HEADER ANTITUMOR PROTEIN 27-SEP-24 9GWT TITLE CRYSTAL STRUCTURE OF 23ME-00610 FAB IN COMPLEX WITH HUMAN CD200R1 COMPND MOL_ID: 1; COMPND 2 MOLECULE: 23ME-00610 FAB (HEAVY); COMPND 3 CHAIN: H; COMPND 4 SYNONYM: 23ME-00610 FAB; COMPND 5 ENGINEERED: YES; COMPND 6 OTHER_DETAILS: FAB HEAVY CHAIN; COMPND 7 MOL_ID: 2; COMPND 8 MOLECULE: 23ME-00610 FAB (LIGHT); COMPND 9 CHAIN: L; COMPND 10 SYNONYM: 23ME-00610 FAB; COMPND 11 ENGINEERED: YES; COMPND 12 OTHER_DETAILS: FAB LIGHT CHAIN; COMPND 13 MOL_ID: 3; COMPND 14 MOLECULE: ISOFORM 1 OF CELL SURFACE GLYCOPROTEIN CD200 RECEPTOR 1; COMPND 15 CHAIN: P; COMPND 16 SYNONYM: CD200 CELL SURFACE GLYCOPROTEIN RECEPTOR,CELL SURFACE COMPND 17 GLYCOPROTEIN OX2 RECEPTOR 1; COMPND 18 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_TAXID: 9606; SOURCE 4 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 5 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 6 EXPRESSION_SYSTEM_CELL_LINE: EXPI293; SOURCE 7 MOL_ID: 2; SOURCE 8 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 9 ORGANISM_TAXID: 9606; SOURCE 10 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 11 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 12 MOL_ID: 3; SOURCE 13 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 14 ORGANISM_COMMON: HUMAN; SOURCE 15 ORGANISM_TAXID: 9606; SOURCE 16 GENE: CD200R1, CD200R, CRTR2, MOX2R, OX2R, UNQ2522/PRO6015; SOURCE 17 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 18 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 19 EXPRESSION_SYSTEM_CELL_LINE: EXPI293 KEYWDS 23ME-00610, HUMAN CD200R1, IMMUNE CHECKPOINT INHIBITOR, IMMUNO- KEYWDS 2 ONCOLOGY, ANTITUMOR PROTEIN EXPDTA X-RAY DIFFRACTION AUTHOR Y.M.HUANG,O.M.GANICHKIN REVDAT 1 23-OCT-24 9GWT 0 JRNL AUTH C.MELERO,S.J.BUDIARDJO,A.DARUWALLA,L.LARRABEE,O.GANICHKIN, JRNL AUTH 2 A.J.HEILER,J.FENAUX,B.CHUNG,G.FUH,Y.M.HUANG JRNL TITL CD200R1 IMMUNE CHECKPOINT BLOCKADE BY THE FIRST-IN-HUMAN JRNL TITL 2 ANTI-CD200R1 ANTIBODY 23ME-00610: MOLECULAR MECHANISM AND JRNL TITL 3 ENGINEERING OF A SURROGATE ANTIBODY. JRNL REF MABS V. 16 10316 2024 JRNL REFN ESSN 1942-0870 JRNL PMID 39402718 JRNL DOI 10.1080/19420862.2024.2410316 REMARK 2 REMARK 2 RESOLUTION. 2.89 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : REFMAC 5.8.0352 REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER, REMARK 3 : NICHOLLS,WINN,LONG,VAGIN REMARK 3 REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.89 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 93.03 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000 REMARK 3 COMPLETENESS FOR RANGE (%) : 86.0 REMARK 3 NUMBER OF REFLECTIONS : 26177 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) : 0.204 REMARK 3 R VALUE (WORKING SET) : 0.202 REMARK 3 FREE R VALUE : 0.236 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900 REMARK 3 FREE R VALUE TEST SET COUNT : 1362 REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : NULL REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.89 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.96 REMARK 3 REFLECTION IN BIN (WORKING SET) : 141 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 6.32 REMARK 3 BIN R VALUE (WORKING SET) : 0.3380 REMARK 3 BIN FREE R VALUE SET COUNT : 4 REMARK 3 BIN FREE R VALUE : 0.2580 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 4845 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 234 REMARK 3 SOLVENT ATOMS : 25 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 108.5 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 0.82000 REMARK 3 B22 (A**2) : 0.82000 REMARK 3 B33 (A**2) : -1.64000 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 OVERALL COORDINATE ERROR. REMARK 3 ESU BASED ON R VALUE (A): 0.570 REMARK 3 ESU BASED ON FREE R VALUE (A): 0.320 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.242 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 28.716 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.948 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.933 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 5151 ; 0.003 ; 0.012 REMARK 3 BOND LENGTHS OTHERS (A): 4511 ; 0.021 ; 0.016 REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 7071 ; 0.951 ; 1.670 REMARK 3 BOND ANGLES OTHERS (DEGREES): 10577 ; 0.577 ; 1.558 REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 634 ; 7.171 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 17 ; 1.955 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 717 ;11.800 ;10.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 871 ; 0.045 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5615 ; 0.003 ; 0.020 REMARK 3 GENERAL PLANES OTHERS (A): 934 ; 0.001 ; 0.020 REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL REMARK 3 REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 2539 ; 1.867 ; 7.023 REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 2539 ; 1.866 ; 7.023 REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3172 ; 3.119 ;10.526 REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 REMARK 3 NCS RESTRAINTS STATISTICS REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 6 REMARK 3 REMARK 3 TLS GROUP : 1 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : L 1 L 111 REMARK 3 ORIGIN FOR THE GROUP (A): -12.0740 30.1800 15.8540 REMARK 3 T TENSOR REMARK 3 T11: 0.0327 T22: 0.2949 REMARK 3 T33: 0.2494 T12: -0.0022 REMARK 3 T13: -0.0192 T23: 0.0652 REMARK 3 L TENSOR REMARK 3 L11: 2.7736 L22: 3.0701 REMARK 3 L33: 3.4428 L12: 0.5870 REMARK 3 L13: 0.1476 L23: 0.9924 REMARK 3 S TENSOR REMARK 3 S11: -0.0753 S12: -0.2357 S13: -0.0565 REMARK 3 S21: -0.1050 S22: 0.0466 S23: 0.1942 REMARK 3 S31: 0.0189 S32: -0.0531 S33: 0.0288 REMARK 3 REMARK 3 TLS GROUP : 2 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : L 112 L 255 REMARK 3 ORIGIN FOR THE GROUP (A): -7.9990 19.2440 -20.2720 REMARK 3 T TENSOR REMARK 3 T11: 0.4934 T22: 0.1516 REMARK 3 T33: 0.4208 T12: -0.0491 REMARK 3 T13: -0.1112 T23: -0.0256 REMARK 3 L TENSOR REMARK 3 L11: 4.8808 L22: 1.7125 REMARK 3 L33: 6.7089 L12: 0.4576 REMARK 3 L13: -3.3059 L23: -0.1705 REMARK 3 S TENSOR REMARK 3 S11: -0.1779 S12: 0.2674 S13: -0.7355 REMARK 3 S21: -0.5045 S22: -0.0767 S23: -0.1254 REMARK 3 S31: 0.5930 S32: -0.1692 S33: 0.2547 REMARK 3 REMARK 3 TLS GROUP : 3 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : H 1 H 119 REMARK 3 ORIGIN FOR THE GROUP (A): 3.3970 44.9860 9.3300 REMARK 3 T TENSOR REMARK 3 T11: 0.2006 T22: 0.3424 REMARK 3 T33: 0.2721 T12: -0.1245 REMARK 3 T13: -0.0890 T23: 0.0294 REMARK 3 L TENSOR REMARK 3 L11: 4.8895 L22: 2.9805 REMARK 3 L33: 5.8175 L12: 0.1459 REMARK 3 L13: -2.0384 L23: 0.7278 REMARK 3 S TENSOR REMARK 3 S11: 0.1196 S12: -0.3855 S13: 0.5901 REMARK 3 S21: -0.0517 S22: -0.0182 S23: -0.0788 REMARK 3 S31: -0.5841 S32: 0.4098 S33: -0.1013 REMARK 3 REMARK 3 TLS GROUP : 4 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : H 120 H 300 REMARK 3 ORIGIN FOR THE GROUP (A): -6.9340 35.5790 -18.5230 REMARK 3 T TENSOR REMARK 3 T11: 0.3441 T22: 0.0937 REMARK 3 T33: 0.1704 T12: -0.0481 REMARK 3 T13: -0.0709 T23: 0.0014 REMARK 3 L TENSOR REMARK 3 L11: 6.5370 L22: 3.3743 REMARK 3 L33: 3.6154 L12: 1.0532 REMARK 3 L13: 0.8721 L23: -0.4117 REMARK 3 S TENSOR REMARK 3 S11: -0.0231 S12: 0.2475 S13: 0.0281 REMARK 3 S21: -0.4894 S22: -0.0887 S23: 0.2745 REMARK 3 S31: 0.0872 S32: -0.1654 S33: 0.1118 REMARK 3 REMARK 3 TLS GROUP : 5 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : P 1 P 151 REMARK 3 ORIGIN FOR THE GROUP (A): -10.1670 49.3070 42.1680 REMARK 3 T TENSOR REMARK 3 T11: 0.2313 T22: 0.4355 REMARK 3 T33: 0.4182 T12: 0.0477 REMARK 3 T13: -0.1044 T23: -0.0783 REMARK 3 L TENSOR REMARK 3 L11: 4.1823 L22: 2.5677 REMARK 3 L33: 3.2112 L12: -1.2496 REMARK 3 L13: -2.8182 L23: 2.0217 REMARK 3 S TENSOR REMARK 3 S11: -0.1192 S12: 0.3551 S13: -0.0641 REMARK 3 S21: -0.1060 S22: 0.0448 S23: 0.2680 REMARK 3 S31: -0.0663 S32: 0.0522 S33: 0.0744 REMARK 3 REMARK 3 TLS GROUP : 6 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : P 152 P 400 REMARK 3 ORIGIN FOR THE GROUP (A): -36.8460 57.2170 54.7320 REMARK 3 T TENSOR REMARK 3 T11: 0.4439 T22: 0.2265 REMARK 3 T33: 0.4593 T12: 0.0168 REMARK 3 T13: -0.0259 T23: -0.0598 REMARK 3 L TENSOR REMARK 3 L11: 9.2019 L22: 2.0402 REMARK 3 L33: 2.9990 L12: -1.2535 REMARK 3 L13: -0.8511 L23: -0.1219 REMARK 3 S TENSOR REMARK 3 S11: -0.0272 S12: -0.1805 S13: 0.0466 REMARK 3 S21: 0.0509 S22: -0.0147 S23: 0.3489 REMARK 3 S31: 0.0022 S32: -0.3209 S33: 0.0419 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : MASK REMARK 3 PARAMETERS FOR MASK CALCULATION REMARK 3 VDW PROBE RADIUS : 1.20 REMARK 3 ION PROBE RADIUS : 0.80 REMARK 3 SHRINKAGE RADIUS : 0.80 REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: U VALUES : WITH TLS ADDED HYDROGENS REMARK 3 HAVE BEEN ADDED IN THE RIDING POSITIONS REMARK 4 REMARK 4 9GWT COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 27-SEP-24. REMARK 100 THE DEPOSITION ID IS D_1292142033. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 07-SEP-22 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 6.5 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : SLS REMARK 200 BEAMLINE : X10SA REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : .999 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER2 S 16M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : AIMLESS REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 27539 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.887 REMARK 200 RESOLUTION RANGE LOW (A) : 93.031 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 94.3 REMARK 200 DATA REDUNDANCY : 25.10 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 16.3000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.89 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.08 REMARK 200 COMPLETENESS FOR SHELL (%) : NULL REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : NULL REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: PHASER REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 71.52 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.32 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: SODIUM CACODYLATE 0.1M, GLYCEROL 10% REMARK 280 (V/V), NACL 1M, PEG 600 30.0% (W/V), PH 6.5, VAPOR DIFFUSION, REMARK 280 SITTING DROP, TEMPERATURE 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,-Y,Z+1/2 REMARK 290 3555 -Y+1/2,X+1/2,Z+1/4 REMARK 290 4555 Y+1/2,-X+1/2,Z+3/4 REMARK 290 5555 -X+1/2,Y+1/2,-Z+1/4 REMARK 290 6555 X+1/2,-Y+1/2,-Z+3/4 REMARK 290 7555 Y,X,-Z REMARK 290 8555 -Y,-X,-Z+1/2 REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 139.77500 REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 49.32700 REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 49.32700 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 69.88750 REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 49.32700 REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 49.32700 REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 209.66250 REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 49.32700 REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 49.32700 REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 69.88750 REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 49.32700 REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 49.32700 REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 209.66250 REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 139.77500 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: H, L, P, A, B, C, D, E 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 LYS H 134 REMARK 465 SER H 135 REMARK 465 THR H 136 REMARK 465 SER H 137 REMARK 465 LYS H 223 REMARK 465 THR H 224 REMARK 465 HIS H 225 REMARK 465 THR H 226 REMARK 465 HIS H 227 REMARK 465 HIS H 228 REMARK 465 HIS H 229 REMARK 465 HIS H 230 REMARK 465 HIS H 231 REMARK 465 HIS H 232 REMARK 465 HIS H 233 REMARK 465 HIS H 234 REMARK 465 MET P 10 REMARK 465 GLY P 11 REMARK 465 TRP P 12 REMARK 465 SER P 13 REMARK 465 CYS P 14 REMARK 465 ILE P 15 REMARK 465 ILE P 16 REMARK 465 LEU P 17 REMARK 465 PHE P 18 REMARK 465 LEU P 19 REMARK 465 VAL P 20 REMARK 465 ALA P 21 REMARK 465 THR P 22 REMARK 465 ALA P 23 REMARK 465 THR P 24 REMARK 465 GLY P 25 REMARK 465 VAL P 26 REMARK 465 HIS P 27 REMARK 465 SER P 28 REMARK 465 MET P 29 REMARK 465 ASP P 30 REMARK 465 GLU P 31 REMARK 465 LYS P 32 REMARK 465 GLN P 33 REMARK 465 ILE P 34 REMARK 465 THR P 35 REMARK 465 GLN P 36 REMARK 465 PRO P 233 REMARK 465 VAL P 234 REMARK 465 PRO P 235 REMARK 465 GLY P 236 REMARK 465 ALA P 237 REMARK 465 LYS P 238 REMARK 465 LYS P 239 REMARK 465 SER P 240 REMARK 465 ALA P 241 REMARK 465 LYS P 242 REMARK 465 LEU P 243 REMARK 465 GLY P 244 REMARK 465 GLY P 245 REMARK 465 GLY P 246 REMARK 465 SER P 247 REMARK 465 GLY P 248 REMARK 465 LEU P 249 REMARK 465 ASN P 250 REMARK 465 ASP P 251 REMARK 465 ILE P 252 REMARK 465 PHE P 253 REMARK 465 GLU P 254 REMARK 465 ALA P 255 REMARK 465 GLN P 256 REMARK 465 LYS P 257 REMARK 465 ILE P 258 REMARK 465 GLU P 259 REMARK 465 TRP P 260 REMARK 465 HIS P 261 REMARK 465 GLU P 262 REMARK 465 GLY P 263 REMARK 465 GLY P 264 REMARK 465 SER P 265 REMARK 465 GLY P 266 REMARK 465 SER P 267 REMARK 465 GLY P 268 REMARK 465 THR P 269 REMARK 465 HIS P 270 REMARK 465 HIS P 271 REMARK 465 HIS P 272 REMARK 465 HIS P 273 REMARK 465 HIS P 274 REMARK 465 HIS P 275 REMARK 465 HIS P 276 REMARK 465 HIS P 277 REMARK 480 REMARK 480 ZERO OCCUPANCY ATOM REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME; REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE): REMARK 480 M RES C SSEQI ATOMS REMARK 480 GLU H 1 CD OE1 OE2 REMARK 480 LYS H 43 CE NZ REMARK 480 LYS H 81 NZ REMARK 480 ILE H 200 CD1 REMARK 480 LYS H 206 CD CE NZ REMARK 480 LYS H 211 CE NZ REMARK 480 LYS H 215 CE NZ REMARK 480 LYS H 219 CE NZ REMARK 480 ARG L 24 NE CZ NH1 NH2 REMARK 480 ARG L 72 CZ NH1 NH2 REMARK 480 LYS L 107 NZ REMARK 480 LYS L 111 NZ REMARK 480 LYS L 130 CE NZ REMARK 480 LYS L 149 CD CE NZ REMARK 480 GLN L 151 CD OE1 NE2 REMARK 480 LYS L 153 CD CE NZ REMARK 480 GLU L 169 CD OE1 OE2 REMARK 480 LYS L 194 CD CE NZ REMARK 480 GLU L 199 CD OE1 OE2 REMARK 480 ASN P 37 CG OD1 ND2 REMARK 480 LYS P 40 CD CE NZ REMARK 480 LEU P 42 CD1 CD2 REMARK 480 ARG P 79 CZ NH1 NH2 REMARK 480 GLU P 91 CD OE1 OE2 REMARK 480 GLN P 159 CD OE1 NE2 REMARK 480 ARG P 161 CD NE CZ NH1 NH2 REMARK 480 ASN P 162 CG OD1 ND2 REMARK 480 GLU P 207 CD OE1 OE2 REMARK 480 LYS P 225 CD CE NZ REMARK 480 TYR P 228 CG CD1 CD2 CE1 CE2 CZ OH REMARK 480 GLU P 230 CG CD OE1 OE2 REMARK 480 LEU P 232 CD1 CD2 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS 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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3) 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 RES CSSEQI ATM2 DEVIATION REMARK 500 ARG L 72 NE ARG L 72 CZ 0.078 REMARK 500 GLU L 169 CG GLU L 169 CD -0.125 REMARK 500 ARG P 79 NE ARG P 79 CZ 0.090 REMARK 500 LYS P 225 CG LYS P 225 CD -0.268 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 LYS P 225 CB - CG - CD ANGL. DEV. = 25.1 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 LEU H 101 -50.93 74.20 REMARK 500 ASP H 149 69.56 65.10 REMARK 500 THR H 165 -48.27 -131.01 REMARK 500 PHE L 36 51.70 -105.11 REMARK 500 ARG L 54 72.22 17.35 REMARK 500 ALA L 55 -58.49 77.11 REMARK 500 ARG L 72 -99.73 60.30 REMARK 500 ASN L 142 83.26 66.14 REMARK 500 ILE P 70 -61.06 -106.46 REMARK 500 SER P 109 -91.44 -140.00 REMARK 500 ARG P 161 -160.46 -129.53 REMARK 500 PRO P 174 -168.57 -74.95 REMARK 500 SER P 212 -57.40 -138.01 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 L 72 0.08 SIDE CHAIN REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 9GWZ RELATED DB: PDB DBREF 9GWT H 1 234 PDB 9GWT 9GWT 1 234 DBREF 9GWT L 1 218 PDB 9GWT 9GWT 1 218 DBREF 9GWT P 29 243 UNP Q8TD46 MO2R1_HUMAN 29 243 SEQADV 9GWT MET P 10 UNP Q8TD46 INITIATING METHIONINE SEQADV 9GWT GLY P 11 UNP Q8TD46 EXPRESSION TAG SEQADV 9GWT TRP P 12 UNP Q8TD46 EXPRESSION TAG SEQADV 9GWT SER P 13 UNP Q8TD46 EXPRESSION TAG SEQADV 9GWT CYS P 14 UNP Q8TD46 EXPRESSION TAG SEQADV 9GWT ILE P 15 UNP Q8TD46 EXPRESSION TAG SEQADV 9GWT ILE P 16 UNP Q8TD46 EXPRESSION TAG SEQADV 9GWT LEU P 17 UNP Q8TD46 EXPRESSION TAG SEQADV 9GWT PHE P 18 UNP Q8TD46 EXPRESSION TAG SEQADV 9GWT LEU P 19 UNP Q8TD46 EXPRESSION TAG SEQADV 9GWT VAL P 20 UNP Q8TD46 EXPRESSION TAG SEQADV 9GWT ALA P 21 UNP Q8TD46 EXPRESSION TAG SEQADV 9GWT THR P 22 UNP Q8TD46 EXPRESSION TAG SEQADV 9GWT ALA P 23 UNP Q8TD46 EXPRESSION TAG SEQADV 9GWT THR P 24 UNP Q8TD46 EXPRESSION TAG SEQADV 9GWT GLY P 25 UNP Q8TD46 EXPRESSION TAG SEQADV 9GWT VAL P 26 UNP Q8TD46 EXPRESSION TAG SEQADV 9GWT HIS P 27 UNP Q8TD46 EXPRESSION TAG SEQADV 9GWT SER P 28 UNP Q8TD46 EXPRESSION TAG SEQADV 9GWT GLY P 244 UNP Q8TD46 EXPRESSION TAG SEQADV 9GWT GLY P 245 UNP Q8TD46 EXPRESSION TAG SEQADV 9GWT GLY P 246 UNP Q8TD46 EXPRESSION TAG SEQADV 9GWT SER P 247 UNP Q8TD46 EXPRESSION TAG SEQADV 9GWT GLY P 248 UNP Q8TD46 EXPRESSION TAG SEQADV 9GWT LEU P 249 UNP Q8TD46 EXPRESSION TAG SEQADV 9GWT ASN P 250 UNP Q8TD46 EXPRESSION TAG SEQADV 9GWT ASP P 251 UNP Q8TD46 EXPRESSION TAG SEQADV 9GWT ILE P 252 UNP Q8TD46 EXPRESSION TAG SEQADV 9GWT PHE P 253 UNP Q8TD46 EXPRESSION TAG SEQADV 9GWT GLU P 254 UNP Q8TD46 EXPRESSION TAG SEQADV 9GWT ALA P 255 UNP Q8TD46 EXPRESSION TAG SEQADV 9GWT GLN P 256 UNP Q8TD46 EXPRESSION TAG SEQADV 9GWT LYS P 257 UNP Q8TD46 EXPRESSION TAG SEQADV 9GWT ILE P 258 UNP Q8TD46 EXPRESSION TAG SEQADV 9GWT GLU P 259 UNP Q8TD46 EXPRESSION TAG SEQADV 9GWT TRP P 260 UNP Q8TD46 EXPRESSION TAG SEQADV 9GWT HIS P 261 UNP Q8TD46 EXPRESSION TAG SEQADV 9GWT GLU P 262 UNP Q8TD46 EXPRESSION TAG SEQADV 9GWT GLY P 263 UNP Q8TD46 EXPRESSION TAG SEQADV 9GWT GLY P 264 UNP Q8TD46 EXPRESSION TAG SEQADV 9GWT SER P 265 UNP Q8TD46 EXPRESSION TAG SEQADV 9GWT GLY P 266 UNP Q8TD46 EXPRESSION TAG SEQADV 9GWT SER P 267 UNP Q8TD46 EXPRESSION TAG SEQADV 9GWT GLY P 268 UNP Q8TD46 EXPRESSION TAG SEQADV 9GWT THR P 269 UNP Q8TD46 EXPRESSION TAG SEQADV 9GWT HIS P 270 UNP Q8TD46 EXPRESSION TAG SEQADV 9GWT HIS P 271 UNP Q8TD46 EXPRESSION TAG SEQADV 9GWT HIS P 272 UNP Q8TD46 EXPRESSION TAG SEQADV 9GWT HIS P 273 UNP Q8TD46 EXPRESSION TAG SEQADV 9GWT HIS P 274 UNP Q8TD46 EXPRESSION TAG SEQADV 9GWT HIS P 275 UNP Q8TD46 EXPRESSION TAG SEQADV 9GWT HIS P 276 UNP Q8TD46 EXPRESSION TAG SEQADV 9GWT HIS P 277 UNP Q8TD46 EXPRESSION TAG SEQRES 1 H 234 GLU VAL GLN LEU GLN GLU SER GLY PRO GLY LEU VAL LYS SEQRES 2 H 234 PRO SER GLU THR LEU SER LEU THR CYS THR VAL SER GLY SEQRES 3 H 234 PHE SER LEU THR ASN TYR ALA VAL SER TRP VAL ARG GLN SEQRES 4 H 234 PRO PRO GLY LYS GLY LEU GLU TRP LEU GLY VAL MET TRP SEQRES 5 H 234 ALA GLY GLY GLY THR ASN TYR ASN SER VAL PHE LYS SER SEQRES 6 H 234 ARG LEU THR ILE SER LYS ASP ASN SER LYS ASN GLN VAL SEQRES 7 H 234 SER LEU LYS LEU SER SER VAL THR ALA ALA ASP THR ALA SEQRES 8 H 234 VAL TYR TYR CYS ALA ARG GLU ARG PRO LEU THR GLY VAL SEQRES 9 H 234 MET ASP TYR TRP GLY GLN GLY THR LEU VAL THR VAL SER SEQRES 10 H 234 SER ALA SER THR LYS GLY PRO SER VAL PHE PRO LEU ALA SEQRES 11 H 234 PRO SER SER LYS SER THR SER GLY GLY THR ALA ALA LEU SEQRES 12 H 234 GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU PRO VAL THR SEQRES 13 H 234 VAL SER TRP ASN SER GLY ALA LEU THR SER GLY VAL HIS SEQRES 14 H 234 THR PHE PRO ALA VAL LEU GLN SER SER GLY LEU TYR SER SEQRES 15 H 234 LEU SER SER VAL VAL THR VAL PRO SER SER SER LEU GLY SEQRES 16 H 234 THR GLN THR TYR ILE CYS ASN VAL ASN HIS LYS PRO SER SEQRES 17 H 234 ASN THR LYS VAL ASP LYS LYS VAL GLU PRO LYS SER CYS SEQRES 18 H 234 ASP LYS THR HIS THR HIS HIS HIS HIS HIS HIS HIS HIS SEQRES 1 L 218 ASP ILE VAL LEU THR GLN SER PRO ASP SER LEU ALA VAL SEQRES 2 L 218 SER LEU GLY GLU ARG ALA THR ILE ASN CYS ARG ALA SER SEQRES 3 L 218 GLU SER VAL ASP TYR SER GLY ASN SER PHE MET HIS TRP SEQRES 4 L 218 PHE GLN GLN LYS PRO GLY GLN PRO PRO LYS LEU LEU ILE SEQRES 5 L 218 TYR ARG ALA SER ASN LEU GLU SER GLY ILE PRO ASP ARG SEQRES 6 L 218 PHE SER GLY SER GLY SER ARG THR ASP PHE THR LEU THR SEQRES 7 L 218 ILE SER SER LEU GLN ALA GLU ASP VAL ALA VAL TYR TYR SEQRES 8 L 218 CYS HIS GLN SER ASN GLU ASP PRO PRO THR PHE GLY GLY SEQRES 9 L 218 GLY THR LYS VAL GLU ILE LYS ARG THR VAL ALA ALA PRO SEQRES 10 L 218 SER VAL PHE ILE PHE PRO PRO SER ASP GLU GLN LEU LYS SEQRES 11 L 218 SER GLY THR ALA SER VAL VAL CYS LEU LEU ASN ASN PHE SEQRES 12 L 218 TYR PRO ARG GLU ALA LYS VAL GLN TRP LYS VAL ASP ASN SEQRES 13 L 218 ALA LEU GLN SER GLY ASN SER GLN GLU SER VAL THR GLU SEQRES 14 L 218 GLN ASP SER LYS ASP SER THR TYR SER LEU SER SER THR SEQRES 15 L 218 LEU THR LEU SER LYS ALA ASP TYR GLU LYS HIS LYS VAL SEQRES 16 L 218 TYR ALA CYS GLU VAL THR HIS GLN GLY LEU SER SER PRO SEQRES 17 L 218 VAL THR LYS SER PHE ASN ARG GLY GLU CYS SEQRES 1 P 268 MET GLY TRP SER CYS ILE ILE LEU PHE LEU VAL ALA THR SEQRES 2 P 268 ALA THR GLY VAL HIS SER MET ASP GLU LYS GLN ILE THR SEQRES 3 P 268 GLN ASN TYR SER LYS VAL LEU ALA GLU VAL ASN THR SER SEQRES 4 P 268 TRP PRO VAL LYS MET ALA THR ASN ALA VAL LEU CYS CYS SEQRES 5 P 268 PRO PRO ILE ALA LEU ARG ASN LEU ILE ILE ILE THR TRP SEQRES 6 P 268 GLU ILE ILE LEU ARG GLY GLN PRO SER CYS THR LYS ALA SEQRES 7 P 268 TYR LYS LYS GLU THR ASN GLU THR LYS GLU THR ASN CYS SEQRES 8 P 268 THR ASP GLU ARG ILE THR TRP VAL SER ARG PRO ASP GLN SEQRES 9 P 268 ASN SER ASP LEU GLN ILE ARG THR VAL ALA ILE THR HIS SEQRES 10 P 268 ASP GLY TYR TYR ARG CYS ILE MET VAL THR PRO ASP GLY SEQRES 11 P 268 ASN PHE HIS ARG GLY TYR HIS LEU GLN VAL LEU VAL THR SEQRES 12 P 268 PRO GLU VAL THR LEU PHE GLN ASN ARG ASN ARG THR ALA SEQRES 13 P 268 VAL CYS LYS ALA VAL ALA GLY LYS PRO ALA ALA HIS ILE SEQRES 14 P 268 SER TRP ILE PRO GLU GLY ASP CYS ALA THR LYS GLN GLU SEQRES 15 P 268 TYR TRP SER ASN GLY THR VAL THR VAL LYS SER THR CYS SEQRES 16 P 268 HIS TRP GLU VAL HIS ASN VAL SER THR VAL THR CYS HIS SEQRES 17 P 268 VAL SER HIS LEU THR GLY ASN LYS SER LEU TYR ILE GLU SEQRES 18 P 268 LEU LEU PRO VAL PRO GLY ALA LYS LYS SER ALA LYS LEU SEQRES 19 P 268 GLY GLY GLY SER GLY LEU ASN ASP ILE PHE GLU ALA GLN SEQRES 20 P 268 LYS ILE GLU TRP HIS GLU GLY GLY SER GLY SER GLY THR SEQRES 21 P 268 HIS HIS HIS HIS HIS HIS HIS HIS HET NAG A 1 14 HET NAG A 2 14 HET NAG B 1 14 HET NAG B 2 14 HET BMA B 3 11 HET NAG C 1 14 HET NAG C 2 14 HET BMA C 3 11 HET MAN C 4 11 HET MAN C 5 11 HET MAN C 6 11 HET MAN C 7 11 HET NAG D 1 14 HET NAG D 2 14 HET BMA D 3 11 HET MAN D 4 11 HET NAG E 1 14 HET NAG E 2 14 HET GOL L 301 6 HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE HETNAM BMA BETA-D-MANNOPYRANOSE HETNAM MAN ALPHA-D-MANNOPYRANOSE HETNAM GOL GLYCEROL 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 HETSYN BMA BETA-D-MANNOSE; D-MANNOSE; MANNOSE HETSYN MAN ALPHA-D-MANNOSE; D-MANNOSE; MANNOSE HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL FORMUL 4 NAG 10(C8 H15 N O6) FORMUL 5 BMA 3(C6 H12 O6) FORMUL 6 MAN 5(C6 H12 O6) FORMUL 9 GOL C3 H8 O3 FORMUL 10 HOH *25(H2 O) HELIX 1 AA1 SER H 61 LYS H 64 5 4 HELIX 2 AA2 THR H 86 THR H 90 5 5 HELIX 3 AA3 SER H 161 ALA H 163 5 3 HELIX 4 AA4 SER H 192 GLY H 195 5 4 HELIX 5 AA5 GLN L 83 VAL L 87 5 5 HELIX 6 AA6 SER L 125 GLY L 132 1 8 HELIX 7 AA7 LYS L 187 GLU L 191 1 5 HELIX 8 AA8 ALA P 65 LEU P 69 5 5 HELIX 9 AA9 ALA P 123 HIS P 126 5 4 SHEET 1 AA1 4 GLN H 3 SER H 7 0 SHEET 2 AA1 4 LEU H 18 SER H 25 -1 O SER H 25 N GLN H 3 SHEET 3 AA1 4 GLN H 77 LEU H 82 -1 O LEU H 82 N LEU H 18 SHEET 4 AA1 4 LEU H 67 ASP H 72 -1 N ASP H 72 O GLN H 77 SHEET 1 AA2 6 LEU H 11 VAL H 12 0 SHEET 2 AA2 6 THR H 112 VAL H 116 1 O THR H 115 N VAL H 12 SHEET 3 AA2 6 ALA H 91 GLU H 98 -1 N ALA H 91 O VAL H 114 SHEET 4 AA2 6 ALA H 33 GLN H 39 -1 N VAL H 37 O TYR H 94 SHEET 5 AA2 6 GLU H 46 MET H 51 -1 O MET H 51 N VAL H 34 SHEET 6 AA2 6 THR H 57 TYR H 59 -1 O ASN H 58 N VAL H 50 SHEET 1 AA3 4 LEU H 11 VAL H 12 0 SHEET 2 AA3 4 THR H 112 VAL H 116 1 O THR H 115 N VAL H 12 SHEET 3 AA3 4 ALA H 91 GLU H 98 -1 N ALA H 91 O VAL H 114 SHEET 4 AA3 4 MET H 105 TRP H 108 -1 O TYR H 107 N ARG H 97 SHEET 1 AA4 4 SER H 125 LEU H 129 0 SHEET 2 AA4 4 THR H 140 TYR H 150 -1 O LYS H 148 N SER H 125 SHEET 3 AA4 4 TYR H 181 PRO H 190 -1 O TYR H 181 N TYR H 150 SHEET 4 AA4 4 VAL H 168 THR H 170 -1 N HIS H 169 O VAL H 186 SHEET 1 AA5 4 SER H 125 LEU H 129 0 SHEET 2 AA5 4 THR H 140 TYR H 150 -1 O LYS H 148 N SER H 125 SHEET 3 AA5 4 TYR H 181 PRO H 190 -1 O TYR H 181 N TYR H 150 SHEET 4 AA5 4 VAL H 174 LEU H 175 -1 N VAL H 174 O SER H 182 SHEET 1 AA6 3 THR H 156 TRP H 159 0 SHEET 2 AA6 3 ILE H 200 HIS H 205 -1 O ASN H 202 N SER H 158 SHEET 3 AA6 3 THR H 210 LYS H 215 -1 O VAL H 212 N VAL H 203 SHEET 1 AA7 4 LEU L 4 SER L 7 0 SHEET 2 AA7 4 ALA L 19 ALA L 25 -1 O ASN L 22 N SER L 7 SHEET 3 AA7 4 ASP L 74 ILE L 79 -1 O LEU L 77 N ILE L 21 SHEET 4 AA7 4 PHE L 66 SER L 71 -1 N SER L 67 O THR L 78 SHEET 1 AA8 6 SER L 10 SER L 14 0 SHEET 2 AA8 6 THR L 106 LYS L 111 1 O LYS L 107 N LEU L 11 SHEET 3 AA8 6 VAL L 89 GLN L 94 -1 N TYR L 90 O THR L 106 SHEET 4 AA8 6 MET L 37 GLN L 42 -1 N PHE L 40 O TYR L 91 SHEET 5 AA8 6 LYS L 49 TYR L 53 -1 O LYS L 49 N GLN L 41 SHEET 6 AA8 6 ASN L 57 LEU L 58 -1 O ASN L 57 N TYR L 53 SHEET 1 AA9 4 SER L 10 SER L 14 0 SHEET 2 AA9 4 THR L 106 LYS L 111 1 O LYS L 107 N LEU L 11 SHEET 3 AA9 4 VAL L 89 GLN L 94 -1 N TYR L 90 O THR L 106 SHEET 4 AA9 4 THR L 101 PHE L 102 -1 O THR L 101 N GLN L 94 SHEET 1 AB1 2 ASP L 30 TYR L 31 0 SHEET 2 AB1 2 ASN L 34 SER L 35 -1 O ASN L 34 N TYR L 31 SHEET 1 AB2 4 SER L 118 PHE L 122 0 SHEET 2 AB2 4 THR L 133 PHE L 143 -1 O LEU L 139 N PHE L 120 SHEET 3 AB2 4 TYR L 177 SER L 186 -1 O LEU L 185 N ALA L 134 SHEET 4 AB2 4 SER L 163 VAL L 167 -1 N GLN L 164 O THR L 182 SHEET 1 AB3 3 LYS L 149 VAL L 154 0 SHEET 2 AB3 3 VAL L 195 THR L 201 -1 O GLU L 199 N GLN L 151 SHEET 3 AB3 3 VAL L 209 ASN L 214 -1 O VAL L 209 N VAL L 200 SHEET 1 AB4 6 GLU P 44 LYS P 52 0 SHEET 2 AB4 6 ASN P 140 LEU P 150 1 O GLY P 144 N VAL P 45 SHEET 3 AB4 6 GLY P 128 VAL P 135 -1 N TYR P 130 O TYR P 145 SHEET 4 AB4 6 ILE P 71 LEU P 78 -1 N GLU P 75 O ARG P 131 SHEET 5 AB4 6 CYS P 84 LYS P 89 -1 O CYS P 84 N ILE P 76 SHEET 6 AB4 6 GLU P 94 THR P 98 -1 O LYS P 96 N ALA P 87 SHEET 1 AB5 3 ALA P 57 LEU P 59 0 SHEET 2 AB5 3 LEU P 117 ILE P 119 -1 O LEU P 117 N LEU P 59 SHEET 3 AB5 3 ILE P 105 TRP P 107 -1 N THR P 106 O GLN P 118 SHEET 1 AB6 4 GLU P 154 GLN P 159 0 SHEET 2 AB6 4 THR P 164 GLY P 172 -1 O VAL P 170 N GLU P 154 SHEET 3 AB6 4 VAL P 198 HIS P 205 -1 O VAL P 198 N GLY P 172 SHEET 4 AB6 4 ASP P 185 TYR P 192 -1 N ALA P 187 O THR P 203 SHEET 1 AB7 3 HIS P 177 ILE P 181 0 SHEET 2 AB7 3 THR P 213 SER P 219 -1 O SER P 219 N HIS P 177 SHEET 3 AB7 3 LYS P 225 GLU P 230 -1 O LEU P 227 N CYS P 216 SSBOND 1 CYS H 22 CYS H 95 1555 1555 2.05 SSBOND 2 CYS H 145 CYS H 201 1555 1555 2.04 SSBOND 3 CYS L 23 CYS L 92 1555 1555 2.09 SSBOND 4 CYS L 138 CYS L 198 1555 1555 2.03 SSBOND 5 CYS P 61 CYS P 132 1555 1555 2.05 SSBOND 6 CYS P 84 CYS P 100 1555 1555 2.06 SSBOND 7 CYS P 167 CYS P 216 1555 1555 2.03 SSBOND 8 CYS P 186 CYS P 204 1555 1555 2.06 LINK ND2 ASN P 46 C1 NAG C 1 1555 1555 1.45 LINK ND2 ASN P 93 C1 NAG E 1 1555 1555 1.44 LINK ND2 ASN P 99 C1 NAG D 1 1555 1555 1.44 LINK ND2 ASN P 195 C1 NAG B 1 1555 1555 1.45 LINK ND2 ASN P 224 C1 NAG A 1 1555 1555 1.44 LINK O4 NAG A 1 C1 NAG A 2 1555 1555 1.45 LINK O4 NAG B 1 C1 NAG B 2 1555 1555 1.44 LINK O4 NAG B 2 C1 BMA B 3 1555 1555 1.45 LINK O4 NAG C 1 C1 NAG C 2 1555 1555 1.45 LINK O4 NAG C 2 C1 BMA C 3 1555 1555 1.45 LINK O6 BMA C 3 C1 MAN C 4 1555 1555 1.44 LINK O3 BMA C 3 C1 MAN C 7 1555 1555 1.44 LINK O3 MAN C 4 C1 MAN C 5 1555 1555 1.45 LINK O6 MAN C 4 C1 MAN C 6 1555 1555 1.44 LINK O4 NAG D 1 C1 NAG D 2 1555 1555 1.44 LINK O4 NAG D 2 C1 BMA D 3 1555 1555 1.45 LINK O6 BMA D 3 C1 MAN D 4 1555 1555 1.45 LINK O4 NAG E 1 C1 NAG E 2 1555 1555 1.44 CISPEP 1 PHE H 151 PRO H 152 0 -12.36 CISPEP 2 GLU H 153 PRO H 154 0 -1.90 CISPEP 3 SER L 7 PRO L 8 0 -0.89 CISPEP 4 ASP L 98 PRO L 99 0 -1.68 CISPEP 5 TYR L 144 PRO L 145 0 2.85 CISPEP 6 LYS P 173 PRO P 174 0 -5.06 CISPEP 7 ILE P 181 PRO P 182 0 -4.40 CRYST1 98.654 98.654 279.550 90.00 90.00 90.00 P 41 21 2 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 0.010136 0.000000 0.000000 0.00000 SCALE2 0.000000 0.010136 0.000000 0.00000 SCALE3 0.000000 0.000000 0.003577 0.00000