39.51 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000 REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8 REMARK 3 NUMBER OF REFLECTIONS : 30803 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM REMARK 3 R VALUE (WORKING + TEST SET) : 0.231 REMARK 3 R VALUE (WORKING SET) : 0.229 REMARK 3 FREE R VALUE : 0.274 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.040 REMARK 3 FREE R VALUE TEST SET COUNT : 1551 REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.000 REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : 15 REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 4.10 REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 4.24 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.73 REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 2997 REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2540 REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2841 REMARK 3 BIN R VALUE (WORKING SET) : 0.2520 REMARK 3 BIN FREE R VALUE : 0.2880 REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.21 REMARK 3 BIN FREE R VALUE TEST SET COUNT : 156 REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.000 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 11183 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 1142 REMARK 3 SOLVENT ATOMS : 0 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 141.7 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 229.7 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : -18.49900 REMARK 3 B22 (A**2) : -18.49900 REMARK 3 B33 (A**2) : 36.99790 REMARK 3 B12 (A**2) : 0.00000 REMARK 3 B13 (A**2) : 0.00000 REMARK 3 B23 (A**2) : 0.00000 REMARK 3 REMARK 3 ESTIMATED COORDINATE ERROR. REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.660 REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : NULL REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.688 REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : NULL REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : NULL REMARK 3 REMARK 3 REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797 REMARK 3 CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.924 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.899 REMARK 3 REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15 REMARK 3 TERM COUNT WEIGHT FUNCTION. REMARK 3 BOND LENGTHS : 12683 ; 2.000 ; HARMONIC REMARK 3 BOND ANGLES : 17434 ; 2.000 ; HARMONIC REMARK 3 TORSION ANGLES : 4435 ; 2.000 ; SINUSOIDAL REMARK 3 TRIGONAL CARBON PLANES : 238 ; 2.000 ; HARMONIC REMARK 3 GENERAL PLANES : 1744 ; 5.000 ; HARMONIC REMARK 3 ISOTROPIC THERMAL FACTORS : 12683 ; 20.000 ; HARMONIC REMARK 3 BAD NON-BONDED CONTACTS : NULL ; NULL ; NULL REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL REMARK 3 CHIRAL IMPROPER TORSION : 2032 ; 5.000 ; SEMIHARMONIC REMARK 3 SUM OF OCCUPANCIES : NULL ; NULL ; NULL REMARK 3 UTILITY DISTANCES : NULL ; NULL ; NULL REMARK 3 UTILITY ANGLES : NULL ; NULL ; NULL REMARK 3 UTILITY TORSION : NULL ; NULL ; NULL REMARK 3 IDEAL-DIST CONTACT TERM : 13552 ; 4.000 ; SEMIHARMONIC REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. REMARK 3 BOND LENGTHS (A) : 0.008 REMARK 3 BOND ANGLES (DEGREES) : 1.16 REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 2.04 REMARK 3 OTHER TORSION ANGLES (DEGREES) : 20.00 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 6CH8 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 26-FEB-18. REMARK 100 THE DEPOSITION ID IS D_1000232700. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 26-APR-17 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 8.0 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : SSRL REMARK 200 BEAMLINE : BL12-2 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.0 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : AIMLESS 0.5.31 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 30846 REMARK 200 RESOLUTION RANGE HIGH (A) : 4.100 REMARK 200 RESOLUTION RANGE LOW (A) : 39.550 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9 REMARK 200 DATA REDUNDANCY : 14.90 REMARK 200 R MERGE (I) : 0.29500 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 8.7000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 4.10 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 4.32 REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0 REMARK 200 DATA REDUNDANCY IN SHELL : 15.30 REMARK 200 R MERGE FOR SHELL (I) : 4.34600 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: 5T3Z, 5UD9, 4TOY REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 78.69 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 5.77 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 5% TACISMATE PH 8.0, 15% PEG 3350, REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: H 3 2 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -Y,X-Y,Z REMARK 290 3555 -X+Y,-X,Z REMARK 290 4555 Y,X,-Z REMARK 290 5555 X-Y,-Y,-Z REMARK 290 6555 -X,-X+Y,-Z REMARK 290 7555 X+2/3,Y+1/3,Z+1/3 REMARK 290 8555 -Y+2/3,X-Y+1/3,Z+1/3 REMARK 290 9555 -X+Y+2/3,-X+1/3,Z+1/3 REMARK 290 10555 Y+2/3,X+1/3,-Z+1/3 REMARK 290 11555 X-Y+2/3,-Y+1/3,-Z+1/3 REMARK 290 12555 -X+2/3,-X+Y+1/3,-Z+1/3 REMARK 290 13555 X+1/3,Y+2/3,Z+2/3 REMARK 290 14555 -Y+1/3,X-Y+2/3,Z+2/3 REMARK 290 15555 -X+Y+1/3,-X+2/3,Z+2/3 REMARK 290 16555 Y+1/3,X+2/3,-Z+2/3 REMARK 290 17555 X-Y+1/3,-Y+2/3,-Z+2/3 REMARK 290 18555 -X+1/3,-X+Y+2/3,-Z+2/3 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 -0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 4 0.866025 0.500000 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 0.00000 REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000 REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 7 1.000000 0.000000 0.000000 119.61150 REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 69.05773 REMARK 290 SMTRY3 7 0.000000 0.000000 1.000000 118.42200 REMARK 290 SMTRY1 8 -0.500000 -0.866025 0.000000 119.61150 REMARK 290 SMTRY2 8 0.866025 -0.500000 0.000000 69.05773 REMARK 290 SMTRY3 8 0.000000 0.000000 1.000000 118.42200 REMARK 290 SMTRY1 9 -0.500000 0.866025 0.000000 119.61150 REMARK 290 SMTRY2 9 -0.866025 -0.500000 0.000000 69.05773 REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 118.42200 REMARK 290 SMTRY1 10 -0.500000 0.866025 0.000000 119.61150 REMARK 290 SMTRY2 10 0.866025 0.500000 0.000000 69.05773 REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 118.42200 REMARK 290 SMTRY1 11 1.000000 0.000000 0.000000 119.61150 REMARK 290 SMTRY2 11 0.000000 -1.000000 0.000000 69.05773 REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 118.42200 REMARK 290 SMTRY1 12 -0.500000 -0.866025 0.000000 119.61150 REMARK 290 SMTRY2 12 -0.866025 0.500000 0.000000 69.05773 REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 118.42200 REMARK 290 SMTRY1 13 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 13 0.000000 1.000000 0.000000 138.11546 REMARK 290 SMTRY3 13 0.000000 0.000000 1.000000 236.84400 REMARK 290 SMTRY1 14 -0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 14 0.866025 -0.500000 0.000000 138.11546 REMARK 290 SMTRY3 14 0.000000 0.000000 1.000000 236.84400 REMARK 290 SMTRY1 15 -0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 15 -0.866025 -0.500000 0.000000 138.11546 REMARK 290 SMTRY3 15 0.000000 0.000000 1.000000 236.84400 REMARK 290 SMTRY1 16 -0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 16 0.866025 0.500000 0.000000 138.11546 REMARK 290 SMTRY3 16 0.000000 0.000000 -1.000000 236.84400 REMARK 290 SMTRY1 17 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 17 0.000000 -1.000000 0.000000 138.11546 REMARK 290 SMTRY3 17 0.000000 0.000000 -1.000000 236.84400 REMARK 290 SMTRY1 18 -0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 18 -0.866025 0.500000 0.000000 138.11546 REMARK 290 SMTRY3 18 0.000000 0.000000 -1.000000 236.84400 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: OCTADECAMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, D, E, G, Q, R 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: B, D, E, G, Q, R REMARK 350 BIOMT1 2 -0.500000 -0.866025 0.000000 119.61150 REMARK 350 BIOMT2 2 0.866025 -0.500000 0.000000 -207.17320 REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000 REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, D, E, G, Q, R REMARK 350 BIOMT1 3 -0.500000 0.866025 0.000000 239.22300 REMARK 350 BIOMT2 3 -0.866025 -0.500000 0.000000 0.00000 REMARK 350 BIOMT3 3 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 ALA B 512 REMARK 465 VAL B 513 REMARK 465 GLY B 514 REMARK 465 ILE B 515 REMARK 465 GLY B 516 REMARK 465 ALA B 517 REMARK 465 VAL B 518 REMARK 465 PHE B 519 REMARK 465 ALA B 558 REMARK 465 ILE B 559 REMARK 465 GLU B 560 REMARK 465 ALA B 561 REMARK 465 GLN B 562 REMARK 465 GLN B 563 REMARK 465 LYS D 218 REMARK 465 GLY D 219 REMARK 465 LEU D 220 REMARK 465 GLU D 221 REMARK 465 VAL D 222 REMARK 465 LEU D 223 REMARK 465 PHE D 224 REMARK 465 GLN D 225 REMARK 465 GLN E 1 REMARK 465 PRO E 212 REMARK 465 THR E 213 REMARK 465 GLU E 214 REMARK 465 CYS E 215 REMARK 465 SER E 216 REMARK 465 ALA G 31 REMARK 465 THR G 147 REMARK 465 ASP G 148 REMARK 465 ASP G 149 REMARK 465 MET G 150 REMARK 465 GLU G 185A REMARK 465 ASN G 185B REMARK 465 GLN G 185C REMARK 465 GLY G 185D REMARK 465 ASN G 185E REMARK 465 ARG G 185F REMARK 465 SER G 185G REMARK 465 ASN G 185H REMARK 465 ASN G 185I REMARK 465 THR G 400 REMARK 465 SER G 401 REMARK 465 VAL G 402 REMARK 465 GLN G 403 REMARK 465 GLY G 404 REMARK 465 SER G 405 REMARK 465 ASN G 406 REMARK 465 SER G 407 REMARK 465 THR G 408 REMARK 465 GLY G 409 REMARK 465 ARG G 508 REMARK 465 GLU G 509 REMARK 465 LYS G 510 REMARK 465 ARG G 511 REMARK 465 GLN Q 1 REMARK 465 PRO Q 230 REMARK 465 LYS Q 231 REMARK 465 SER Q 232 REMARK 465 CYS Q 233 REMARK 465 ASP Q 234 REMARK 465 LYS Q 235 REMARK 465 HIS Q 236 REMARK 465 HIS Q 237 REMARK 465 HIS Q 238 REMARK 465 HIS Q 239 REMARK 465 HIS Q 240 REMARK 465 HIS Q 241 REMARK 465 TRP R 1 REMARK 465 ALA R 2 REMARK 465 SER R 3 REMARK 465 SER R 4 REMARK 470 REMARK 470 MISSING ATOM REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 470 I=INSERTION CODE): REMARK 470 M RES CSSEQI ATOMS REMARK 470 GLN D 6 CG CD OE1 NE2 REMARK 470 TRP D 100D CG CD1 CD2 NE1 CE2 CE3 CZ2 REMARK 470 TRP D 100D CZ3 CH2 REMARK 470 ASP D 144 CG OD1 OD2 REMARK 470 GLU D 148 CG CD OE1 OE2 REMARK 470 LEU D 175 CG CD1 CD2 REMARK 470 ARG G 151 CG CD NE CZ NH1 NH2 REMARK 470 ILE G 215 CG1 CG2 CD1 REMARK 470 LYS Q 13 CG CD CE NZ REMARK 470 ARG Q 67 CG CD NE CZ NH1 NH2 REMARK 470 GLN Q 122 CG CD OE1 NE2 REMARK 470 LEU Q 141 CG CD1 CD2 REMARK 470 LEU Q 158 CG CD1 CD2 REMARK 470 THR Q 208 OG1 CG2 REMARK 470 ASN Q 214 CG OD1 ND2 REMARK 470 VAL Q 215 CG1 CG2 REMARK 470 ASN Q 216 CG OD1 ND2 REMARK 470 HIS Q 217 CG ND1 CD2 CE1 NE2 REMARK 470 ASN Q 221 CG OD1 ND2 REMARK 470 THR Q 222 OG1 CG2 REMARK 470 LYS Q 223 CG CD CE NZ REMARK 470 VAL Q 224 CG1 CG2 REMARK 470 GLU R 5 CG CD OE1 OE2 REMARK 470 GLN R 8 CG CD OE1 NE2 REMARK 470 GLN R 18 CG CD OE1 NE2 REMARK 470 ARG R 32 CG CD NE CZ NH1 NH2 REMARK 470 SER R 66 OG REMARK 470 TRP R 67 CG CD1 CD2 NE1 CE2 CE3 CZ2 REMARK 470 TRP R 67 CZ3 CH2 REMARK 470 THR R 71 OG1 CG2 REMARK 470 ARG R 77 CG CD NE CZ NH1 NH2 REMARK 470 GLN R 80 CG CD OE1 NE2 REMARK 470 LYS R 106 CG CD CE NZ REMARK 470 LEU R 110 CG CD1 CD2 REMARK 470 GLN R 112 CG CD OE1 NE2 REMARK 470 GLU R 127 CG CD OE1 OE2 REMARK 470 LYS R 160 CG CD CE NZ REMARK 470 GLU R 187 CG CD OE1 OE2 REMARK 470 LYS R 193 CG CD CE NZ REMARK 470 THR R 213 OG1 CG2 REMARK 470 GLU R 214 CG CD OE1 OE2 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 ND2 ASN G 276 C1 NAG G 640 1.15 REMARK 500 OD2 ASP B 624 OD1 ASP D 99 1.53 REMARK 500 OD1 ASN B 618 C1 NAG B 702 1.70 REMARK 500 CG ASN B 618 C1 NAG B 702 1.70 REMARK 500 CE1 HIS Q 33 O6 MAN Q 309 1.73 REMARK 500 ND2 ASN G 386 C1 NAG G 659 1.75 REMARK 500 O SER G 364 OG SER G 365 1.76 REMARK 500 CB GLN Q 188 OE1 GLU R 164 1.78 REMARK 500 O MET B 626 CG2 THR B 627 1.79 REMARK 500 CB GLN Q 188 CD GLU R 164 1.81 REMARK 500 OD1 ASN B 625 OH TYR D 32 1.81 REMARK 500 ND2 ASN B 618 O5 NAG B 702 1.82 REMARK 500 ND2 ASN G 386 N2 NAG G 659 1.86 REMARK 500 ND2 ASN G 276 O5 NAG G 640 1.90 REMARK 500 O ILE G 358 OG1 THR G 465 1.92 REMARK 500 ND2 ASN G 295 O5 NAG G 648 2.01 REMARK 500 OE1 GLU G 64 O2 MAN G 638 2.06 REMARK 500 OE1 GLU G 64 C3 MAN G 638 2.07 REMARK 500 ND2 ASN G 386 C2 NAG G 659 2.09 REMARK 500 O ASP B 624 CG ARG D 98 2.13 REMARK 500 OD1 ASN B 554 NZ LYS B 567 2.19 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS REMARK 500 REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15 REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375 REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS. REMARK 500 REMARK 500 DISTANCE CUTOFF: REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE REMARK 500 O MET B 535 NE2 GLN B 652 2545 2.11 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND ANGLES REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1) REMARK 500 REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999 REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996 REMARK 500 REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3 REMARK 500 THR B 627 N - CA - C ANGL. DEV. = 17.8 DEGREES REMARK 500 PRO G 220 C - N - CA ANGL. DEV. = 19.9 DEGREES REMARK 500 PRO G 220 C - N - CD ANGL. DEV. = -18.8 DEGREES REMARK 500 PRO G 313 C - N - CA ANGL. DEV. = 9.5 DEGREES REMARK 500 THR G 464 N - CA - C ANGL. DEV. = 16.5 DEGREES 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 B 536 -93.51 -92.05 REMARK 500 LEU B 537 -37.94 80.98 REMARK 500 SER B 553 -126.06 49.71 REMARK 500 ASN B 554 138.18 0.01 REMARK 500 LEU B 556 -131.62 52.08 REMARK 500 THR B 627 -0.64 81.52 REMARK 500 TRP B 628 -51.33 75.61 REMARK 500 GLU B 657 -5.66 -58.48 REMARK 500 GLN D 3 99.67 -62.32 REMARK 500 ALA D 9 -0.65 78.00 REMARK 500 SER D 17 153.87 91.28 REMARK 500 ARG D 28 96.29 -62.56 REMARK 500 ARG D 43 -165.41 58.25 REMARK 500 SER D 54 -54.99 62.17 REMARK 500 ASN D 82B 115.90 65.05 REMARK 500 ARG D 98 56.89 -105.07 REMARK 500 SER D 100B 116.05 -162.05 REMARK 500 THR D 100C -33.19 -138.82 REMARK 500 TYR D 101 -69.03 -131.54 REMARK 500 VAL D 111 59.21 -104.82 REMARK 500 ASP D 144 85.29 58.70 REMARK 500 PHE D 146 142.78 -178.89 REMARK 500 GLU D 148 149.40 64.91 REMARK 500 ALA D 158 -54.11 62.89 REMARK 500 THR D 183 75.72 -109.70 REMARK 500 SER D 187 -123.71 58.63 REMARK 500 HIS D 200 -159.34 -141.53 REMARK 500 LYS D 201 -125.66 -100.42 REMARK 500 ASN D 204 -160.56 55.64 REMARK 500 LYS D 206 -35.15 -151.77 REMARK 500 ALA E 8 -125.53 55.98 REMARK 500 GLN E 16 -167.33 -122.00 REMARK 500 ASP E 53 -97.48 57.21 REMARK 500 SER E 65 -125.47 -135.46 REMARK 500 SER E 69 -162.96 -111.23 REMARK 500 ASP E 79 72.43 50.72 REMARK 500 GLU E 85 88.86 -67.72 REMARK 500 THR E 86 -166.29 -162.51 REMARK 500 TYR E 89 -169.71 -128.37 REMARK 500 ASP E 142 72.38 50.53 REMARK 500 ASN E 173 22.36 -76.40 REMARK 500 GLU E 202 105.11 -59.58 REMARK 500 ASP G 57 -144.72 -87.64 REMARK 500 LYS G 59 -100.81 -124.08 REMARK 500 TYR G 61 -137.65 60.11 REMARK 500 LYS G 65 -141.73 -119.86 REMARK 500 THR G 71 -159.11 53.81 REMARK 500 ASN G 88 -3.56 64.68 REMARK 500 LEU G 122 43.15 -106.94 REMARK 500 ASN G 133 -176.34 -65.95 REMARK 500 REMARK 500 THIS ENTRY HAS 145 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 610 REMARK 610 MISSING HETEROATOM REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 610 I=INSERTION CODE): REMARK 610 M RES C SSEQI REMARK 610 NAG G 640 REMARK 610 NAG G 659 REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 701 bound REMARK 800 to ASN B 611 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG B REMARK 800 702 through BMA B 704 bound to ASN B 618 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG B REMARK 800 705 through MAN B 709 bound to ASN B 637 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG G REMARK 800 601 through MAN G 607 bound to ASN G 88 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG G REMARK 800 608 through MAN G 612 bound to ASN G 133 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG G REMARK 800 613 through MAN G 619 bound to ASN G 156 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG G REMARK 800 620 through MAN G 624 bound to ASN G 160 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC8 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG G REMARK 800 625 through MAN G 628 bound to ASN G 197 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC9 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG G REMARK 800 629 through MAN G 632 bound to ASN G 234 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues GLU G REMARK 800 64 through MAN G 639 bound to ASN G 262 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG G REMARK 800 648 through BMA G 650 bound to ASN G 295 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG G REMARK 800 651 through MAN G 656 bound to ASN G 301 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues HIS Q REMARK 800 33 through MAN Q 309 bound to ASN G 332 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG G 657 bound REMARK 800 to ASN G 355 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG G 658 bound REMARK 800 to ASN G 363 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG G REMARK 800 667 through MAN G 670 bound to ASN G 392 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD8 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG G 671 bound REMARK 800 to ASN G 411 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD9 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG G REMARK 800 672 through MAN G 676 bound to ASN G 448 REMARK 800 REMARK 800 SITE_IDENTIFIER: AE1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG G REMARK 800 640 through MAN G 647 REMARK 800 REMARK 800 SITE_IDENTIFIER: AE2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG G REMARK 800 659 through MAN G 666 DBREF 6CH8 B 512 664 UNP Q2N0S7 Q2N0S7_9HIV1 509 661 DBREF 6CH8 D 1 225 PDB 6CH8 6CH8 1 225 DBREF 6CH8 E 1 216 PDB 6CH8 6CH8 1 216 DBREF 6CH8 G 31 511 UNP Q2N0S6 Q2N0S6_9HIV1 30 508 DBREF 6CH8 Q 1 241 PDB 6CH8 6CH8 1 241 DBREF 6CH8 R 1 215 PDB 6CH8 6CH8 1 215 SEQADV 6CH8 CYS B 605 UNP Q2N0S7 THR 602 ENGINEERED MUTATION SEQADV 6CH8 ASN G 332 UNP Q2N0S6 THR 330 CONFLICT SEQADV 6CH8 CYS G 501 UNP Q2N0S6 ALA 498 ENGINEERED MUTATION SEQRES 1 B 153 ALA VAL GLY ILE GLY ALA VAL PHE LEU GLY PHE LEU GLY SEQRES 2 B 153 ALA ALA GLY SER THR MET GLY ALA ALA SER MET THR LEU SEQRES 3 B 153 THR VAL GLN ALA ARG ASN LEU LEU SER GLY ILE VAL GLN SEQRES 4 B 153 GLN GLN SER ASN LEU LEU ARG ALA ILE GLU ALA GLN GLN SEQRES 5 B 153 HIS LEU LEU LYS LEU THR VAL TRP GLY ILE LYS GLN LEU SEQRES 6 B 153 GLN ALA ARG VAL LEU ALA VAL GLU ARG TYR LEU ARG ASP SEQRES 7 B 153 GLN GLN LEU LEU GLY ILE TRP GLY CYS SER GLY LYS LEU SEQRES 8 B 153 ILE CYS CYS THR ASN VAL PRO TRP ASN SER SER TRP SER SEQRES 9 B 153 ASN ARG ASN LEU SER GLU ILE TRP ASP ASN MET THR TRP SEQRES 10 B 153 LEU GLN TRP ASP LYS GLU ILE SER ASN TYR THR GLN ILE SEQRES 11 B 153 ILE TYR GLY LEU LEU GLU GLU SER GLN ASN GLN GLN GLU SEQRES 12 B 153 LYS ASN GLU GLN ASP LEU LEU ALA LEU ASP SEQRES 1 D 243 GLU GLY GLN LEU VAL GLN SER GLY ALA GLU LEU LYS LYS SEQRES 2 D 243 PRO GLY ALA SER VAL LYS ILE SER CYS LYS THR SER GLY SEQRES 3 D 243 TYR ARG PHE ASN PHE TYR HIS ILE ASN TRP ILE ARG GLN SEQRES 4 D 243 THR ALA GLY ARG GLY PRO GLU TRP MET GLY TRP ILE SER SEQRES 5 D 243 PRO TYR SER GLY ASP LYS ASN LEU ALA PRO ALA PHE GLN SEQRES 6 D 243 ASP ARG VAL ILE MET THR THR ASP THR GLU VAL PRO VAL SEQRES 7 D 243 THR SER PHE THR SER THR GLY ALA ALA TYR MET GLU ILE SEQRES 8 D 243 ARG ASN LEU LYS PHE ASP ASP THR GLY THR TYR PHE CYS SEQRES 9 D 243 ALA LYS GLY LEU LEU ARG ASP GLY SER SER THR TRP LEU SEQRES 10 D 243 PRO TYR LEU TRP GLY GLN GLY THR LEU LEU THR VAL SER SEQRES 11 D 243 SER ALA SER THR LYS GLY PRO SER VAL PHE PRO LEU ALA SEQRES 12 D 243 PRO SER SER LYS SER THR SER GLY GLY THR ALA ALA LEU SEQRES 13 D 243 GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU PRO VAL THR SEQRES 14 D 243 VAL SER TRP ASN SER GLY ALA LEU THR SER GLY VAL HIS SEQRES 15 D 243 THR PHE PRO ALA VAL LEU GLN SER SER GLY LEU TYR SER SEQRES 16 D 243 LEU SER SER VAL VAL THR VAL PRO SER SER SER LEU GLY SEQRES 17 D 243 THR GLN THR TYR ILE CYS ASN VAL ASN HIS LYS PRO SER SEQRES 18 D 243 ASN THR LYS VAL ASP LYS ARG VAL GLU PRO LYS SER CYS SEQRES 19 D 243 ASP LYS GLY LEU GLU VAL LEU PHE GLN SEQRES 1 E 216 GLN SER VAL LEU THR GLN SER ALA SER VAL SER GLY SER SEQRES 2 E 216 LEU GLY GLN SER VAL THR ILE SER CYS THR GLY PRO ASN SEQRES 3 E 216 SER VAL CYS CYS SER HIS LYS SER ILE SER TRP TYR GLN SEQRES 4 E 216 TRP PRO PRO GLY ARG ALA PRO THR LEU ILE ILE TYR GLU SEQRES 5 E 216 ASP ASN GLU ARG ALA PRO GLY ILE SER PRO ARG PHE SER SEQRES 6 E 216 GLY TYR LYS SER TYR TRP SER ALA TYR LEU THR ILE SER SEQRES 7 E 216 ASP LEU ARG PRO GLU ASP GLU THR THR TYR TYR CYS CYS SEQRES 8 E 216 SER TYR THR HIS ASN SER GLY CYS VAL PHE GLY THR GLY SEQRES 9 E 216 THR LYS VAL SER VAL LEU GLY GLN SER LYS ALA ASN PRO SEQRES 10 E 216 SER VAL THR LEU PHE PRO PRO SER SER GLU GLU LEU GLN SEQRES 11 E 216 ALA ASN LYS ALA THR LEU VAL CYS LEU ILE SER ASP PHE SEQRES 12 E 216 TYR PRO GLY ALA VAL THR VAL ALA TRP LYS ALA ASP SER SEQRES 13 E 216 SER PRO VAL LYS ALA GLY VAL GLU THR THR THR PRO SER SEQRES 14 E 216 LYS GLN SER ASN ASN LYS TYR ALA ALA SER SER TYR LEU SEQRES 15 E 216 SER LEU THR PRO GLU GLN TRP LYS SER HIS ARG SER TYR SEQRES 16 E 216 SER CYS GLN VAL THR HIS GLU GLY SER THR VAL GLU LYS SEQRES 17 E 216 THR VAL ALA PRO THR GLU CYS SER SEQRES 1 G 479 ALA GLU ASN LEU TRP VAL THR VAL TYR TYR GLY VAL PRO SEQRES 2 G 479 VAL TRP LYS ASP ALA GLU THR THR LEU PHE CYS ALA SER SEQRES 3 G 479 ASP ALA LYS ALA TYR GLU THR GLU LYS HIS ASN VAL TRP SEQRES 4 G 479 ALA THR HIS ALA CYS VAL PRO THR ASP PRO ASN PRO GLN SEQRES 5 G 479 GLU ILE HIS LEU GLU ASN VAL THR GLU GLU PHE ASN MET SEQRES 6 G 479 TRP LYS ASN ASN MET VAL GLU GLN MET HIS THR ASP ILE SEQRES 7 G 479 ILE SER LEU TRP ASP GLN SER LEU LYS PRO CYS VAL LYS SEQRES 8 G 479 LEU THR PRO LEU CYS VAL THR LEU GLN CYS THR ASN VAL SEQRES 9 G 479 THR ASN ASN ILE THR ASP ASP MET ARG GLY GLU LEU LYS SEQRES 10 G 479 ASN CYS SER PHE ASN MET THR THR GLU LEU ARG ASP LYS SEQRES 11 G 479 LYS GLN LYS VAL TYR SER LEU PHE TYR ARG LEU ASP VAL SEQRES 12 G 479 VAL GLN ILE ASN GLU ASN GLN GLY ASN ARG SER ASN ASN SEQRES 13 G 479 SER ASN LYS GLU TYR ARG LEU ILE ASN CYS ASN THR SER SEQRES 14 G 479 ALA ILE THR GLN ALA CYS PRO LYS VAL SER PHE GLU PRO SEQRES 15 G 479 ILE PRO ILE HIS TYR CYS ALA PRO ALA GLY PHE ALA ILE SEQRES 16 G 479 LEU LYS CYS LYS ASP LYS LYS PHE ASN GLY THR GLY PRO SEQRES 17 G 479 CYS PRO SER VAL SER THR VAL GLN CYS THR HIS GLY ILE SEQRES 18 G 479 LYS PRO VAL VAL SER THR GLN LEU LEU LEU ASN GLY SER SEQRES 19 G 479 LEU ALA GLU GLU GLU VAL MET ILE ARG SER GLU ASN ILE SEQRES 20 G 479 THR ASN ASN ALA LYS ASN ILE LEU VAL GLN PHE ASN THR SEQRES 21 G 479 PRO VAL GLN ILE ASN CYS THR ARG PRO ASN ASN ASN THR SEQRES 22 G 479 ARG LYS SER ILE ARG ILE GLY PRO GLY GLN ALA PHE TYR SEQRES 23 G 479 ALA THR GLY ASP ILE ILE GLY ASP ILE ARG GLN ALA HIS SEQRES 24 G 479 CYS ASN VAL SER LYS ALA THR TRP ASN GLU THR LEU GLY SEQRES 25 G 479 LYS VAL VAL LYS GLN LEU ARG LYS HIS PHE GLY ASN ASN SEQRES 26 G 479 THR ILE ILE ARG PHE ALA ASN SER SER GLY GLY ASP LEU SEQRES 27 G 479 GLU VAL THR THR HIS SER PHE ASN CYS GLY GLY GLU PHE SEQRES 28 G 479 PHE TYR CYS ASN THR SER GLY LEU PHE ASN SER THR TRP SEQRES 29 G 479 ILE SER ASN THR SER VAL GLN GLY SER ASN SER THR GLY SEQRES 30 G 479 SER ASN ASP SER ILE THR LEU PRO CYS ARG ILE LYS GLN SEQRES 31 G 479 ILE ILE ASN MET TRP GLN ARG ILE GLY GLN ALA MET TYR SEQRES 32 G 479 ALA PRO PRO ILE GLN GLY VAL ILE ARG CYS VAL SER ASN SEQRES 33 G 479 ILE THR GLY LEU ILE LEU THR ARG ASP GLY GLY SER THR SEQRES 34 G 479 ASN SER THR THR GLU THR PHE ARG PRO GLY GLY GLY ASP SEQRES 35 G 479 MET ARG ASP ASN TRP ARG SER GLU LEU TYR LYS TYR LYS SEQRES 36 G 479 VAL VAL LYS ILE GLU PRO LEU GLY VAL ALA PRO THR ARG SEQRES 37 G 479 CYS LYS ARG ARG VAL VAL GLY ARG GLU LYS ARG SEQRES 1 Q 241 GLN VAL GLN LEU ARG GLU SER GLY PRO GLY LEU VAL LYS SEQRES 2 Q 241 PRO SER GLU THR LEU SER LEU SER CYS THR VAL SER GLN SEQRES 3 Q 241 ASP SER ARG PRO SER ASP HIS SER TRP THR TRP VAL ARG SEQRES 4 Q 241 GLN SER PRO GLY LYS ALA LEU GLU TRP ILE GLY ASP ILE SEQRES 5 Q 241 HIS TYR ASN GLY ALA THR THR TYR ASN PRO SER LEU ARG SEQRES 6 Q 241 SER ARG VAL ARG ILE GLU LEU ASP GLN SER ILE PRO ARG SEQRES 7 Q 241 PHE SER LEU LYS MET THR SER MET THR ALA ALA ASP THR SEQRES 8 Q 241 GLY MET TYR TYR CYS ALA ARG ASN ALA ILE ARG ILE TYR SEQRES 9 Q 241 GLY VAL VAL ALA LEU GLY GLU TRP PHE HIS TYR GLY MET SEQRES 10 Q 241 ASP VAL TRP GLY GLN GLY THR ALA VAL THR VAL SER SER SEQRES 11 Q 241 ALA SER THR LYS GLY PRO SER VAL PHE PRO LEU ALA PRO SEQRES 12 Q 241 SER SER LYS SER THR SER GLY GLY THR ALA ALA LEU GLY SEQRES 13 Q 241 CYS LEU VAL LYS ASP TYR PHE PRO GLU PRO VAL THR VAL SEQRES 14 Q 241 SER TRP ASN SER GLY ALA LEU THR SER GLY VAL HIS THR SEQRES 15 Q 241 PHE PRO ALA VAL LEU GLN SER SER GLY LEU TYR SER LEU SEQRES 16 Q 241 SER SER VAL VAL THR VAL PRO SER SER SER LEU GLY THR SEQRES 17 Q 241 GLN THR TYR ILE CYS ASN VAL ASN HIS LYS PRO SER ASN SEQRES 18 Q 241 THR LYS VAL ASP LYS ARG VAL GLU PRO LYS SER CYS ASP SEQRES 19 Q 241 LYS HIS HIS HIS HIS HIS HIS SEQRES 1 R 215 TRP ALA SER SER GLU LEU THR GLN PRO PRO SER VAL SER SEQRES 2 R 215 VAL SER PRO GLY GLN THR ALA ARG ILE THR CYS SER GLY SEQRES 3 R 215 ALA PRO LEU THR SER ARG PHE THR TYR TRP TYR ARG GLN SEQRES 4 R 215 LYS PRO GLY GLN ALA PRO VAL LEU ILE ILE SER ARG SER SEQRES 5 R 215 SER GLN ARG SER SER GLY TRP SER GLY ARG PHE SER ALA SEQRES 6 R 215 SER TRP SER GLY THR THR VAL THR LEU THR ILE ARG GLY SEQRES 7 R 215 VAL GLN ALA ASP ASP GLU ALA ASP TYR TYR CYS GLN SER SEQRES 8 R 215 SER ASP THR SER ASP SER TYR LYS MET PHE GLY GLY GLY SEQRES 9 R 215 THR LYS LEU THR VAL LEU GLY GLN PRO ALA ALA ALA PRO SEQRES 10 R 215 SER VAL THR LEU PHE PRO PRO SER SER GLU GLU LEU GLN SEQRES 11 R 215 ALA ASN LYS ALA THR LEU VAL CYS LEU ILE SER ASP PHE SEQRES 12 R 215 TYR PRO GLY ALA VAL THR VAL ALA TRP LYS ALA ASP SER SEQRES 13 R 215 SER PRO VAL LYS ALA GLY VAL GLU THR THR THR PRO SER SEQRES 14 R 215 LYS GLN SER ASN ASN LYS TYR ALA ALA SER SER TYR LEU SEQRES 15 R 215 SER LEU THR PRO GLU GLN TRP LYS SER HIS LYS SER TYR SEQRES 16 R 215 SER CYS GLN VAL THR HIS GLU GLY SER THR VAL GLU LYS SEQRES 17 R 215 THR VAL ALA PRO THR GLU CYS HET NAG B 701 14 HET NAG B 702 14 HET NAG B 703 14 HET BMA B 704 11 HET NAG B 705 14 HET NAG B 706 14 HET BMA B 707 11 HET MAN B 708 11 HET MAN B 709 11 HET NAG G 601 14 HET NAG G 602 14 HET BMA G 603 11 HET MAN G 604 11 HET MAN G 605 11 HET MAN G 606 11 HET MAN G 607 11 HET NAG G 608 14 HET NAG G 609 14 HET BMA G 610 11 HET MAN G 611 11 HET MAN G 612 11 HET NAG G 613 14 HET NAG G 614 14 HET BMA G 615 11 HET MAN G 616 11 HET MAN G 617 11 HET MAN G 618 11 HET MAN G 619 11 HET NAG G 620 14 HET NAG G 621 14 HET BMA G 622 11 HET MAN G 623 11 HET MAN G 624 11 HET NAG G 625 14 HET NAG G 626 14 HET BMA G 627 11 HET MAN G 628 11 HET NAG G 629 14 HET NAG G 630 14 HET BMA G 631 11 HET MAN G 632 11 HET NAG G 633 14 HET NAG G 634 14 HET BMA G 635 11 HET MAN G 636 11 HET MAN G 637 11 HET MAN G 638 11 HET MAN G 639 11 HET NAG G 640 14 HET NAG G 641 14 HET BMA G 642 11 HET MAN G 643 11 HET MAN G 644 11 HET MAN G 645 11 HET MAN G 646 11 HET MAN G 647 11 HET NAG G 648 14 HET NAG G 649 14 HET BMA G 650 11 HET NAG G 651 14 HET NAG G 652 14 HET BMA G 653 11 HET MAN G 654 11 HET MAN G 655 11 HET MAN G 656 11 HET NAG G 657 14 HET NAG G 658 14 HET NAG G 659 14 HET NAG G 660 14 HET BMA G 661 11 HET MAN G 662 11 HET MAN G 663 11 HET MAN G 664 11 HET MAN G 665 11 HET MAN G 666 11 HET NAG G 667 14 HET NAG G 668 14 HET BMA G 669 11 HET MAN G 670 11 HET NAG G 671 14 HET NAG G 672 14 HET NAG G 673 14 HET BMA G 674 11 HET MAN G 675 11 HET MAN G 676 11 HET NAG Q 301 14 HET NAG Q 302 14 HET BMA Q 303 11 HET MAN Q 304 11 HET MAN Q 305 11 HET MAN Q 306 11 HET MAN Q 307 11 HET MAN Q 308 11 HET MAN Q 309 11 HETNAM NAG N-ACETYL-D-GLUCOSAMINE HETNAM BMA BETA-D-MANNOSE HETNAM MAN ALPHA-D-MANNOSE FORMUL 7 NAG 36(C8 H15 N O6) FORMUL 8 BMA 16(C6 H12 O6) FORMUL 9 MAN 42(C6 H12 O6) HELIX 1 AA1 THR B 529 THR B 536 1 8 HELIX 2 AA2 LEU B 537 ASN B 543 1 7 HELIX 3 AA3 THR B 569 ILE B 595 1 27 HELIX 4 AA4 ASN B 618 ASP B 624 1 7 HELIX 5 AA5 TRP B 628 SER B 636 1 9 HELIX 6 AA6 TYR B 638 GLN B 652 1 15 HELIX 7 AA7 GLU B 657 ALA B 662 1 6 HELIX 8 AA8 LYS D 83 ASP D 86 5 4 HELIX 9 AA9 ARG E 81 GLU E 85 5 5 HELIX 10 AB1 THR E 185 SER E 191 1 7 HELIX 11 AB2 ASN G 99 SER G 115 1 17 HELIX 12 AB3 LEU G 122 CYS G 126 5 5 HELIX 13 AB4 LYS G 335 LYS G 351 1 17 HELIX 14 AB5 THR G 387 LEU G 390 5 4 HELIX 15 AB6 MET G 475 SER G 481 1 7 HELIX 16 AB7 THR R 185 LYS R 190 1 6 SHEET 1 AA1 3 CYS B 605 PRO B 609 0 SHEET 2 AA1 3 TRP G 35 TYR G 40 -1 O VAL G 36 N VAL B 608 SHEET 3 AA1 3 LEU G 494 THR G 499 -1 O THR G 499 N TRP G 35 SHEET 1 AA2 4 VAL D 5 SER D 7 0 SHEET 2 AA2 4 LYS D 19 LYS D 23 -1 O LYS D 23 N VAL D 5 SHEET 3 AA2 4 ALA D 77 ILE D 82 -1 O MET D 80 N ILE D 20 SHEET 4 AA2 4 VAL D 67 ILE D 68 -1 N ILE D 68 O GLU D 81 SHEET 1 AA3 5 LYS D 57 LEU D 59 0 SHEET 2 AA3 5 ARG D 43 ILE D 51 -1 N TRP D 50 O ASN D 58 SHEET 3 AA3 5 ILE D 34 THR D 40 -1 N TRP D 36 O MET D 48 SHEET 4 AA3 5 GLY D 88 GLY D 95 -1 O PHE D 91 N ILE D 37 SHEET 5 AA3 5 PRO D 100F TRP D 103 -1 O LEU D 102 N LYS D 94 SHEET 1 AA4 5 LYS D 57 LEU D 59 0 SHEET 2 AA4 5 ARG D 43 ILE D 51 -1 N TRP D 50 O ASN D 58 SHEET 3 AA4 5 ILE D 34 THR D 40 -1 N TRP D 36 O MET D 48 SHEET 4 AA4 5 GLY D 88 GLY D 95 -1 O PHE D 91 N ILE D 37 SHEET 5 AA4 5 THR D 107 LEU D 109 -1 O THR D 107 N TYR D 90 SHEET 1 AA5 2 VAL D 72C PRO D 72D 0 SHEET 2 AA5 2 SER D 74 THR D 75 -1 O THR D 75 N VAL D 72C SHEET 1 AA6 4 SER D 120 PRO D 123 0 SHEET 2 AA6 4 CYS D 140 TYR D 145 -1 O LEU D 141 N PHE D 122 SHEET 3 AA6 4 TYR D 176 VAL D 182 -1 O TYR D 176 N TYR D 145 SHEET 4 AA6 4 VAL D 163 LEU D 170 -1 N VAL D 169 O SER D 177 SHEET 1 AA7 2 VAL D 152 TRP D 154 0 SHEET 2 AA7 2 CYS D 196 VAL D 198 -1 O ASN D 197 N SER D 153 SHEET 1 AA8 4 THR E 5 GLN E 6 0 SHEET 2 AA8 4 VAL E 18 THR E 23 -1 O THR E 23 N THR E 5 SHEET 3 AA8 4 SER E 72 ILE E 77 -1 O ILE E 77 N VAL E 18 SHEET 4 AA8 4 TYR E 67 LYS E 68 -1 N TYR E 67 O TYR E 74 SHEET 1 AA9 6 ALA E 8 SER E 13 0 SHEET 2 AA9 6 THR E 105 LEU E 110 1 O LEU E 110 N GLY E 12 SHEET 3 AA9 6 THR E 87 TYR E 93 -1 N TYR E 88 O THR E 105 SHEET 4 AA9 6 SER E 34 TRP E 40 -1 N TRP E 40 O THR E 87 SHEET 5 AA9 6 THR E 47 GLU E 52 -1 O THR E 47 N GLN E 39 SHEET 6 AA9 6 GLU E 55 ARG E 56 -1 O GLU E 55 N GLU E 52 SHEET 1 AB1 4 ALA E 8 SER E 13 0 SHEET 2 AB1 4 THR E 105 LEU E 110 1 O LEU E 110 N GLY E 12 SHEET 3 AB1 4 THR E 87 TYR E 93 -1 N TYR E 88 O THR E 105 SHEET 4 AB1 4 VAL E 100 PHE E 101 -1 O VAL E 100 N SER E 92 SHEET 1 AB2 4 THR E 120 PHE E 122 0 SHEET 2 AB2 4 VAL E 137 SER E 141 -1 O VAL E 137 N PHE E 122 SHEET 3 AB2 4 TYR E 176 SER E 179 -1 O ALA E 178 N ILE E 140 SHEET 4 AB2 4 SER E 169 LYS E 170 -1 N SER E 169 O ALA E 177 SHEET 1 AB3 2 TRP E 152 LYS E 153 0 SHEET 2 AB3 2 SER E 196 CYS E 197 -1 O SER E 196 N LYS E 153 SHEET 1 AB4 4 TRP G 45 ASP G 47 0 SHEET 2 AB4 4 TYR G 486 ILE G 491 -1 O LYS G 490 N LYS G 46 SHEET 3 AB4 4 PHE G 223 CYS G 228 -1 N LEU G 226 O LYS G 487 SHEET 4 AB4 4 VAL G 242 SER G 243 -1 O SER G 243 N LYS G 227 SHEET 1 AB5 3 GLN G 130 THR G 132 0 SHEET 2 AB5 3 LEU G 154 THR G 162 -1 O ASN G 156 N THR G 132 SHEET 3 AB5 3 LYS G 169 TYR G 177 -1 O SER G 174 N CYS G 157 SHEET 1 AB6 2 VAL G 181 GLN G 183 0 SHEET 2 AB6 2 TYR G 191 LEU G 193 -1 O ARG G 192 N VAL G 182 SHEET 1 AB7 3 ALA G 200 GLN G 203 0 SHEET 2 AB7 3 GLN G 432 TYR G 435 1 O TYR G 435 N THR G 202 SHEET 3 AB7 3 ILE G 423 ILE G 424 -1 N ILE G 424 O MET G 434 SHEET 1 AB8 4 LEU G 259 LEU G 261 0 SHEET 2 AB8 4 GLY G 441 LEU G 454 -1 O GLY G 451 N LEU G 260 SHEET 3 AB8 4 ILE G 284 ASN G 302 -1 N CYS G 296 O CYS G 445 SHEET 4 AB8 4 MET G 271 ARG G 273 -1 N MET G 271 O GLN G 287 SHEET 1 AB9 7 LEU G 259 LEU G 261 0 SHEET 2 AB9 7 GLY G 441 LEU G 454 -1 O GLY G 451 N LEU G 260 SHEET 3 AB9 7 ILE G 284 ASN G 302 -1 N CYS G 296 O CYS G 445 SHEET 4 AB9 7 ALA G 329 SER G 334 -1 O ASN G 332 N ASN G 295 SHEET 5 AB9 7 SER G 413 LYS G 421 -1 O ILE G 414 N VAL G 333 SHEET 6 AB9 7 GLU G 381 CYS G 385 -1 N TYR G 384 O ARG G 419 SHEET 7 AB9 7 HIS G 374 CYS G 378 -1 N CYS G 378 O GLU G 381 SHEET 1 AC1 2 ARG G 304 ARG G 310 0 SHEET 2 AC1 2 ALA G 316 THR G 320 -1 O PHE G 317 N ILE G 309 SHEET 1 AC2 2 ILE G 358 ARG G 360 0 SHEET 2 AC2 2 THR G 465 THR G 467 1 O GLU G 466 N ILE G 358 SHEET 1 AC3 4 GLN Q 3 SER Q 7 0 SHEET 2 AC3 4 LEU Q 18 SER Q 25 -1 O SER Q 21 N SER Q 7 SHEET 3 AC3 4 ARG Q 78 MET Q 83 -1 O PHE Q 79 N CYS Q 22 SHEET 4 AC3 4 ARG Q 69 GLU Q 71 -1 N GLU Q 71 O SER Q 80 SHEET 1 AC4 2 LEU Q 11 VAL Q 12 0 SHEET 2 AC4 2 THR Q 127 VAL Q 128 1 O THR Q 127 N VAL Q 12 SHEET 1 AC5 5 THR Q 58 THR Q 59 0 SHEET 2 AC5 5 ALA Q 45 ILE Q 52 -1 N ASP Q 51 O THR Q 59 SHEET 3 AC5 5 SER Q 34 SER Q 41 -1 N TRP Q 35 O ILE Q 52 SHEET 4 AC5 5 MET Q 93 ILE Q 101 -1 O MET Q 93 N GLN Q 40 SHEET 5 AC5 5 HIS Q 114 TRP Q 120 -1 O GLY Q 116 N ALA Q 100 SHEET 1 AC6 2 ILE Q 212 CYS Q 213 0 SHEET 2 AC6 2 LYS Q 226 ARG Q 227 -1 O LYS Q 226 N CYS Q 213 SHEET 1 AC7 2 SER R 13 VAL R 14 0 SHEET 2 AC7 2 THR R 108 VAL R 109 1 O THR R 108 N VAL R 14 SHEET 1 AC8 3 THR R 23 SER R 25 0 SHEET 2 AC8 3 THR R 71 THR R 73 -1 O VAL R 72 N CYS R 24 SHEET 3 AC8 3 SER R 66 TRP R 67 -1 N SER R 66 O THR R 73 SHEET 1 AC9 3 ARG R 38 GLN R 39 0 SHEET 2 AC9 3 ASP R 86 TYR R 87 -1 O ASP R 86 N GLN R 39 SHEET 3 AC9 3 THR R 105 LYS R 106 -1 O THR R 105 N TYR R 87 SSBOND 1 CYS D 22 CYS D 92 1555 1555 2.03 SSBOND 2 CYS D 140 CYS D 196 1555 1555 2.04 SSBOND 3 CYS G 54 CYS G 74 1555 1555 2.04 SSBOND 4 CYS G 126 CYS G 196 1555 1555 2.03 SSBOND 5 CYS G 296 CYS G 331 1555 1555 1.99 SSBOND 6 CYS G 378 CYS G 445 1555 1555 2.04 SSBOND 7 CYS G 385 CYS G 418 1555 1555 2.03 SSBOND 8 CYS Q 22 CYS Q 96 1555 1555 2.03 SSBOND 9 CYS Q 157 CYS Q 213 1555 1555 2.03 SSBOND 10 CYS R 24 CYS R 89 1555 1555 2.03 LINK ND2 ASN B 611 C1 NAG B 701 1555 1555 1.44 LINK ND2 ASN B 618 C1 NAG B 702 1555 1555 1.43 LINK OD2 ASP B 624 CB ASP D 99 1555 1555 1.51 LINK OD2 ASP B 624 CG ASP D 99 1555 1555 1.24 LINK ND2 ASN B 637 C1 NAG B 705 1555 1555 1.44 LINK OE1 GLU G 64 C2 MAN G 638 1555 1555 1.38 LINK ND2 ASN G 88 C1 NAG G 601 1555 1555 1.45 LINK ND2 ASN G 133 C1 NAG G 608 1555 1555 1.43 LINK ND2 ASN G 156 C1 NAG G 613 1555 1555 1.43 LINK ND2 ASN G 160 C1 NAG G 620 1555 1555 1.46 LINK ND2 ASN G 197 C1 NAG G 625 1555 1555 1.50 LINK ND2 ASN G 234 C1 NAG G 629 1555 1555 1.44 LINK ND2 ASN G 262 C1 NAG G 633 1555 1555 1.45 LINK ND2 ASN G 295 C1 NAG G 648 1555 1555 1.36 LINK ND2 ASN G 301 C1 NAG G 651 1555 1555 1.44 LINK ND2 ASN G 332 C1 NAG Q 301 1555 1555 1.43 LINK ND2 ASN G 355 C1 NAG G 657 1555 1555 1.44 LINK ND2 ASN G 363 C1 NAG G 658 1555 1555 1.45 LINK ND2 ASN G 392 C1 NAG G 667 1555 1555 1.44 LINK ND2 ASN G 411 C1 NAG G 671 1555 1555 1.44 LINK ND2 ASN G 448 C1 NAG G 672 1555 1555 1.43 LINK NE2 HIS Q 33 O6 MAN Q 309 1555 1555 1.30 LINK CA GLN Q 188 OE1 GLU R 164 1555 1555 1.45 LINK CB GLN Q 188 OE2 GLU R 164 1555 1555 1.48 LINK O4 NAG B 702 C1 NAG B 703 1555 1555 1.44 LINK O4 NAG B 703 C1 BMA B 704 1555 1555 1.45 LINK O4 NAG B 705 C1 NAG B 706 1555 1555 1.44 LINK O4 NAG B 706 C1 BMA B 707 1555 1555 1.45 LINK O6 BMA B 707 C1 MAN B 708 1555 1555 1.46 LINK O6 MAN B 708 C1 MAN B 709 1555 1555 1.44 LINK O4 NAG G 601 C1 NAG G 602 1555 1555 1.44 LINK O4 NAG G 602 C1 BMA G 603 1555 1555 1.46 LINK O3 BMA G 603 C1 MAN G 605 1555 1555 1.45 LINK O6 BMA G 603 C1 MAN G 604 1555 1555 1.45 LINK O3 MAN G 604 C1 MAN G 606 1555 1555 1.45 LINK O6 MAN G 605 C1 MAN G 607 1555 1555 1.45 LINK O4 NAG G 608 C1 NAG G 609 1555 1555 1.44 LINK O4 NAG G 609 C1 BMA G 610 1555 1555 1.44 LINK O3 BMA G 610 C1 MAN G 612 1555 1555 1.50 LINK O6 BMA G 610 C1 MAN G 611 1555 1555 1.44 LINK O4 NAG G 613 C1 NAG G 614 1555 1555 1.44 LINK O4 NAG G 614 C1 BMA G 615 1555 1555 1.44 LINK O6 BMA G 615 C1 MAN G 616 1555 1555 1.45 LINK O3 MAN G 616 C1 MAN G 618 1555 1555 1.46 LINK O6 MAN G 616 C1 MAN G 617 1555 1555 1.46 LINK O6 MAN G 618 C1 MAN G 619 1555 1555 1.45 LINK O4 NAG G 620 C1 NAG G 621 1555 1555 1.46 LINK O4 NAG G 621 C1 BMA G 622 1555 1555 1.45 LINK O6 BMA G 622 C1 MAN G 623 1555 1555 1.44 LINK O6 MAN G 623 C1 MAN G 624 1555 1555 1.44 LINK O4 NAG G 625 C1 NAG G 626 1555 1555 1.43 LINK O4 NAG G 626 C1 BMA G 627 1555 1555 1.43 LINK O3 BMA G 627 C1 MAN G 628 1555 1555 1.44 LINK O4 NAG G 629 C1 NAG G 630 1555 1555 1.44 LINK O4 NAG G 630 C1 BMA G 631 1555 1555 1.44 LINK O6 BMA G 631 C1 MAN G 632 1555 1555 1.44 LINK O4 NAG G 633 C1 NAG G 634 1555 1555 1.45 LINK O4 NAG G 634 C1 BMA G 635 1555 1555 1.45 LINK O3 BMA G 635 C1 MAN G 638 1555 1555 1.46 LINK O6 BMA G 635 C1 MAN G 636 1555 1555 1.45 LINK O3 MAN G 636 C1 MAN G 639 1555 1555 1.46 LINK O6 MAN G 636 C1 MAN G 637 1555 1555 1.44 LINK O4 NAG G 640 C1 NAG G 641 1555 1555 1.43 LINK O4 NAG G 641 C1 BMA G 642 1555 1555 1.43 LINK O3 BMA G 642 C1 MAN G 646 1555 1555 1.46 LINK O6 BMA G 642 C1 MAN G 643 1555 1555 1.45 LINK O3 MAN G 643 C1 MAN G 644 1555 1555 1.44 LINK O6 MAN G 643 C1 MAN G 645 1555 1555 1.44 LINK O6 MAN G 644 C1 MAN G 647 1555 1555 1.44 LINK O4 NAG G 648 C1 NAG G 649 1555 1555 1.43 LINK O4 NAG G 649 C1 BMA G 650 1555 1555 1.44 LINK O4 NAG G 651 C1 NAG G 652 1555 1555 1.44 LINK O4 NAG G 652 C1 BMA G 653 1555 1555 1.48 LINK O3 BMA G 653 C1 MAN G 655 1555 1555 1.44 LINK O6 BMA G 653 C1 MAN G 654 1555 1555 1.44 LINK O6 MAN G 654 C1 MAN G 656 1555 1555 1.45 LINK O4 NAG G 659 C1 NAG G 660 1555 1555 1.46 LINK O4 NAG G 660 C1 BMA G 661 1555 1555 1.48 LINK O3 BMA G 661 C1 MAN G 662 1555 1555 1.45 LINK O6 BMA G 661 C1 MAN G 663 1555 1555 1.45 LINK O2 MAN G 662 C1 MAN G 666 1555 1555 1.45 LINK O3 MAN G 663 C1 MAN G 665 1555 1555 1.45 LINK O6 MAN G 663 C1 MAN G 664 1555 1555 1.44 LINK O4 NAG G 667 C1 NAG G 668 1555 1555 1.45 LINK O4 NAG G 668 C1 BMA G 669 1555 1555 1.44 LINK O3 BMA G 669 C1 MAN G 670 1555 1555 1.44 LINK O4 NAG G 672 C1 NAG G 673 1555 1555 1.45 LINK O4 NAG G 673 C1 BMA G 674 1555 1555 1.45 LINK O3 BMA G 674 C1 MAN G 675 1555 1555 1.50 LINK O6 BMA G 674 C1 MAN G 676 1555 1555 1.49 LINK O4 NAG Q 301 C1 NAG Q 302 1555 1555 1.43 LINK O4 NAG Q 302 C1 BMA Q 303 1555 1555 1.43 LINK O3 BMA Q 303 C1 MAN Q 307 1555 1555 1.43 LINK O6 BMA Q 303 C1 MAN Q 304 1555 1555 1.44 LINK O3 MAN Q 304 C1 MAN Q 306 1555 1555 1.44 LINK O6 MAN Q 304 C1 MAN Q 305 1555 1555 1.44 LINK O2 MAN Q 305 C1 MAN Q 309 1555 1555 1.45 LINK O6 MAN Q 307 C1 MAN Q 308 1555 1555 1.46 CISPEP 1 PHE D 146 PRO D 147 0 -4.95 CISPEP 2 TYR E 144 PRO E 145 0 2.81 CISPEP 3 TYR R 144 PRO R 145 0 -3.94 SITE 1 AC1 1 ASN B 611 SITE 1 AC2 7 ASN B 616 ASN B 618 ARG E 56 PRO E 58 SITE 2 AC2 7 GLY E 59 PRO E 62 GLU G 32 SITE 1 AC3 1 ASN B 637 SITE 1 AC4 10 THR B 529 PHE D 31 TRP D 50 ARG D 98 SITE 2 AC4 10 ASP D 99 GLY D 100 SER D 100A THR D 100C SITE 3 AC4 10 HIS E 95 ASN G 88 SITE 1 AC5 2 ASN G 133 LYS G 189 SITE 1 AC6 2 ASN G 156 ASP G 321A SITE 1 AC7 3 GLN G 130 ASN G 160 LYS G 171 SITE 1 AC8 2 ASN G 197 ARG G 310 SITE 1 AC9 3 ASN G 234 THR G 236 SER G 274 SITE 1 AD1 12 ALA G 60 GLU G 62 THR G 63 LYS G 65 SITE 2 AD1 12 SER G 209 GLU G 211 PRO G 212 VAL G 254 SITE 3 AD1 12 ASN G 262 ASN G 377 SER G 447 NAG G 672 SITE 1 AD2 6 GLN G 293 ASN G 295 ASN G 332 VAL G 333 SITE 2 AD2 6 SER G 334 ARG G 444 SITE 1 AD3 2 ASN G 301 ILE G 323 SITE 1 AD4 22 ARG G 327 HIS G 330 ASN G 332 ARG G 444 SITE 2 AD4 22 ASP Q 27 SER Q 28 ARG Q 29 PRO Q 30 SITE 3 AD4 22 SER Q 31 ASP Q 32 SER Q 34 TRP Q 35 SITE 4 AD4 22 HIS Q 53 ARG Q 98 ILE Q 101 ILE Q 103 SITE 5 AD4 22 TYR Q 104 GLY Q 105 VAL Q 106 VAL Q 107 SITE 6 AD4 22 SER R 52 SER R 53 SITE 1 AD5 3 LYS G 351 ASN G 355 ASN G 356 SITE 1 AD6 2 ASN G 363 NAG G 659 SITE 1 AD7 2 ASN G 392 NAG G 660 SITE 1 AD8 1 ASN G 411 SITE 1 AD9 3 ASN G 262 ASN G 448 NAG G 633 SITE 1 AE1 6 ASN G 276 ILE G 277 THR G 278 ASN G 279 SITE 2 AE1 6 THR G 461 ASN G 462 SITE 1 AE2 8 ASN G 386 SER G 388 PRO G 417 THR G 461 SITE 2 AE2 8 ASN G 462 NAG G 640 NAG G 658 NAG G 667 CRYST1 239.223 239.223 355.266 90.00 90.00 120.00 H 3 2 18 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 0.004180 0.002413 0.000000 0.00000 SCALE2 0.000000 0.004827 0.000000 0.00000 SCALE3 0.000000 0.000000 0.002815 0.00000