HEADER VIRAL PROTEIN/IMMUNE SYSTEM 07-FEB-25 9LU3 TITLE LN1F9 FAB BOUND TO NIPAH VIRUS ATTACHMENT (G) GLYCOPROTEIN HEAD DOMAIN COMPND MOL_ID: 1; COMPND 2 MOLECULE: GLYCOPROTEIN G; COMPND 3 CHAIN: A, B; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: MAB LN1F9 FAB HEAVY CHAIN; COMPND 7 CHAIN: H, D; COMPND 8 ENGINEERED: YES; COMPND 9 MOL_ID: 3; COMPND 10 MOLECULE: MAB LN1F9 FAB LIGHT CHAIN; COMPND 11 CHAIN: L, E; COMPND 12 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HENIPAVIRUS NIPAHENSE; SOURCE 3 ORGANISM_TAXID: 3052225; SOURCE 4 EXPRESSION_SYSTEM: HOMO; SOURCE 5 EXPRESSION_SYSTEM_TAXID: 9605; SOURCE 6 MOL_ID: 2; SOURCE 7 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 8 ORGANISM_TAXID: 10090; SOURCE 9 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 10 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 11 MOL_ID: 3; SOURCE 12 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 13 ORGANISM_TAXID: 10090; SOURCE 14 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 15 EXPRESSION_SYSTEM_TAXID: 9606 KEYWDS GLYCOPROTEIN G, FAB, VIRAL PROTEIN/IMMUNE SYSTEM, VIRAL PROTEIN- KEYWDS 2 IMMUNE SYSTEM COMPLEX EXPDTA X-RAY DIFFRACTION AUTHOR Z.DENG,W.KUANG REVDAT 1 26-NOV-25 9LU3 0 JRNL AUTH D.ZHOU,Y.WANG,Y.YAO,W.KUANG,R.CHENG,G.ZHANG,H.LIU,X.LI, JRNL AUTH 2 S.CHIU,Z.DENG,H.ZHAO JRNL TITL ANTIGENIC LANDSCAPE OF NIPAH VIRUS ATTACHMENT GLYCOPROTEIN JRNL TITL 2 ANALYSIS REVEALS A PROTECTIVE IMMUNODOMINANT EPITOPE ACROSS JRNL TITL 3 SPECIES JRNL REF NPJ VACCINES 2025 JRNL REFN ESSN 2059-0105 REMARK 2 REMARK 2 RESOLUTION. 3.00 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX (1.20.1_4487: ???) 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) : 3.00 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.44 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340 REMARK 3 COMPLETENESS FOR RANGE (%) : 98.4 REMARK 3 NUMBER OF REFLECTIONS : 46949 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.222 REMARK 3 R VALUE (WORKING SET) : 0.219 REMARK 3 FREE R VALUE : 0.269 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.050 REMARK 3 FREE R VALUE TEST SET COUNT : 2373 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 20.4400 - 7.5900 0.98 2786 126 0.1691 0.1951 REMARK 3 2 7.5900 - 6.0800 0.99 2720 138 0.2002 0.2357 REMARK 3 3 6.0800 - 5.3200 0.99 2644 160 0.1931 0.2463 REMARK 3 4 5.3200 - 4.8400 0.99 2684 136 0.1766 0.2314 REMARK 3 5 4.8400 - 4.5000 0.99 2627 142 0.1725 0.2106 REMARK 3 6 4.5000 - 4.2400 0.98 2621 151 0.1731 0.2145 REMARK 3 7 4.2400 - 4.0300 0.99 2622 141 0.2017 0.2210 REMARK 3 8 4.0300 - 3.8500 0.99 2596 154 0.2234 0.2742 REMARK 3 9 3.8500 - 3.7100 0.99 2626 124 0.2341 0.2960 REMARK 3 10 3.7100 - 3.5800 0.97 2561 133 0.2505 0.3155 REMARK 3 11 3.5800 - 3.4700 0.98 2577 146 0.2679 0.2958 REMARK 3 12 3.4700 - 3.3700 0.98 2595 135 0.2770 0.3791 REMARK 3 13 3.3700 - 3.2800 0.99 2607 148 0.2940 0.3836 REMARK 3 14 3.2800 - 3.2000 0.99 2613 125 0.2966 0.3380 REMARK 3 15 3.2000 - 3.1300 0.98 2568 143 0.3043 0.4181 REMARK 3 16 3.1300 - 3.0600 0.99 2599 132 0.3316 0.3572 REMARK 3 17 3.0600 - 3.0000 0.96 2530 139 0.3322 0.4022 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) : 0.410 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 33.380 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 : 0.011 13647 REMARK 3 ANGLE : 1.326 18558 REMARK 3 CHIRALITY : 0.068 2105 REMARK 3 PLANARITY : 0.012 2362 REMARK 3 DIHEDRAL : 7.198 1896 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 9LU3 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBC ON 12-FEB-25. REMARK 100 THE DEPOSITION ID IS D_1300055165. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 29-NOV-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 : SSRF REMARK 200 BEAMLINE : BL10U2 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.9792 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 16M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XIA2 REMARK 200 DATA SCALING SOFTWARE : XIA2 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 47546 REMARK 200 RESOLUTION RANGE HIGH (A) : 3.000 REMARK 200 RESOLUTION RANGE LOW (A) : 28.600 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.1 REMARK 200 DATA REDUNDANCY : 5.200 REMARK 200 R MERGE (I) : 0.12800 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 5.6000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.00 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.10 REMARK 200 COMPLETENESS FOR SHELL (%) : NULL REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : 0.59400 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 1.800 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 (%): 58.94 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.00 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.3 M AMMONIUM FORMATE, 0.1 M HEPES PH REMARK 280 7.0, 20 % [VOL/VOL] SOKALAN CP5, EVAPORATION, TEMPERATURE 289K 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 61.70800 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 76.18800 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 62.57750 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 76.18800 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 61.70800 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 62.57750 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1, 2 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: 6630 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 34730 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -16.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A 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: D, E REMARK 350 BIOMT1 2 -1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 -62.57750 REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 -76.18800 REMARK 350 REMARK 350 BIOMOLECULE: 2 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: 6820 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 35160 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -15.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: B 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 0.00000 REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 62.57750 REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 76.18800 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 HIS A 162 REMARK 465 HIS A 163 REMARK 465 HIS A 164 REMARK 465 HIS A 165 REMARK 465 HIS A 166 REMARK 465 HIS A 167 REMARK 465 LEU A 168 REMARK 465 GLU A 169 REMARK 465 VAL A 170 REMARK 465 LEU A 171 REMARK 465 PHE A 172 REMARK 465 GLN A 173 REMARK 465 GLY A 174 REMARK 465 VAL A 210 REMARK 465 GLY A 211 REMARK 465 GLN A 212 REMARK 465 SER A 213 REMARK 465 GLY A 214 REMARK 465 TYR A 581 REMARK 465 ASP A 582 REMARK 465 THR A 583 REMARK 465 GLY A 584 REMARK 465 ASP A 585 REMARK 465 ASN A 586 REMARK 465 SER H 215 REMARK 465 CYS H 216 REMARK 465 ASP H 217 REMARK 465 LYS H 218 REMARK 465 THR H 219 REMARK 465 HIS H 220 REMARK 465 HIS H 221 REMARK 465 HIS H 222 REMARK 465 HIS H 223 REMARK 465 HIS H 224 REMARK 465 HIS H 225 REMARK 465 HIS B 162 REMARK 465 HIS B 163 REMARK 465 HIS B 164 REMARK 465 HIS B 165 REMARK 465 HIS B 166 REMARK 465 HIS B 167 REMARK 465 LEU B 168 REMARK 465 GLU B 169 REMARK 465 VAL B 170 REMARK 465 LEU B 171 REMARK 465 PHE B 172 REMARK 465 GLN B 173 REMARK 465 GLY B 174 REMARK 465 VAL B 210 REMARK 465 GLY B 211 REMARK 465 GLN B 212 REMARK 465 SER B 213 REMARK 465 GLY B 214 REMARK 465 THR B 215 REMARK 465 TYR B 581 REMARK 465 ASP B 582 REMARK 465 THR B 583 REMARK 465 GLY B 584 REMARK 465 LYS D 214 REMARK 465 SER D 215 REMARK 465 CYS D 216 REMARK 465 ASP D 217 REMARK 465 LYS D 218 REMARK 465 THR D 219 REMARK 465 HIS D 220 REMARK 465 HIS D 221 REMARK 465 HIS D 222 REMARK 465 HIS D 223 REMARK 465 HIS D 224 REMARK 465 HIS D 225 REMARK 465 ASN E 210 REMARK 465 ARG E 211 REMARK 465 GLY E 212 REMARK 465 GLU E 213 REMARK 465 CYS E 214 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 CYS L 214 SG 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 NZ LYS B 415 O7 NAG B 701 1.31 REMARK 500 OE2 GLU B 501 OG SER D 98 1.84 REMARK 500 OE2 GLU H 50 OD2 ASP H 95 1.96 REMARK 500 OG SER D 203 OG1 THR D 205 2.05 REMARK 500 O SER B 307 NZ LYS B 347 2.11 REMARK 500 OE2 GLU H 6 N CYS H 92 2.15 REMARK 500 NZ LYS B 391 O GLY D 100 2.17 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 OD2 ASP A 360 NE2 GLN E 79 3544 1.77 REMARK 500 OE1 GLN L 79 OD2 ASP B 360 3545 1.82 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 GLN A 196 49.74 -98.75 REMARK 500 ASP A 219 49.18 73.27 REMARK 500 ASP A 225 130.33 -178.72 REMARK 500 ASN A 269 118.37 -169.18 REMARK 500 PRO A 273 155.04 -48.75 REMARK 500 ARG A 338 -78.37 -67.60 REMARK 500 TYR A 351 73.16 -156.70 REMARK 500 SER A 398 34.66 -95.02 REMARK 500 ASP A 420 54.81 -101.33 REMARK 500 ARG A 435 62.31 38.93 REMARK 500 GLN A 490 -157.50 -86.49 REMARK 500 ASN A 534 75.52 69.99 REMARK 500 ASN A 543 40.13 -149.83 REMARK 500 GLU A 544 113.65 -170.26 REMARK 500 ALA A 549 107.49 -170.09 REMARK 500 ALA A 552 -159.25 -163.40 REMARK 500 GLN A 559 -80.79 -123.34 REMARK 500 SER H 28 88.19 -69.47 REMARK 500 TYR H 100A -45.90 77.11 REMARK 500 LEU H 100B 62.00 -112.91 REMARK 500 ASP H 144 75.56 56.08 REMARK 500 PHE H 146 141.11 -170.11 REMARK 500 LEU L 11 117.23 -176.75 REMARK 500 ASN L 30 -121.96 63.80 REMARK 500 LEU L 47 -64.73 -102.82 REMARK 500 ALA L 51 -37.70 72.85 REMARK 500 ASP L 68 -99.00 61.92 REMARK 500 ASN L 138 71.22 29.80 REMARK 500 PRO L 141 -178.68 -69.90 REMARK 500 ASN L 152 -5.45 81.69 REMARK 500 PRO L 204 133.12 -38.94 REMARK 500 LEU B 184 79.10 -117.55 REMARK 500 GLN B 196 55.08 -90.05 REMARK 500 ASP B 225 124.89 -177.56 REMARK 500 ASN B 269 121.38 -170.15 REMARK 500 CYS B 282 132.96 -32.19 REMARK 500 ASN B 288 72.08 54.92 REMARK 500 LYS B 386 31.08 -93.19 REMARK 500 SER B 459 -159.04 -153.23 REMARK 500 SER B 486 -154.57 -142.40 REMARK 500 GLN B 490 -147.95 -100.90 REMARK 500 TRP B 519 56.70 38.05 REMARK 500 ASN B 534 82.53 68.85 REMARK 500 ALA B 552 -148.49 -151.55 REMARK 500 ALA B 558 -66.21 -125.04 REMARK 500 GLN B 559 -127.59 66.52 REMARK 500 PRO D 14 102.70 -47.79 REMARK 500 SER D 28 96.22 -69.15 REMARK 500 VAL D 48 -41.89 -130.28 REMARK 500 TYR D 100A -43.98 78.88 REMARK 500 REMARK 500 THIS ENTRY HAS 61 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS REMARK 500 REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES. REMARK 500 MODEL OMEGA REMARK 500 SER D 130 THR D 131 -148.42 REMARK 500 THR D 205 LYS D 206 140.18 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: PLANAR GROUPS REMARK 500 REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS REMARK 500 AN RMSD GREATER THAN THIS VALUE REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 M RES CSSEQI RMS TYPE REMARK 500 ARG H 83 0.09 SIDE CHAIN REMARK 500 ARG B 548 0.11 SIDE CHAIN REMARK 500 ARG E 108 0.09 SIDE CHAIN REMARK 500 REMARK 500 REMARK: NULL DBREF 9LU3 A 176 602 UNP Q9IH62 GLYCP_NIPAV 176 602 DBREF 9LU3 H 1 225 PDB 9LU3 9LU3 1 225 DBREF 9LU3 L 1 214 PDB 9LU3 9LU3 1 214 DBREF 9LU3 B 176 602 UNP Q9IH62 GLYCP_NIPAV 176 602 DBREF 9LU3 D 1 225 PDB 9LU3 9LU3 1 225 DBREF 9LU3 E 1 214 PDB 9LU3 9LU3 1 214 SEQADV 9LU3 HIS A 162 UNP Q9IH62 EXPRESSION TAG SEQADV 9LU3 HIS A 163 UNP Q9IH62 EXPRESSION TAG SEQADV 9LU3 HIS A 164 UNP Q9IH62 EXPRESSION TAG SEQADV 9LU3 HIS A 165 UNP Q9IH62 EXPRESSION TAG SEQADV 9LU3 HIS A 166 UNP Q9IH62 EXPRESSION TAG SEQADV 9LU3 HIS A 167 UNP Q9IH62 EXPRESSION TAG SEQADV 9LU3 LEU A 168 UNP Q9IH62 EXPRESSION TAG SEQADV 9LU3 GLU A 169 UNP Q9IH62 EXPRESSION TAG SEQADV 9LU3 VAL A 170 UNP Q9IH62 EXPRESSION TAG SEQADV 9LU3 LEU A 171 UNP Q9IH62 EXPRESSION TAG SEQADV 9LU3 PHE A 172 UNP Q9IH62 EXPRESSION TAG SEQADV 9LU3 GLN A 173 UNP Q9IH62 EXPRESSION TAG SEQADV 9LU3 GLY A 174 UNP Q9IH62 EXPRESSION TAG SEQADV 9LU3 PRO A 175 UNP Q9IH62 EXPRESSION TAG SEQADV 9LU3 HIS B 162 UNP Q9IH62 EXPRESSION TAG SEQADV 9LU3 HIS B 163 UNP Q9IH62 EXPRESSION TAG SEQADV 9LU3 HIS B 164 UNP Q9IH62 EXPRESSION TAG SEQADV 9LU3 HIS B 165 UNP Q9IH62 EXPRESSION TAG SEQADV 9LU3 HIS B 166 UNP Q9IH62 EXPRESSION TAG SEQADV 9LU3 HIS B 167 UNP Q9IH62 EXPRESSION TAG SEQADV 9LU3 LEU B 168 UNP Q9IH62 EXPRESSION TAG SEQADV 9LU3 GLU B 169 UNP Q9IH62 EXPRESSION TAG SEQADV 9LU3 VAL B 170 UNP Q9IH62 EXPRESSION TAG SEQADV 9LU3 LEU B 171 UNP Q9IH62 EXPRESSION TAG SEQADV 9LU3 PHE B 172 UNP Q9IH62 EXPRESSION TAG SEQADV 9LU3 GLN B 173 UNP Q9IH62 EXPRESSION TAG SEQADV 9LU3 GLY B 174 UNP Q9IH62 EXPRESSION TAG SEQADV 9LU3 PRO B 175 UNP Q9IH62 EXPRESSION TAG SEQRES 1 A 441 HIS HIS HIS HIS HIS HIS LEU GLU VAL LEU PHE GLN GLY SEQRES 2 A 441 PRO GLU GLY VAL SER ASN LEU VAL GLY LEU PRO ASN ASN SEQRES 3 A 441 ILE CYS LEU GLN LYS THR SER ASN GLN ILE LEU LYS PRO SEQRES 4 A 441 LYS LEU ILE SER TYR THR LEU PRO VAL VAL GLY GLN SER SEQRES 5 A 441 GLY THR CYS ILE THR ASP PRO LEU LEU ALA MET ASP GLU SEQRES 6 A 441 GLY TYR PHE ALA TYR SER HIS LEU GLU ARG ILE GLY SER SEQRES 7 A 441 CYS SER ARG GLY VAL SER LYS GLN ARG ILE ILE GLY VAL SEQRES 8 A 441 GLY GLU VAL LEU ASP ARG GLY ASP GLU VAL PRO SER LEU SEQRES 9 A 441 PHE MET THR ASN VAL TRP THR PRO PRO ASN PRO ASN THR SEQRES 10 A 441 VAL TYR HIS CYS SER ALA VAL TYR ASN ASN GLU PHE TYR SEQRES 11 A 441 TYR VAL LEU CYS ALA VAL SER THR VAL GLY ASP PRO ILE SEQRES 12 A 441 LEU ASN SER THR TYR TRP SER GLY SER LEU MET MET THR SEQRES 13 A 441 ARG LEU ALA VAL LYS PRO LYS SER ASN GLY GLY GLY TYR SEQRES 14 A 441 ASN GLN HIS GLN LEU ALA LEU ARG SER ILE GLU LYS GLY SEQRES 15 A 441 ARG TYR ASP LYS VAL MET PRO TYR GLY PRO SER GLY ILE SEQRES 16 A 441 LYS GLN GLY ASP THR LEU TYR PHE PRO ALA VAL GLY PHE SEQRES 17 A 441 LEU VAL ARG THR GLU PHE LYS TYR ASN ASP SER ASN CYS SEQRES 18 A 441 PRO ILE THR LYS CYS GLN TYR SER LYS PRO GLU ASN CYS SEQRES 19 A 441 ARG LEU SER MET GLY ILE ARG PRO ASN SER HIS TYR ILE SEQRES 20 A 441 LEU ARG SER GLY LEU LEU LYS TYR ASN LEU SER ASP GLY SEQRES 21 A 441 GLU ASN PRO LYS VAL VAL PHE ILE GLU ILE SER ASP GLN SEQRES 22 A 441 ARG LEU SER ILE GLY SER PRO SER LYS ILE TYR ASP SER SEQRES 23 A 441 LEU GLY GLN PRO VAL PHE TYR GLN ALA SER PHE SER TRP SEQRES 24 A 441 ASP THR MET ILE LYS PHE GLY ASP VAL LEU THR VAL ASN SEQRES 25 A 441 PRO LEU VAL VAL ASN TRP ARG ASN ASN THR VAL ILE SER SEQRES 26 A 441 ARG PRO GLY GLN SER GLN CYS PRO ARG PHE ASN THR CYS SEQRES 27 A 441 PRO GLU ILE CYS TRP GLU GLY VAL TYR ASN ASP ALA PHE SEQRES 28 A 441 LEU ILE ASP ARG ILE ASN TRP ILE SER ALA GLY VAL PHE SEQRES 29 A 441 LEU ASP SER ASN GLN THR ALA GLU ASN PRO VAL PHE THR SEQRES 30 A 441 VAL PHE LYS ASP ASN GLU ILE LEU TYR ARG ALA GLN LEU SEQRES 31 A 441 ALA SER GLU ASP THR ASN ALA GLN LYS THR ILE THR ASN SEQRES 32 A 441 CYS PHE LEU LEU LYS ASN LYS ILE TRP CYS ILE SER LEU SEQRES 33 A 441 VAL GLU ILE TYR ASP THR GLY ASP ASN VAL ILE ARG PRO SEQRES 34 A 441 LYS LEU PHE ALA VAL LYS ILE PRO GLU GLN CYS THR SEQRES 1 H 234 GLU VAL LYS LEU VAL GLU SER GLY GLY GLY LEU VAL LYS SEQRES 2 H 234 PRO GLY GLY SER LEU LYS LEU SER CYS ALA ALA SER GLY SEQRES 3 H 234 PHE SER PHE ARG ASN TYR ALA MET SER TRP VAL ARG GLN SEQRES 4 H 234 SER PRO GLU LYS ARG LEU GLU TRP VAL ALA GLU VAL SER SEQRES 5 H 234 SER GLY GLY GLY TYR THR TYR TYR PRO ASP THR VAL THR SEQRES 6 H 234 GLY ARG PHE THR ILE SER ARG ASP ASN ALA LYS ASN ILE SEQRES 7 H 234 LEU TYR LEU GLU MET SER SER LEU ARG SER GLU ASP THR SEQRES 8 H 234 ALA MET TYR TYR CYS THR ARG ASP PRO ASP SER SER GLY SEQRES 9 H 234 TYR LEU ALA TRP PHE ALA TYR TRP GLY GLN GLY THR LEU SEQRES 10 H 234 VAL THR VAL SER ALA ALA SER THR LYS GLY PRO SER VAL SEQRES 11 H 234 PHE PRO LEU ALA PRO SER SER LYS SER THR SER GLY GLY SEQRES 12 H 234 THR ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO SEQRES 13 H 234 GLU PRO VAL THR VAL SER TRP ASN SER GLY ALA LEU THR SEQRES 14 H 234 SER GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SER SER SEQRES 15 H 234 GLY LEU TYR SER LEU SER SER VAL VAL THR VAL PRO SER SEQRES 16 H 234 SER SER LEU GLY THR GLN THR TYR ILE CYS ASN VAL ASN SEQRES 17 H 234 HIS LYS PRO SER ASN THR LYS VAL ASP LYS LYS VAL GLU SEQRES 18 H 234 PRO LYS SER CYS ASP LYS THR HIS HIS HIS HIS HIS HIS SEQRES 1 L 214 ASP ILE LEU LEU THR GLN SER PRO ALA SER LEU SER ALA SEQRES 2 L 214 SER VAL GLY GLU THR VAL THR ILE THR CYS ARG ALA SER SEQRES 3 L 214 GLU ASN ILE ASN SER TYR LEU ALA TRP TYR GLN GLN LYS SEQRES 4 L 214 GLN GLY LYS SER PRO GLN LEU LEU VAL TYR ASN ALA LYS SEQRES 5 L 214 THR LEU ALA GLU GLY VAL PRO SER ARG PHE SER GLY SER SEQRES 6 L 214 GLY SER ASP THR GLN PHE SER LEU LYS ILE ASN THR LEU SEQRES 7 L 214 GLN PRO GLU ASP PHE GLY THR TYR TYR CYS GLN HIS HIS SEQRES 8 L 214 SER GLY THR PRO TYR THR PHE GLY GLY GLY THR LYS LEU SEQRES 9 L 214 GLU ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE ILE SEQRES 10 L 214 PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR ALA SEQRES 11 L 214 SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG GLU SEQRES 12 L 214 ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SER SEQRES 13 L 214 GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER LYS SEQRES 14 L 214 ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SER SEQRES 15 L 214 LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS GLU SEQRES 16 L 214 VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SER SEQRES 17 L 214 PHE ASN ARG GLY GLU CYS SEQRES 1 B 441 HIS HIS HIS HIS HIS HIS LEU GLU VAL LEU PHE GLN GLY SEQRES 2 B 441 PRO GLU GLY VAL SER ASN LEU VAL GLY LEU PRO ASN ASN SEQRES 3 B 441 ILE CYS LEU GLN LYS THR SER ASN GLN ILE LEU LYS PRO SEQRES 4 B 441 LYS LEU ILE SER TYR THR LEU PRO VAL VAL GLY GLN SER SEQRES 5 B 441 GLY THR CYS ILE THR ASP PRO LEU LEU ALA MET ASP GLU SEQRES 6 B 441 GLY TYR PHE ALA TYR SER HIS LEU GLU ARG ILE GLY SER SEQRES 7 B 441 CYS SER ARG GLY VAL SER LYS GLN ARG ILE ILE GLY VAL SEQRES 8 B 441 GLY GLU VAL LEU ASP ARG GLY ASP GLU VAL PRO SER LEU SEQRES 9 B 441 PHE MET THR ASN VAL TRP THR PRO PRO ASN PRO ASN THR SEQRES 10 B 441 VAL TYR HIS CYS SER ALA VAL TYR ASN ASN GLU PHE TYR SEQRES 11 B 441 TYR VAL LEU CYS ALA VAL SER THR VAL GLY ASP PRO ILE SEQRES 12 B 441 LEU ASN SER THR TYR TRP SER GLY SER LEU MET MET THR SEQRES 13 B 441 ARG LEU ALA VAL LYS PRO LYS SER ASN GLY GLY GLY TYR SEQRES 14 B 441 ASN GLN HIS GLN LEU ALA LEU ARG SER ILE GLU LYS GLY SEQRES 15 B 441 ARG TYR ASP LYS VAL MET PRO TYR GLY PRO SER GLY ILE SEQRES 16 B 441 LYS GLN GLY ASP THR LEU TYR PHE PRO ALA VAL GLY PHE SEQRES 17 B 441 LEU VAL ARG THR GLU PHE LYS TYR ASN ASP SER ASN CYS SEQRES 18 B 441 PRO ILE THR LYS CYS GLN TYR SER LYS PRO GLU ASN CYS SEQRES 19 B 441 ARG LEU SER MET GLY ILE ARG PRO ASN SER HIS TYR ILE SEQRES 20 B 441 LEU ARG SER GLY LEU LEU LYS TYR ASN LEU SER ASP GLY SEQRES 21 B 441 GLU ASN PRO LYS VAL VAL PHE ILE GLU ILE SER ASP GLN SEQRES 22 B 441 ARG LEU SER ILE GLY SER PRO SER LYS ILE TYR ASP SER SEQRES 23 B 441 LEU GLY GLN PRO VAL PHE TYR GLN ALA SER PHE SER TRP SEQRES 24 B 441 ASP THR MET ILE LYS PHE GLY ASP VAL LEU THR VAL ASN SEQRES 25 B 441 PRO LEU VAL VAL ASN TRP ARG ASN ASN THR VAL ILE SER SEQRES 26 B 441 ARG PRO GLY GLN SER GLN CYS PRO ARG PHE ASN THR CYS SEQRES 27 B 441 PRO GLU ILE CYS TRP GLU GLY VAL TYR ASN ASP ALA PHE SEQRES 28 B 441 LEU ILE ASP ARG ILE ASN TRP ILE SER ALA GLY VAL PHE SEQRES 29 B 441 LEU ASP SER ASN GLN THR ALA GLU ASN PRO VAL PHE THR SEQRES 30 B 441 VAL PHE LYS ASP ASN GLU ILE LEU TYR ARG ALA GLN LEU SEQRES 31 B 441 ALA SER GLU ASP THR ASN ALA GLN LYS THR ILE THR ASN SEQRES 32 B 441 CYS PHE LEU LEU LYS ASN LYS ILE TRP CYS ILE SER LEU SEQRES 33 B 441 VAL GLU ILE TYR ASP THR GLY ASP ASN VAL ILE ARG PRO SEQRES 34 B 441 LYS LEU PHE ALA VAL LYS ILE PRO GLU GLN CYS THR SEQRES 1 D 234 GLU VAL LYS LEU VAL GLU SER GLY GLY GLY LEU VAL LYS SEQRES 2 D 234 PRO GLY GLY SER LEU LYS LEU SER CYS ALA ALA SER GLY SEQRES 3 D 234 PHE SER PHE ARG ASN TYR ALA MET SER TRP VAL ARG GLN SEQRES 4 D 234 SER PRO GLU LYS ARG LEU GLU TRP VAL ALA GLU VAL SER SEQRES 5 D 234 SER GLY GLY GLY TYR THR TYR TYR PRO ASP THR VAL THR SEQRES 6 D 234 GLY ARG PHE THR ILE SER ARG ASP ASN ALA LYS ASN ILE SEQRES 7 D 234 LEU TYR LEU GLU MET SER SER LEU ARG SER GLU ASP THR SEQRES 8 D 234 ALA MET TYR TYR CYS THR ARG ASP PRO ASP SER SER GLY SEQRES 9 D 234 TYR LEU ALA TRP PHE ALA TYR TRP GLY GLN GLY THR LEU SEQRES 10 D 234 VAL THR VAL SER ALA ALA SER THR LYS GLY PRO SER VAL SEQRES 11 D 234 PHE PRO LEU ALA PRO SER SER LYS SER THR SER GLY GLY SEQRES 12 D 234 THR ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO SEQRES 13 D 234 GLU PRO VAL THR VAL SER TRP ASN SER GLY ALA LEU THR SEQRES 14 D 234 SER GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SER SER SEQRES 15 D 234 GLY LEU TYR SER LEU SER SER VAL VAL THR VAL PRO SER SEQRES 16 D 234 SER SER LEU GLY THR GLN THR TYR ILE CYS ASN VAL ASN SEQRES 17 D 234 HIS LYS PRO SER ASN THR LYS VAL ASP LYS LYS VAL GLU SEQRES 18 D 234 PRO LYS SER CYS ASP LYS THR HIS HIS HIS HIS HIS HIS SEQRES 1 E 214 ASP ILE LEU LEU THR GLN SER PRO ALA SER LEU SER ALA SEQRES 2 E 214 SER VAL GLY GLU THR VAL THR ILE THR CYS ARG ALA SER SEQRES 3 E 214 GLU ASN ILE ASN SER TYR LEU ALA TRP TYR GLN GLN LYS SEQRES 4 E 214 GLN GLY LYS SER PRO GLN LEU LEU VAL TYR ASN ALA LYS SEQRES 5 E 214 THR LEU ALA GLU GLY VAL PRO SER ARG PHE SER GLY SER SEQRES 6 E 214 GLY SER ASP THR GLN PHE SER LEU LYS ILE ASN THR LEU SEQRES 7 E 214 GLN PRO GLU ASP PHE GLY THR TYR TYR CYS GLN HIS HIS SEQRES 8 E 214 SER GLY THR PRO TYR THR PHE GLY GLY GLY THR LYS LEU SEQRES 9 E 214 GLU ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE ILE SEQRES 10 E 214 PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR ALA SEQRES 11 E 214 SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG GLU SEQRES 12 E 214 ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SER SEQRES 13 E 214 GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER LYS SEQRES 14 E 214 ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SER SEQRES 15 E 214 LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS GLU SEQRES 16 E 214 VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SER SEQRES 17 E 214 PHE ASN ARG GLY GLU CYS HET NAG A 701 14 HET NAG A 702 14 HET NAG A 703 14 HET NAG A 704 14 HET NAG A 705 14 HET NAG B 701 14 HET NAG B 702 14 HET NAG B 703 14 HET NAG B 704 14 HET NAG B 705 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 7 NAG 10(C8 H15 N O6) HELIX 1 AA1 SER A 204 LEU A 207 5 4 HELIX 2 AA2 ASN A 275 ASN A 277 5 3 HELIX 3 AA3 ASN A 306 TRP A 310 5 5 HELIX 4 AA4 GLY A 327 TYR A 330 5 4 HELIX 5 AA5 THR A 373 PHE A 375 5 3 HELIX 6 AA6 ASN A 378 CYS A 382 5 5 HELIX 7 AA7 GLU A 393 SER A 398 1 6 HELIX 8 AA8 SER H 28 TYR H 32 5 5 HELIX 9 AA9 PRO H 60 THR H 64 5 5 HELIX 10 AB1 ARG H 83 THR H 87 5 5 HELIX 11 AB2 SER H 156 ALA H 158 5 3 HELIX 12 AB3 SER H 187 GLY H 190 5 4 HELIX 13 AB4 GLN L 79 PHE L 83 5 5 HELIX 14 AB5 SER L 121 GLY L 128 1 8 HELIX 15 AB6 LYS L 183 HIS L 189 1 7 HELIX 16 AB7 SER B 204 LEU B 207 5 4 HELIX 17 AB8 ASN B 275 ASN B 277 5 3 HELIX 18 AB9 ASN B 306 TRP B 310 5 5 HELIX 19 AC1 GLY B 327 ASN B 331 1 5 HELIX 20 AC2 THR B 373 PHE B 375 5 3 HELIX 21 AC3 ASN B 378 CYS B 382 5 5 HELIX 22 AC4 GLU B 393 SER B 398 1 6 HELIX 23 AC5 SER D 28 TYR D 32 5 5 HELIX 24 AC6 PRO D 60 THR D 64 5 5 HELIX 25 AC7 ARG D 83 THR D 87 5 5 HELIX 26 AC8 THR D 131 GLY D 133 5 3 HELIX 27 AC9 SER D 156 ALA D 158 5 3 HELIX 28 AD1 SER D 187 LEU D 189 5 3 HELIX 29 AD2 GLN E 79 PHE E 83 5 5 HELIX 30 AD3 SER E 121 LYS E 126 1 6 HELIX 31 AD4 LYS E 183 LYS E 188 1 6 SHEET 1 AA1 5 VAL A 178 SER A 179 0 SHEET 2 AA1 5 THR A 561 LEU A 568 -1 O LEU A 567 N SER A 179 SHEET 3 AA1 5 LYS A 571 ILE A 580 -1 O ILE A 575 N ASN A 564 SHEET 4 AA1 5 ARG A 589 LYS A 596 -1 O PHE A 593 N SER A 576 SHEET 5 AA1 5 LYS A 201 LEU A 202 -1 N LYS A 201 O ALA A 594 SHEET 1 AA2 4 CYS A 216 ASP A 225 0 SHEET 2 AA2 4 TYR A 228 ILE A 237 -1 O ALA A 230 N ALA A 223 SHEET 3 AA2 4 VAL A 244 ASP A 257 -1 O GLY A 251 N TYR A 231 SHEET 4 AA2 4 PRO A 263 TRP A 271 -1 O THR A 268 N VAL A 252 SHEET 1 AA3 4 VAL A 279 TYR A 286 0 SHEET 2 AA3 4 PHE A 290 VAL A 297 -1 O ALA A 296 N TYR A 280 SHEET 3 AA3 4 LEU A 314 ALA A 320 -1 O LEU A 319 N TYR A 291 SHEET 4 AA3 4 GLN A 332 LEU A 335 -1 O HIS A 333 N ARG A 318 SHEET 1 AA4 5 ILE A 340 GLU A 341 0 SHEET 2 AA4 5 VAL A 426 GLU A 430 1 O VAL A 426 N GLU A 341 SHEET 3 AA4 5 TYR A 407 ASN A 417 -1 N LEU A 413 O ILE A 429 SHEET 4 AA4 5 THR A 361 VAL A 371 -1 N ALA A 366 O GLY A 412 SHEET 5 AA4 5 LYS A 347 PRO A 350 -1 N LYS A 347 O PHE A 369 SHEET 1 AA5 5 ILE A 340 GLU A 341 0 SHEET 2 AA5 5 VAL A 426 GLU A 430 1 O VAL A 426 N GLU A 341 SHEET 3 AA5 5 TYR A 407 ASN A 417 -1 N LEU A 413 O ILE A 429 SHEET 4 AA5 5 THR A 361 VAL A 371 -1 N ALA A 366 O GLY A 412 SHEET 5 AA5 5 ILE A 356 GLN A 358 -1 N ILE A 356 O TYR A 363 SHEET 1 AA6 4 SER A 442 SER A 447 0 SHEET 2 AA6 4 GLN A 450 GLN A 455 -1 O VAL A 452 N TYR A 445 SHEET 3 AA6 4 LYS A 465 THR A 471 -1 O VAL A 469 N PRO A 451 SHEET 4 AA6 4 VAL A 476 VAL A 477 -1 O VAL A 476 N LEU A 470 SHEET 1 AA7 4 ALA A 511 ASP A 515 0 SHEET 2 AA7 4 ILE A 520 LEU A 526 -1 O ALA A 522 N PHE A 512 SHEET 3 AA7 4 PRO A 535 PHE A 540 -1 O PHE A 540 N SER A 521 SHEET 4 AA7 4 ILE A 545 GLN A 550 -1 O LEU A 546 N VAL A 539 SHEET 1 AA8 4 LYS H 3 SER H 7 0 SHEET 2 AA8 4 LEU H 18 SER H 25 -1 O SER H 25 N LYS H 3 SHEET 3 AA8 4 ILE H 77 MET H 82 -1 O LEU H 78 N CYS H 22 SHEET 4 AA8 4 PHE H 67 ASP H 72 -1 N THR H 68 O GLU H 81 SHEET 1 AA9 6 LEU H 11 VAL H 12 0 SHEET 2 AA9 6 THR H 107 VAL H 111 1 O THR H 110 N VAL H 12 SHEET 3 AA9 6 ALA H 88 ARG H 94 -1 N TYR H 90 O THR H 107 SHEET 4 AA9 6 MET H 34 GLN H 39 -1 N VAL H 37 O TYR H 91 SHEET 5 AA9 6 LEU H 45 VAL H 51 -1 O GLU H 46 N ARG H 38 SHEET 6 AA9 6 THR H 57 TYR H 58 -1 O TYR H 58 N GLU H 50 SHEET 1 AB1 4 LEU H 11 VAL H 12 0 SHEET 2 AB1 4 THR H 107 VAL H 111 1 O THR H 110 N VAL H 12 SHEET 3 AB1 4 ALA H 88 ARG H 94 -1 N TYR H 90 O THR H 107 SHEET 4 AB1 4 TYR H 102 TRP H 103 -1 O TYR H 102 N ARG H 94 SHEET 1 AB2 4 SER H 120 LEU H 124 0 SHEET 2 AB2 4 THR H 135 TYR H 145 -1 O GLY H 139 N LEU H 124 SHEET 3 AB2 4 TYR H 176 PRO H 185 -1 O VAL H 184 N ALA H 136 SHEET 4 AB2 4 VAL H 163 THR H 165 -1 N HIS H 164 O VAL H 181 SHEET 1 AB3 4 THR H 131 SER H 132 0 SHEET 2 AB3 4 THR H 135 TYR H 145 -1 O THR H 135 N SER H 132 SHEET 3 AB3 4 TYR H 176 PRO H 185 -1 O VAL H 184 N ALA H 136 SHEET 4 AB3 4 VAL H 169 LEU H 170 -1 N VAL H 169 O SER H 177 SHEET 1 AB4 3 THR H 151 TRP H 154 0 SHEET 2 AB4 3 TYR H 194 HIS H 200 -1 O ASN H 197 N SER H 153 SHEET 3 AB4 3 THR H 205 VAL H 211 -1 O VAL H 211 N TYR H 194 SHEET 1 AB5 4 LEU L 4 SER L 7 0 SHEET 2 AB5 4 VAL L 19 ALA L 25 -1 O THR L 22 N SER L 7 SHEET 3 AB5 4 GLN L 70 ILE L 75 -1 O ILE L 75 N VAL L 19 SHEET 4 AB5 4 PHE L 62 SER L 67 -1 N SER L 63 O LYS L 74 SHEET 1 AB6 6 SER L 10 SER L 14 0 SHEET 2 AB6 6 THR L 102 LYS L 107 1 O GLU L 105 N LEU L 11 SHEET 3 AB6 6 GLY L 84 HIS L 90 -1 N GLY L 84 O LEU L 104 SHEET 4 AB6 6 LEU L 33 GLN L 38 -1 N ALA L 34 O GLN L 89 SHEET 5 AB6 6 GLN L 45 TYR L 49 -1 O VAL L 48 N TRP L 35 SHEET 6 AB6 6 THR L 53 LEU L 54 -1 O THR L 53 N TYR L 49 SHEET 1 AB7 4 SER L 10 SER L 14 0 SHEET 2 AB7 4 THR L 102 LYS L 107 1 O GLU L 105 N LEU L 11 SHEET 3 AB7 4 GLY L 84 HIS L 90 -1 N GLY L 84 O LEU L 104 SHEET 4 AB7 4 THR L 97 PHE L 98 -1 O THR L 97 N HIS L 90 SHEET 1 AB8 4 SER L 114 PHE L 118 0 SHEET 2 AB8 4 THR L 129 PHE L 139 -1 O VAL L 133 N PHE L 118 SHEET 3 AB8 4 TYR L 173 SER L 182 -1 O LEU L 179 N VAL L 132 SHEET 4 AB8 4 SER L 159 VAL L 163 -1 N SER L 162 O SER L 176 SHEET 1 AB9 4 ALA L 153 LEU L 154 0 SHEET 2 AB9 4 ALA L 144 VAL L 150 -1 N VAL L 150 O ALA L 153 SHEET 3 AB9 4 VAL L 191 HIS L 198 -1 O GLU L 195 N GLN L 147 SHEET 4 AB9 4 VAL L 205 ASN L 210 -1 O VAL L 205 N VAL L 196 SHEET 1 AC1 5 VAL B 178 ASN B 180 0 SHEET 2 AC1 5 THR B 561 LEU B 568 -1 O LEU B 567 N SER B 179 SHEET 3 AC1 5 LYS B 571 GLU B 579 -1 O LEU B 577 N ILE B 562 SHEET 4 AC1 5 PRO B 590 LYS B 596 -1 O VAL B 595 N CYS B 574 SHEET 5 AC1 5 LYS B 201 LEU B 202 -1 N LYS B 201 O ALA B 594 SHEET 1 AC2 4 ILE B 217 ASP B 225 0 SHEET 2 AC2 4 TYR B 228 ILE B 237 -1 O ALA B 230 N ALA B 223 SHEET 3 AC2 4 VAL B 244 ASP B 257 -1 O GLY B 251 N TYR B 231 SHEET 4 AC2 4 PRO B 263 TRP B 271 -1 O TRP B 271 N ILE B 250 SHEET 1 AC3 4 VAL B 279 TYR B 286 0 SHEET 2 AC3 4 PHE B 290 VAL B 297 -1 O ALA B 296 N TYR B 280 SHEET 3 AC3 4 LEU B 314 ALA B 320 -1 O MET B 315 N CYS B 295 SHEET 4 AC3 4 GLN B 332 LEU B 335 -1 O HIS B 333 N ARG B 318 SHEET 1 AC4 5 ILE B 340 GLU B 341 0 SHEET 2 AC4 5 VAL B 426 GLU B 430 1 O VAL B 426 N GLU B 341 SHEET 3 AC4 5 TYR B 407 ASN B 417 -1 N LYS B 415 O VAL B 427 SHEET 4 AC4 5 THR B 361 VAL B 371 -1 N ALA B 366 O GLY B 412 SHEET 5 AC4 5 LYS B 347 PRO B 350 -1 N LYS B 347 O PHE B 369 SHEET 1 AC5 5 ILE B 340 GLU B 341 0 SHEET 2 AC5 5 VAL B 426 GLU B 430 1 O VAL B 426 N GLU B 341 SHEET 3 AC5 5 TYR B 407 ASN B 417 -1 N LYS B 415 O VAL B 427 SHEET 4 AC5 5 THR B 361 VAL B 371 -1 N ALA B 366 O GLY B 412 SHEET 5 AC5 5 ILE B 356 LYS B 357 -1 N ILE B 356 O TYR B 363 SHEET 1 AC6 4 SER B 442 SER B 447 0 SHEET 2 AC6 4 GLN B 450 GLN B 455 -1 O TYR B 454 N LYS B 443 SHEET 3 AC6 4 LYS B 465 THR B 471 -1 O GLY B 467 N PHE B 453 SHEET 4 AC6 4 VAL B 476 TRP B 479 -1 O VAL B 476 N LEU B 470 SHEET 1 AC7 4 ALA B 511 ASP B 515 0 SHEET 2 AC7 4 ILE B 520 LEU B 526 -1 O ALA B 522 N PHE B 512 SHEET 3 AC7 4 PRO B 535 PHE B 540 -1 O THR B 538 N GLY B 523 SHEET 4 AC7 4 ILE B 545 GLN B 550 -1 O LEU B 546 N VAL B 539 SHEET 1 AC8 4 LYS D 3 SER D 7 0 SHEET 2 AC8 4 LEU D 18 SER D 25 -1 O SER D 25 N LYS D 3 SHEET 3 AC8 4 ILE D 77 MET D 82 -1 O MET D 82 N LEU D 18 SHEET 4 AC8 4 PHE D 67 ASP D 72 -1 N ASP D 72 O ILE D 77 SHEET 1 AC9 6 LEU D 11 VAL D 12 0 SHEET 2 AC9 6 THR D 107 VAL D 111 1 O THR D 110 N VAL D 12 SHEET 3 AC9 6 ALA D 88 ARG D 94 -1 N TYR D 90 O THR D 107 SHEET 4 AC9 6 MET D 34 GLN D 39 -1 N SER D 35 O THR D 93 SHEET 5 AC9 6 LEU D 45 VAL D 51 -1 O GLU D 46 N ARG D 38 SHEET 6 AC9 6 THR D 57 TYR D 58 -1 O TYR D 58 N GLU D 50 SHEET 1 AD1 4 LEU D 11 VAL D 12 0 SHEET 2 AD1 4 THR D 107 VAL D 111 1 O THR D 110 N VAL D 12 SHEET 3 AD1 4 ALA D 88 ARG D 94 -1 N TYR D 90 O THR D 107 SHEET 4 AD1 4 TYR D 102 TRP D 103 -1 O TYR D 102 N ARG D 94 SHEET 1 AD2 4 SER D 120 LEU D 124 0 SHEET 2 AD2 4 THR D 135 TYR D 145 -1 O LYS D 143 N SER D 120 SHEET 3 AD2 4 TYR D 176 PRO D 185 -1 O VAL D 182 N LEU D 138 SHEET 4 AD2 4 VAL D 163 THR D 165 -1 N HIS D 164 O VAL D 181 SHEET 1 AD3 4 SER D 120 LEU D 124 0 SHEET 2 AD3 4 THR D 135 TYR D 145 -1 O LYS D 143 N SER D 120 SHEET 3 AD3 4 TYR D 176 PRO D 185 -1 O VAL D 182 N LEU D 138 SHEET 4 AD3 4 VAL D 169 LEU D 170 -1 N VAL D 169 O SER D 177 SHEET 1 AD4 3 THR D 151 TRP D 154 0 SHEET 2 AD4 3 TYR D 194 HIS D 200 -1 O ASN D 199 N THR D 151 SHEET 3 AD4 3 THR D 205 VAL D 211 -1 O VAL D 211 N TYR D 194 SHEET 1 AD5 4 LEU E 4 SER E 7 0 SHEET 2 AD5 4 VAL E 19 ALA E 25 -1 O THR E 22 N SER E 7 SHEET 3 AD5 4 GLN E 70 ILE E 75 -1 O ILE E 75 N VAL E 19 SHEET 4 AD5 4 PHE E 62 SER E 67 -1 N SER E 63 O LYS E 74 SHEET 1 AD6 6 SER E 10 SER E 14 0 SHEET 2 AD6 6 THR E 102 LYS E 107 1 O LYS E 107 N ALA E 13 SHEET 3 AD6 6 GLY E 84 HIS E 90 -1 N GLY E 84 O LEU E 104 SHEET 4 AD6 6 LEU E 33 GLN E 38 -1 N ALA E 34 O GLN E 89 SHEET 5 AD6 6 GLN E 45 TYR E 49 -1 O VAL E 48 N TRP E 35 SHEET 6 AD6 6 THR E 53 LEU E 54 -1 O THR E 53 N TYR E 49 SHEET 1 AD7 4 SER E 114 PHE E 118 0 SHEET 2 AD7 4 THR E 129 PHE E 139 -1 O VAL E 133 N PHE E 118 SHEET 3 AD7 4 TYR E 173 SER E 182 -1 O LEU E 175 N LEU E 136 SHEET 4 AD7 4 SER E 159 VAL E 163 -1 N SER E 162 O SER E 176 SHEET 1 AD8 3 LYS E 145 VAL E 150 0 SHEET 2 AD8 3 TYR E 192 THR E 197 -1 O GLU E 195 N GLN E 147 SHEET 3 AD8 3 VAL E 205 PHE E 209 -1 O LYS E 207 N CYS E 194 SSBOND 1 CYS A 189 CYS A 601 1555 1555 2.05 SSBOND 2 CYS A 216 CYS A 240 1555 1555 2.05 SSBOND 3 CYS A 282 CYS A 295 1555 1555 2.06 SSBOND 4 CYS A 382 CYS A 395 1555 1555 2.06 SSBOND 5 CYS A 387 CYS A 499 1555 1555 2.05 SSBOND 6 CYS A 493 CYS A 503 1555 1555 2.04 SSBOND 7 CYS A 565 CYS A 574 1555 1555 2.06 SSBOND 8 CYS H 22 CYS H 92 1555 1555 2.07 SSBOND 9 CYS H 140 CYS H 196 1555 1555 2.05 SSBOND 10 CYS L 23 CYS L 88 1555 1555 2.09 SSBOND 11 CYS L 134 CYS L 194 1555 1555 2.02 SSBOND 12 CYS B 189 CYS B 601 1555 1555 2.05 SSBOND 13 CYS B 216 CYS B 240 1555 1555 2.05 SSBOND 14 CYS B 282 CYS B 295 1555 1555 2.07 SSBOND 15 CYS B 382 CYS B 395 1555 1555 2.08 SSBOND 16 CYS B 387 CYS B 499 1555 1555 2.06 SSBOND 17 CYS B 493 CYS B 503 1555 1555 2.03 SSBOND 18 CYS B 565 CYS B 574 1555 1555 2.06 SSBOND 19 CYS D 22 CYS D 92 1555 1555 2.04 SSBOND 20 CYS D 140 CYS D 196 1555 1555 2.03 SSBOND 21 CYS E 23 CYS E 88 1555 1555 2.06 SSBOND 22 CYS E 134 CYS E 194 1555 1555 2.03 LINK ND2 ASN A 306 C1 NAG A 704 1555 1555 1.44 LINK ND2 ASN A 378 C1 NAG A 705 1555 1555 1.43 LINK ND2 ASN A 417 C1 NAG A 701 1555 1555 1.45 LINK ND2 ASN A 481 C1 NAG A 703 1555 1555 1.45 LINK ND2 ASN A 529 C1 NAG A 702 1555 1555 1.46 LINK ND2 ASN B 306 C1 NAG B 704 1555 1555 1.43 LINK ND2 ASN B 378 C1 NAG B 705 1555 1555 1.43 LINK ND2 ASN B 417 C1 NAG B 701 1555 1555 1.44 LINK ND2 ASN B 481 C1 NAG B 703 1555 1555 1.44 LINK ND2 ASN B 529 C1 NAG B 702 1555 1555 1.46 CISPEP 1 ASN A 473 PRO A 474 0 1.19 CISPEP 2 PHE H 146 PRO H 147 0 -8.07 CISPEP 3 GLU H 148 PRO H 149 0 0.05 CISPEP 4 SER L 7 PRO L 8 0 -1.91 CISPEP 5 THR L 94 PRO L 95 0 -4.34 CISPEP 6 TYR L 140 PRO L 141 0 -2.56 CISPEP 7 ASN B 473 PRO B 474 0 -10.53 CISPEP 8 PHE D 146 PRO D 147 0 -1.72 CISPEP 9 GLU D 148 PRO D 149 0 7.93 CISPEP 10 SER E 7 PRO E 8 0 0.87 CISPEP 11 THR E 94 PRO E 95 0 4.31 CISPEP 12 TYR E 140 PRO E 141 0 5.90 CRYST1 123.416 125.155 152.376 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 0.008103 0.000000 0.000000 0.00000 SCALE2 0.000000 0.007990 0.000000 0.00000 SCALE3 0.000000 0.000000 0.006563 0.00000