HEADER IMMUNE SYSTEM 14-MAR-20 6YAX TITLE CRYSTAL STRUCTURE OF CD32B (FC GAMMA RECEPTOR IIB) IN COMPLEX WITH TITLE 2 HUMAN IGG1 FAB FRAGMENT (5C05) CAVEAT 6YAX NAG A 2 HAS WRONG CHIRALITY AT ATOM C1 COMPND MOL_ID: 1; COMPND 2 MOLECULE: 5C05 F(AB) HEAVY CHAIN; COMPND 3 CHAIN: HHH, III; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: 5C05 F(AB) LIGHT CHAIN; COMPND 7 CHAIN: MMM, LLL; COMPND 8 ENGINEERED: YES; COMPND 9 MOL_ID: 3; COMPND 10 MOLECULE: LOW AFFINITY IMMUNOGLOBULIN GAMMA FC REGION RECEPTOR II-C; COMPND 11 CHAIN: AAA, BBB; COMPND 12 SYNONYM: IGG FC RECEPTOR II-C,CDW32,FC-GAMMA RII-C,FCRII-C; COMPND 13 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: HEK293; 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 EXPRESSION_SYSTEM_CELL_LINE: HEK293; SOURCE 13 MOL_ID: 3; SOURCE 14 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 15 ORGANISM_COMMON: HUMAN; SOURCE 16 ORGANISM_TAXID: 9606; SOURCE 17 GENE: FCGR2C, CD32, FCG2, IGFR2; SOURCE 18 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 19 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 20 EXPRESSION_SYSTEM_CELL_LINE: HEK293 KEYWDS CD32 CD32B FC GAMMA RECEPTOR FC GAMMA RECEPTOR II B FAB COMPLEX, KEYWDS 2 IMMUNE SYSTEM EXPDTA X-RAY DIFFRACTION AUTHOR H.FISHER,I.TEWS,C.ORR JRNL AUTH H.FISHER,I.TEWS,C.ORR JRNL TITL CRYSTAL STRUCTURE OF CD32B (FC GAMMA RECEPTOR IIB) IN JRNL TITL 2 COMPLEX WITH HUMAN IGG1 FAB FRAGMENT (5C05) JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 2.80 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : REFMAC 5.8.0258 REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER, REMARK 3 : NICHOLLS,WINN,LONG,VAGIN REMARK 3 REMARK 3 REFINEMENT TARGET : NULL REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 47.86 REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL REMARK 3 COMPLETENESS FOR RANGE (%) : 99.6 REMARK 3 NUMBER OF REFLECTIONS : 40956 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 CROSS-VALIDATION METHOD : FREE R-VALUE REMARK 3 FREE R VALUE TEST SET SELECTION : NULL REMARK 3 R VALUE (WORKING + TEST SET) : NULL REMARK 3 R VALUE (WORKING SET) : 0.230 REMARK 3 FREE R VALUE : 0.264 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.812 REMARK 3 FREE R VALUE TEST SET COUNT : 1971 REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : 20 REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.80 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.87 REMARK 3 REFLECTION IN BIN (WORKING SET) : 2802 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 97.55 REMARK 3 BIN R VALUE (WORKING SET) : 0.3340 REMARK 3 BIN FREE R VALUE SET COUNT : 144 REMARK 3 BIN FREE R VALUE : 0.3670 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 8293 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 74 REMARK 3 SOLVENT ATOMS : 277 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 70.40 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 0.21400 REMARK 3 B22 (A**2) : 0.21400 REMARK 3 B33 (A**2) : -0.42700 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): 0.927 REMARK 3 ESU BASED ON FREE R VALUE (A): 0.355 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): NULL REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.919 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.898 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 8609 ; 0.004 ; 0.013 REMARK 3 BOND LENGTHS OTHERS (A): 7564 ; 0.036 ; 0.017 REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 11734 ; 1.383 ; 1.650 REMARK 3 BOND ANGLES OTHERS (DEGREES): 17664 ; 2.427 ; 1.576 REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1083 ; 7.554 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 373 ;32.877 ;23.485 REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1279 ;15.811 ;15.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 27 ;18.786 ;15.000 REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1142 ; 0.049 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 9583 ; 0.004 ; 0.020 REMARK 3 GENERAL PLANES OTHERS (A): 1715 ; 0.007 ; 0.020 REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1376 ; 0.193 ; 0.200 REMARK 3 NON-BONDED CONTACTS OTHERS (A): 79 ; 0.230 ; 0.200 REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 3917 ; 0.158 ; 0.200 REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 289 ; 0.184 ; 0.200 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): 4370 ; 3.042 ; 7.675 REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 4369 ; 3.042 ; 7.675 REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 5431 ; 4.768 ;11.482 REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 5432 ; 4.768 ;11.482 REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 4239 ; 3.187 ; 7.804 REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 4240 ; 3.187 ; 7.805 REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 6300 ; 5.041 ;11.638 REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 6301 ; 5.040 ;11.638 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 : NULL REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : NULL 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: HYDROGENS HAVE BEEN ADDED IN THEIR REMARK 3 RIDING POSITIONS REMARK 4 REMARK 4 6YAX COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE. REMARK 100 THE DEPOSITION ID IS D_1292107291. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 24-JUL-17 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 8.5 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : ESRF REMARK 200 BEAMLINE : MASSIF-3 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.97 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 4M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DIALS REMARK 200 DATA SCALING SOFTWARE : AIMLESS REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 41024 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.800 REMARK 200 RESOLUTION RANGE LOW (A) : 47.860 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.3 REMARK 200 DATA REDUNDANCY : 7.200 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 9.1000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.87 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: MOLREP REMARK 200 STARTING MODEL: 5OCC REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 61.53 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.20 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M 1,6-HEXANEDIOL, 0.2 M 1-BUTANOL, REMARK 280 0.2 M 1,2-PROPANEDIOL, 0.2 M 2- PROPANOL, 0.2 M 1,4-BUTANEDIOL, REMARK 280 0.2 M 1,3-PROPANEDIOL, 1.0 M TRIS (BASE), BICINE, 40% V/V PEG REMARK 280 500 MME, 20% W/V PEG 20000, PH 8.5, VAPOR DIFFUSION, SITTING REMARK 280 DROP, TEMPERATURE 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 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,X,Z+3/4 REMARK 290 4555 Y,-X,Z+1/4 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 93.01900 REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 139.52850 REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 46.50950 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 10990 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 51360 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -35.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: HHH, MMM, AAA, LLL, III, BBB, REMARK 350 AND 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 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 SER H 131 REMARK 465 SER H 132 REMARK 465 LYS H 133 REMARK 465 SER H 134 REMARK 465 THR H 135 REMARK 465 SER H 136 REMARK 465 GLY H 137 REMARK 465 GLY H 138 REMARK 465 THR H 139 REMARK 465 ALA H 140 REMARK 465 GLY H 194 REMARK 465 THR H 195 REMARK 465 GLN H 196 REMARK 465 LYS H 218 REMARK 465 GLN M 1 REMARK 465 PRO M 125 REMARK 465 PRO M 126 REMARK 465 SER M 127 REMARK 465 LEU M 131 REMARK 465 GLN M 132 REMARK 465 LYS M 135 REMARK 465 ALA M 136 REMARK 465 THR M 137 REMARK 465 LEU M 138 REMARK 465 VAL M 139 REMARK 465 LYS M 155 REMARK 465 ALA M 156 REMARK 465 ASP M 157 REMARK 465 VAL M 161 REMARK 465 LYS M 162 REMARK 465 ALA M 163 REMARK 465 GLY M 164 REMARK 465 THR M 187 REMARK 465 PRO M 188 REMARK 465 GLU M 189 REMARK 465 GLN M 190 REMARK 465 TRP M 191 REMARK 465 LYS M 192 REMARK 465 SER M 193 REMARK 465 HIS M 194 REMARK 465 ARG M 195 REMARK 465 SER M 196 REMARK 465 TYR M 197 REMARK 465 SER M 198 REMARK 465 ALA M 213 REMARK 465 PRO M 214 REMARK 465 THR M 215 REMARK 465 GLU M 216 REMARK 465 CYS M 217 REMARK 465 SER M 218 REMARK 465 THR A 43 REMARK 465 PRO A 44 REMARK 465 ALA A 45 REMARK 465 ALA A 46 REMARK 465 GLY A 73 REMARK 465 THR A 74 REMARK 465 HIS A 75 REMARK 465 SER A 76 REMARK 465 PRO A 77 REMARK 465 GLU A 78 REMARK 465 SER A 79 REMARK 465 ASP A 80 REMARK 465 HIS A 220 REMARK 465 HIS A 221 REMARK 465 HIS A 222 REMARK 465 HIS A 223 REMARK 465 GLN L 1 REMARK 465 GLU L 216 REMARK 465 CYS L 217 REMARK 465 SER L 218 REMARK 465 SER I 124 REMARK 465 VAL I 125 REMARK 465 PHE I 126 REMARK 465 PRO I 127 REMARK 465 LEU I 128 REMARK 465 ALA I 129 REMARK 465 PRO I 130 REMARK 465 SER I 131 REMARK 465 SER I 132 REMARK 465 LYS I 133 REMARK 465 SER I 134 REMARK 465 THR I 135 REMARK 465 SER I 136 REMARK 465 GLY I 137 REMARK 465 GLY I 138 REMARK 465 THR I 139 REMARK 465 ALA I 140 REMARK 465 ALA I 141 REMARK 465 LEU I 142 REMARK 465 GLY I 143 REMARK 465 TRP I 158 REMARK 465 ASN I 159 REMARK 465 SER I 160 REMARK 465 GLY I 161 REMARK 465 ALA I 162 REMARK 465 LEU I 163 REMARK 465 THR I 164 REMARK 465 SER I 165 REMARK 465 VAL I 186 REMARK 465 THR I 187 REMARK 465 VAL I 188 REMARK 465 PRO I 189 REMARK 465 SER I 190 REMARK 465 SER I 191 REMARK 465 SER I 192 REMARK 465 LEU I 193 REMARK 465 GLY I 194 REMARK 465 THR I 195 REMARK 465 GLN I 196 REMARK 465 THR I 197 REMARK 465 TYR I 198 REMARK 465 ILE I 199 REMARK 465 CYS I 200 REMARK 465 VAL I 211 REMARK 465 ASP I 212 REMARK 465 LYS I 213 REMARK 465 LYS I 214 REMARK 465 VAL I 215 REMARK 465 GLU I 216 REMARK 465 PRO I 217 REMARK 465 LYS I 218 REMARK 465 THR B 43 REMARK 465 PRO B 44 REMARK 465 ALA B 45 REMARK 465 ALA B 46 REMARK 465 HIS B 75 REMARK 465 SER B 76 REMARK 465 PRO B 77 REMARK 465 GLU B 78 REMARK 465 SER B 79 REMARK 465 ALA B 216 REMARK 465 PRO B 217 REMARK 465 HIS B 218 REMARK 465 HIS B 219 REMARK 465 HIS B 220 REMARK 465 HIS B 221 REMARK 465 HIS B 222 REMARK 465 HIS B 223 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 SER M 72 OG REMARK 470 LYS M 108 CD CE NZ REMARK 470 ASN M 118 CG OD1 ND2 REMARK 470 GLU M 129 CG CD OE1 OE2 REMARK 470 VAL M 165 N CB CG1 CG2 REMARK 470 LYS M 169 CG CD CE NZ REMARK 470 LYS M 172 CG CD CE NZ REMARK 470 LYS M 177 CG CD CE NZ REMARK 470 SER M 185 OG REMARK 470 LEU M 186 CG CD1 CD2 REMARK 470 LYS M 210 CG CD CE NZ REMARK 470 ARG A 72 CG CD NE CZ NH1 NH2 REMARK 470 GLN L 16 CG CD OE1 NE2 REMARK 470 ASN L 118 CG OD1 ND2 REMARK 470 ARG L 195 CG CD NE CZ NH1 NH2 REMARK 470 GLN I 13 CG CD OE1 NE2 REMARK 470 LYS I 121 CG CD CE NZ REMARK 470 CYS I 144 SG REMARK 470 VAL I 146 CG1 CG2 REMARK 470 VAL I 167 CG1 CG2 REMARK 470 ASN I 201 CG OD1 ND2 REMARK 470 LYS I 205 CG CD CE NZ REMARK 470 LYS I 210 CG CD CE NZ REMARK 470 ARG B 72 CG CD NE CZ NH1 NH2 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 HD1 HISHH 35 HE1 TRPHH 47 1.05 REMARK 500 ND2 ASNBB 187 H1 NAG A 1 1.21 REMARK 500 OE1 GLUHH 6 H GLYHH 110 1.32 REMARK 500 HB VALHH 188 HD2 PROHH 189 1.34 REMARK 500 H LYSMM 169 O HOHMM 303 1.34 REMARK 500 OE1 GLULL 85 HZ2 LYSLL 172 1.42 REMARK 500 HO3 NAG A 1 O5 NAG A 2 1.42 REMARK 500 H GLYLL 24 O THRLL 71 1.54 REMARK 500 O PHELL 145 H TYRLL 178 1.54 REMARK 500 H LEUHH 128 O GLYHH 143 1.54 REMARK 500 HH22 ARGMM 63 OD2 ASPMM 84 1.54 REMARK 500 O PHEBB 142 H GLNBB 215 1.55 REMARK 500 O ALAMM 153 H GLNMM 200 1.55 REMARK 500 OE2 GLUHH 6 H CYSHH 96 1.56 REMARK 500 H ILEAA 82 O THRAA 95 1.57 REMARK 500 CG ASNBB 187 H1 NAG A 1 1.58 REMARK 500 O TYRII 149 H TYRII 180 1.59 REMARK 500 H GLNBB 83 O GLNBB 114 1.60 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 HD22 ASNHH 208 HD2 HISAA 195 4555 1.19 REMARK 500 O HOHAA 433 O HOHBB 466 1655 2.19 REMARK 500 REMARK 500 REMARK: NULL 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 ARGII 38 CZ ARGII 38 NH2 -0.098 REMARK 500 ARGII 67 CZ ARGII 67 NH1 0.095 REMARK 500 ARGII 67 CZ ARGII 67 NH2 0.142 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 ARGHH 67 -39.03 -131.52 REMARK 500 PHEHH 150 137.04 -173.63 REMARK 500 ASNHH 159 58.47 38.06 REMARK 500 LEUHH 163 68.83 -114.52 REMARK 500 SERHH 190 4.02 -59.40 REMARK 500 ASNMM 28 -99.98 -123.74 REMARK 500 ASNMM 53 -45.15 80.12 REMARK 500 SERMM 54 8.17 -150.20 REMARK 500 LEUMM 80 136.50 -39.14 REMARK 500 ALAMM 86 166.30 176.88 REMARK 500 LEUMM 97 -142.77 60.02 REMARK 500 ASPMM 144 74.13 54.12 REMARK 500 GLNMM 173 -168.69 -70.08 REMARK 500 ASNMM 176 -8.32 80.98 REMARK 500 GLUMM 204 51.28 37.43 REMARK 500 GLUAA 64 -3.30 76.76 REMARK 500 SERAA 177 -15.05 -144.77 REMARK 500 GLNAA 185 73.86 48.43 REMARK 500 ASNLL 28 -101.76 -117.96 REMARK 500 ASNLL 53 -47.05 81.00 REMARK 500 SERLL 54 16.21 -145.47 REMARK 500 LEULL 97 -104.04 53.14 REMARK 500 ASNLL 134 32.41 74.59 REMARK 500 ASPLL 157 -133.04 63.24 REMARK 500 LYSLL 162 -56.97 -127.89 REMARK 500 ASNLL 176 -17.61 92.30 REMARK 500 SERII 56 -82.57 -75.67 REMARK 500 ALAII 61 161.35 -47.12 REMARK 500 SERII 117 -7.01 -58.15 REMARK 500 ASPII 148 75.04 55.96 REMARK 500 PHEII 150 133.89 -177.42 REMARK 500 GLUII 152 161.97 -47.28 REMARK 500 SERII 176 174.60 -57.94 REMARK 500 SERII 177 -8.09 67.29 REMARK 500 GLUBB 64 -9.89 79.93 REMARK 500 ILEBB 91 77.41 -110.97 REMARK 500 SERBB 177 -18.24 -147.42 REMARK 500 REMARK 500 REMARK: NULL REMARK 525 REMARK 525 SOLVENT REMARK 525 REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER; REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE REMARK 525 NUMBER; I=INSERTION CODE): REMARK 525 REMARK 525 M RES CSSEQI REMARK 525 HOH M 331 DISTANCE = 6.25 ANGSTROMS REMARK 525 HOH M 332 DISTANCE = 7.12 ANGSTROMS REMARK 525 HOH M 333 DISTANCE = 7.68 ANGSTROMS REMARK 525 HOH M 334 DISTANCE = 7.74 ANGSTROMS DBREF 6YAXHH 1 218 PDB 6YAX 6YAX 1 218 DBREF 6YAXMM 1 218 PDB 6YAX 6YAX 1 218 DBREF 6YAXAA 43 217 UNP P31995 FCG2C_HUMAN 43 217 DBREF 6YAXLL 1 218 PDB 6YAX 6YAX 1 218 DBREF 6YAXII 1 218 PDB 6YAX 6YAX 1 218 DBREF 6YAXBB 43 217 UNP P31995 FCG2C_HUMAN 43 217 SEQADV 6YAX HISAA 218 UNP P31995 EXPRESSION TAG SEQADV 6YAX HISAA 219 UNP P31995 EXPRESSION TAG SEQADV 6YAX HISAA 220 UNP P31995 EXPRESSION TAG SEQADV 6YAX HISAA 221 UNP P31995 EXPRESSION TAG SEQADV 6YAX HISAA 222 UNP P31995 EXPRESSION TAG SEQADV 6YAX HISAA 223 UNP P31995 EXPRESSION TAG SEQADV 6YAX HISBB 218 UNP P31995 EXPRESSION TAG SEQADV 6YAX HISBB 219 UNP P31995 EXPRESSION TAG SEQADV 6YAX HISBB 220 UNP P31995 EXPRESSION TAG SEQADV 6YAX HISBB 221 UNP P31995 EXPRESSION TAG SEQADV 6YAX HISBB 222 UNP P31995 EXPRESSION TAG SEQADV 6YAX HISBB 223 UNP P31995 EXPRESSION TAG SEQRES 1HH 218 GLU VAL GLN LEU LEU GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2HH 218 PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3HH 218 PHE THR PHE SER THR TYR GLY MET HIS TRP VAL ARG GLN SEQRES 4HH 218 ALA PRO GLY LYS GLY LEU GLU TRP VAL ALA VAL ILE SER SEQRES 5HH 218 TYR ASP GLY SER ASN LYS TYR TYR ALA ASP SER VAL LYS SEQRES 6HH 218 GLY ARG PHE THR ILE SER ARG ASP ASN SER LYS ASN THR SEQRES 7HH 218 LEU TYR LEU GLN MET ASN SER LEU ARG ALA GLU ASP THR SEQRES 8HH 218 ALA VAL TYR TYR CYS ALA ARG GLU ASN PHE ASP ALA PHE SEQRES 9HH 218 ASP VAL TRP GLY GLN GLY THR LEU VAL THR VAL SER SER SEQRES 10HH 218 ALA SER THR LYS GLY PRO SER VAL PHE PRO LEU ALA PRO SEQRES 11HH 218 SER SER LYS SER THR SER GLY GLY THR ALA ALA LEU GLY SEQRES 12HH 218 CYS LEU VAL LYS ASP TYR PHE PRO GLU PRO VAL THR VAL SEQRES 13HH 218 SER TRP ASN SER GLY ALA LEU THR SER GLY VAL HIS THR SEQRES 14HH 218 PHE PRO ALA VAL LEU GLN SER SER GLY LEU TYR SER LEU SEQRES 15HH 218 SER SER VAL VAL THR VAL PRO SER SER SER LEU GLY THR SEQRES 16HH 218 GLN THR TYR ILE CYS ASN VAL ASN HIS LYS PRO SER ASN SEQRES 17HH 218 THR LYS VAL ASP LYS LYS VAL GLU PRO LYS SEQRES 1MM 218 GLN SER VAL LEU THR GLN PRO PRO SER ALA SER GLY THR SEQRES 2MM 218 PRO GLY GLN ARG VAL THR ILE SER CYS THR GLY SER SER SEQRES 3MM 218 SER ASN ILE GLY ALA GLY TYR ASP VAL HIS TRP TYR GLN SEQRES 4MM 218 GLN LEU PRO GLY THR ALA PRO LYS LEU LEU ILE TYR SER SEQRES 5MM 218 ASN SER GLN ARG PRO SER GLY VAL PRO ASP ARG PHE SER SEQRES 6MM 218 GLY SER LYS SER GLY THR SER ALA SER LEU ALA ILE SER SEQRES 7MM 218 GLY LEU ARG SER GLU ASP GLU ALA ASP TYR TYR CYS ALA SEQRES 8MM 218 ALA TRP ASP ASP SER LEU ASN GLY GLN VAL VAL PHE GLY SEQRES 9MM 218 GLY GLY THR LYS LEU THR VAL LEU GLY GLN PRO LYS ALA SEQRES 10MM 218 ASN PRO THR VAL THR LEU PHE PRO PRO SER SER GLU GLU SEQRES 11MM 218 LEU GLN ALA ASN LYS ALA THR LEU VAL CYS LEU ILE SER SEQRES 12MM 218 ASP PHE TYR PRO GLY ALA VAL THR VAL ALA TRP LYS ALA SEQRES 13MM 218 ASP GLY SER PRO VAL LYS ALA GLY VAL GLU THR THR LYS SEQRES 14MM 218 PRO SER LYS GLN SER ASN ASN LYS TYR ALA ALA SER SER SEQRES 15MM 218 TYR LEU SER LEU THR PRO GLU GLN TRP LYS SER HIS ARG SEQRES 16MM 218 SER TYR SER CYS GLN VAL THR HIS GLU GLY SER THR VAL SEQRES 17MM 218 GLU LYS THR VAL ALA PRO THR GLU CYS SER SEQRES 1AA 181 THR PRO ALA ALA PRO PRO LYS ALA VAL LEU LYS LEU GLU SEQRES 2AA 181 PRO GLN TRP ILE ASN VAL LEU GLN GLU ASP SER VAL THR SEQRES 3AA 181 LEU THR CYS ARG GLY THR HIS SER PRO GLU SER ASP SER SEQRES 4AA 181 ILE GLN TRP PHE HIS ASN GLY ASN LEU ILE PRO THR HIS SEQRES 5AA 181 THR GLN PRO SER TYR ARG PHE LYS ALA ASN ASN ASN ASP SEQRES 6AA 181 SER GLY GLU TYR THR CYS GLN THR GLY GLN THR SER LEU SEQRES 7AA 181 SER ASP PRO VAL HIS LEU THR VAL LEU SER GLU TRP LEU SEQRES 8AA 181 VAL LEU GLN THR PRO HIS LEU GLU PHE GLN GLU GLY GLU SEQRES 9AA 181 THR ILE VAL LEU ARG CYS HIS SER TRP LYS ASP LYS PRO SEQRES 10AA 181 LEU VAL LYS VAL THR PHE PHE GLN ASN GLY LYS SER LYS SEQRES 11AA 181 LYS PHE SER ARG SER ASP PRO ASN PHE SER ILE PRO GLN SEQRES 12AA 181 ALA ASN HIS SER HIS SER GLY ASP TYR HIS CYS THR GLY SEQRES 13AA 181 ASN ILE GLY TYR THR LEU TYR SER SER LYS PRO VAL THR SEQRES 14AA 181 ILE THR VAL GLN ALA PRO HIS HIS HIS HIS HIS HIS SEQRES 1LL 218 GLN SER VAL LEU THR GLN PRO PRO SER ALA SER GLY THR SEQRES 2LL 218 PRO GLY GLN ARG VAL THR ILE SER CYS THR GLY SER SER SEQRES 3LL 218 SER ASN ILE GLY ALA GLY TYR ASP VAL HIS TRP TYR GLN SEQRES 4LL 218 GLN LEU PRO GLY THR ALA PRO LYS LEU LEU ILE TYR SER SEQRES 5LL 218 ASN SER GLN ARG PRO SER GLY VAL PRO ASP ARG PHE SER SEQRES 6LL 218 GLY SER LYS SER GLY THR SER ALA SER LEU ALA ILE SER SEQRES 7LL 218 GLY LEU ARG SER GLU ASP GLU ALA ASP TYR TYR CYS ALA SEQRES 8LL 218 ALA TRP ASP ASP SER LEU ASN GLY GLN VAL VAL PHE GLY SEQRES 9LL 218 GLY GLY THR LYS LEU THR VAL LEU GLY GLN PRO LYS ALA SEQRES 10LL 218 ASN PRO THR VAL THR LEU PHE PRO PRO SER SER GLU GLU SEQRES 11LL 218 LEU GLN ALA ASN LYS ALA THR LEU VAL CYS LEU ILE SER SEQRES 12LL 218 ASP PHE TYR PRO GLY ALA VAL THR VAL ALA TRP LYS ALA SEQRES 13LL 218 ASP GLY SER PRO VAL LYS ALA GLY VAL GLU THR THR LYS SEQRES 14LL 218 PRO SER LYS GLN SER ASN ASN LYS TYR ALA ALA SER SER SEQRES 15LL 218 TYR LEU SER LEU THR PRO GLU GLN TRP LYS SER HIS ARG SEQRES 16LL 218 SER TYR SER CYS GLN VAL THR HIS GLU GLY SER THR VAL SEQRES 17LL 218 GLU LYS THR VAL ALA PRO THR GLU CYS SER SEQRES 1II 218 GLU VAL GLN LEU LEU GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2II 218 PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3II 218 PHE THR PHE SER THR TYR GLY MET HIS TRP VAL ARG GLN SEQRES 4II 218 ALA PRO GLY LYS GLY LEU GLU TRP VAL ALA VAL ILE SER SEQRES 5II 218 TYR ASP GLY SER ASN LYS TYR TYR ALA ASP SER VAL LYS SEQRES 6II 218 GLY ARG PHE THR ILE SER ARG ASP ASN SER LYS ASN THR SEQRES 7II 218 LEU TYR LEU GLN MET ASN SER LEU ARG ALA GLU ASP THR SEQRES 8II 218 ALA VAL TYR TYR CYS ALA ARG GLU ASN PHE ASP ALA PHE SEQRES 9II 218 ASP VAL TRP GLY GLN GLY THR LEU VAL THR VAL SER SER SEQRES 10II 218 ALA SER THR LYS GLY PRO SER VAL PHE PRO LEU ALA PRO SEQRES 11II 218 SER SER LYS SER THR SER GLY GLY THR ALA ALA LEU GLY SEQRES 12II 218 CYS LEU VAL LYS ASP TYR PHE PRO GLU PRO VAL THR VAL SEQRES 13II 218 SER TRP ASN SER GLY ALA LEU THR SER GLY VAL HIS THR SEQRES 14II 218 PHE PRO ALA VAL LEU GLN SER SER GLY LEU TYR SER LEU SEQRES 15II 218 SER SER VAL VAL THR VAL PRO SER SER SER LEU GLY THR SEQRES 16II 218 GLN THR TYR ILE CYS ASN VAL ASN HIS LYS PRO SER ASN SEQRES 17II 218 THR LYS VAL ASP LYS LYS VAL GLU PRO LYS SEQRES 1BB 181 THR PRO ALA ALA PRO PRO LYS ALA VAL LEU LYS LEU GLU SEQRES 2BB 181 PRO GLN TRP ILE ASN VAL LEU GLN GLU ASP SER VAL THR SEQRES 3BB 181 LEU THR CYS ARG GLY THR HIS SER PRO GLU SER ASP SER SEQRES 4BB 181 ILE GLN TRP PHE HIS ASN GLY ASN LEU ILE PRO THR HIS SEQRES 5BB 181 THR GLN PRO SER TYR ARG PHE LYS ALA ASN ASN ASN ASP SEQRES 6BB 181 SER GLY GLU TYR THR CYS GLN THR GLY GLN THR SER LEU SEQRES 7BB 181 SER ASP PRO VAL HIS LEU THR VAL LEU SER GLU TRP LEU SEQRES 8BB 181 VAL LEU GLN THR PRO HIS LEU GLU PHE GLN GLU GLY GLU SEQRES 9BB 181 THR ILE VAL LEU ARG CYS HIS SER TRP LYS ASP LYS PRO SEQRES 10BB 181 LEU VAL LYS VAL THR PHE PHE GLN ASN GLY LYS SER LYS SEQRES 11BB 181 LYS PHE SER ARG SER ASP PRO ASN PHE SER ILE PRO GLN SEQRES 12BB 181 ALA ASN HIS SER HIS SER GLY ASP TYR HIS CYS THR GLY SEQRES 13BB 181 ASN ILE GLY TYR THR LEU TYR SER SER LYS PRO VAL THR SEQRES 14BB 181 ILE THR VAL GLN ALA PRO HIS HIS HIS HIS HIS HIS HET PG4 HH 301 31 HET NAG AA 301 28 HET GOL LL 301 14 HET PG4 II 301 31 HET NAG A 1 28 HET NAG A 2 28 HETNAM PG4 TETRAETHYLENE GLYCOL HETNAM NAG N-ACETYL-D-GLUCOSAMINE HETNAM GOL GLYCEROL HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL FORMUL 7 PG4 2(C8 H18 O5) FORMUL 8 NAG 3(C8 H15 N O6) FORMUL 9 GOL C3 H8 O3 FORMUL 12 HOH *277(H2 O) HELIX 1 AA1 THRHH 28 TYRHH 32 5 5 HELIX 2 AA2 ARGHH 87 THRHH 91 5 5 HELIX 3 AA3 SERHH 160 ALAHH 162 5 3 HELIX 4 AA4 LYSHH 205 ASNHH 208 5 4 HELIX 5 AA5 ARGMM 81 GLUMM 85 5 5 HELIX 6 AA6 ASNAA 104 SERAA 108 5 5 HELIX 7 AA7 LYSAA 156 LYSAA 158 5 3 HELIX 8 AA8 ASNAA 187 SERAA 191 5 5 HELIX 9 AA9 ARGLL 81 GLULL 85 5 5 HELIX 10 AB1 SERLL 127 ALALL 133 1 7 HELIX 11 AB2 THRLL 187 SERLL 193 1 7 HELIX 12 AB3 THRII 28 TYRII 32 5 5 HELIX 13 AB4 ASNBB 104 SERBB 108 5 5 HELIX 14 AB5 LYSBB 156 LYSBB 158 5 3 HELIX 15 AB6 ASNBB 187 SERBB 191 5 5 SHEET 1 AA1 4 GLNHH 3 SERHH 7 0 SHEET 2 AA1 4 LEUHH 18 SERHH 25 -1 O ALAHH 23 N LEUHH 5 SHEET 3 AA1 4 THRHH 78 METHH 83 -1 O METHH 83 N LEUHH 18 SHEET 4 AA1 4 PHEHH 68 ASPHH 73 -1 N SERHH 71 O TYRHH 80 SHEET 1 AA2 6 GLYHH 10 VALHH 12 0 SHEET 2 AA2 6 THRHH 111 VALHH 115 1 O THRHH 114 N VALHH 12 SHEET 3 AA2 6 ALAHH 92 ASNHH 100 -1 N ALAHH 92 O VALHH 113 SHEET 4 AA2 6 METHH 34 GLNHH 39 -1 N VALHH 37 O TYRHH 95 SHEET 5 AA2 6 LEUHH 45 ILEHH 51 -1 O VALHH 48 N TRPHH 36 SHEET 6 AA2 6 LYSHH 58 TYRHH 60 -1 O TYRHH 59 N VALHH 50 SHEET 1 AA3 4 GLYHH 10 VALHH 12 0 SHEET 2 AA3 4 THRHH 111 VALHH 115 1 O THRHH 114 N VALHH 12 SHEET 3 AA3 4 ALAHH 92 ASNHH 100 -1 N ALAHH 92 O VALHH 113 SHEET 4 AA3 4 ALAHH 103 TRPHH 107 -1 O ALAHH 103 N ASNHH 100 SHEET 1 AA4 4 SERHH 124 LEUHH 128 0 SHEET 2 AA4 4 LEUHH 142 TYRHH 149 -1 O GLYHH 143 N LEUHH 128 SHEET 3 AA4 4 TYRHH 180 VALHH 186 -1 O TYRHH 180 N TYRHH 149 SHEET 4 AA4 4 VALHH 167 THRHH 169 -1 N HISHH 168 O VALHH 185 SHEET 1 AA5 4 SERHH 124 LEUHH 128 0 SHEET 2 AA5 4 LEUHH 142 TYRHH 149 -1 O GLYHH 143 N LEUHH 128 SHEET 3 AA5 4 TYRHH 180 VALHH 186 -1 O TYRHH 180 N TYRHH 149 SHEET 4 AA5 4 VALHH 173 LEUHH 174 -1 N VALHH 173 O SERHH 181 SHEET 1 AA6 3 THRHH 155 TRPHH 158 0 SHEET 2 AA6 3 ILEHH 199 HISHH 204 -1 O ASNHH 201 N SERHH 157 SHEET 3 AA6 3 THRHH 209 LYSHH 214 -1 O VALHH 211 N VALHH 202 SHEET 1 AA7 5 SERMM 9 GLYMM 12 0 SHEET 2 AA7 5 THRMM 107 VALMM 111 1 O LYSMM 108 N ALAMM 10 SHEET 3 AA7 5 ALAMM 86 ASPMM 94 -1 N ALAMM 86 O LEUMM 109 SHEET 4 AA7 5 HISMM 36 GLNMM 40 -1 N TYRMM 38 O TYRMM 89 SHEET 5 AA7 5 LYSMM 47 ILEMM 50 -1 O ILEMM 50 N TRPMM 37 SHEET 1 AA8 4 SERMM 9 GLYMM 12 0 SHEET 2 AA8 4 THRMM 107 VALMM 111 1 O LYSMM 108 N ALAMM 10 SHEET 3 AA8 4 ALAMM 86 ASPMM 94 -1 N ALAMM 86 O LEUMM 109 SHEET 4 AA8 4 GLNMM 100 PHEMM 103 -1 O GLNMM 100 N ASPMM 94 SHEET 1 AA9 3 VALMM 18 THRMM 23 0 SHEET 2 AA9 3 SERMM 72 ILEMM 77 -1 O LEUMM 75 N ILEMM 20 SHEET 3 AA9 3 PHEMM 64 SERMM 69 -1 N SERMM 67 O SERMM 74 SHEET 1 AB1 3 THRMM 120 THRMM 122 0 SHEET 2 AB1 3 LEUMM 141 PHEMM 145 -1 O LEUMM 141 N THRMM 122 SHEET 3 AB1 3 TYRMM 178 SERMM 181 -1 O ALAMM 180 N ILEMM 142 SHEET 1 AB2 2 GLNMM 200 HISMM 203 0 SHEET 2 AB2 2 SERMM 206 GLUMM 209 -1 O SERMM 206 N HISMM 203 SHEET 1 AB3 3 LEUAA 52 GLUAA 55 0 SHEET 2 AB3 3 SERAA 66 CYSAA 71 -1 O THRAA 68 N GLUAA 55 SHEET 3 AB3 3 SERAA 98 LYSAA 102 -1 O PHEAA 101 N VALAA 67 SHEET 1 AB4 5 ASNAA 60 LEUAA 62 0 SHEET 2 AB4 5 VALAA 124 LEUAA 129 1 O LEUAA 129 N VALAA 61 SHEET 3 AB4 5 GLYAA 109 GLNAA 114 -1 N GLYAA 109 O LEUAA 126 SHEET 4 AB4 5 GLNAA 83 HISAA 86 -1 N PHEAA 85 O THRAA 112 SHEET 5 AB4 5 ASNAA 89 LEUAA 90 -1 O ASNAA 89 N HISAA 86 SHEET 1 AB5 3 LEUAA 133 GLNAA 136 0 SHEET 2 AB5 3 ILEAA 148 SERAA 154 -1 O ARGAA 151 N GLNAA 136 SHEET 3 AB5 3 ASNAA 180 ILEAA 183 -1 O PHEAA 181 N LEUAA 150 SHEET 1 AB6 5 GLUAA 141 GLNAA 143 0 SHEET 2 AB6 5 VALAA 210 GLNAA 215 1 O GLNAA 215 N PHEAA 142 SHEET 3 AB6 5 GLYAA 192 ILEAA 200 -1 N TYRAA 194 O VALAA 210 SHEET 4 AB6 5 LEUAA 160 GLNAA 167 -1 N THRAA 164 O THRAA 197 SHEET 5 AB6 5 SERAA 171 SERAA 175 -1 O LYSAA 172 N PHEAA 165 SHEET 1 AB7 4 GLUAA 141 GLNAA 143 0 SHEET 2 AB7 4 VALAA 210 GLNAA 215 1 O GLNAA 215 N PHEAA 142 SHEET 3 AB7 4 GLYAA 192 ILEAA 200 -1 N TYRAA 194 O VALAA 210 SHEET 4 AB7 4 THRAA 203 SERAA 206 -1 O TYRAA 205 N GLYAA 198 SHEET 1 AB8 5 SERLL 9 GLYLL 12 0 SHEET 2 AB8 5 THRLL 107 VALLL 111 1 O THRLL 110 N ALALL 10 SHEET 3 AB8 5 ALALL 86 ASPLL 94 -1 N ALALL 86 O LEULL 109 SHEET 4 AB8 5 VALLL 35 GLNLL 40 -1 N HISLL 36 O ALALL 91 SHEET 5 AB8 5 LYSLL 47 ILELL 50 -1 O LEULL 49 N TRPLL 37 SHEET 1 AB9 4 SERLL 9 GLYLL 12 0 SHEET 2 AB9 4 THRLL 107 VALLL 111 1 O THRLL 110 N ALALL 10 SHEET 3 AB9 4 ALALL 86 ASPLL 94 -1 N ALALL 86 O LEULL 109 SHEET 4 AB9 4 GLNLL 100 PHELL 103 -1 O GLNLL 100 N ASPLL 94 SHEET 1 AC1 3 VALLL 18 THRLL 23 0 SHEET 2 AC1 3 SERLL 72 ILELL 77 -1 O LEULL 75 N ILELL 20 SHEET 3 AC1 3 PHELL 64 SERLL 69 -1 N SERLL 69 O SERLL 72 SHEET 1 AC2 4 VALLL 121 PHELL 124 0 SHEET 2 AC2 4 ALALL 136 PHELL 145 -1 O LEULL 141 N THRLL 122 SHEET 3 AC2 4 TYRLL 178 LEULL 186 -1 O TYRLL 178 N PHELL 145 SHEET 4 AC2 4 VALLL 165 THRLL 167 -1 N GLULL 166 O TYRLL 183 SHEET 1 AC3 4 VALLL 121 PHELL 124 0 SHEET 2 AC3 4 ALALL 136 PHELL 145 -1 O LEULL 141 N THRLL 122 SHEET 3 AC3 4 TYRLL 178 LEULL 186 -1 O TYRLL 178 N PHELL 145 SHEET 4 AC3 4 SERLL 171 LYSLL 172 -1 N SERLL 171 O ALALL 179 SHEET 1 AC4 4 SERLL 159 PROLL 160 0 SHEET 2 AC4 4 THRLL 151 ALALL 156 -1 N ALALL 156 O SERLL 159 SHEET 3 AC4 4 TYRLL 197 HISLL 203 -1 O GLNLL 200 N ALALL 153 SHEET 4 AC4 4 SERLL 206 VALLL 212 -1 O VALLL 212 N TYRLL 197 SHEET 1 AC5 4 GLNII 3 SERII 7 0 SHEET 2 AC5 4 LEUII 18 SERII 25 -1 O SERII 21 N SERII 7 SHEET 3 AC5 4 THRII 78 METII 83 -1 O LEUII 79 N CYSII 22 SHEET 4 AC5 4 PHEII 68 ASPII 73 -1 N SERII 71 O TYRII 80 SHEET 1 AC6 6 LEUII 11 VALII 12 0 SHEET 2 AC6 6 THRII 111 VALII 115 1 O THRII 114 N VALII 12 SHEET 3 AC6 6 ALAII 92 GLUII 99 -1 N ALAII 92 O VALII 113 SHEET 4 AC6 6 METII 34 GLNII 39 -1 N VALII 37 O TYRII 95 SHEET 5 AC6 6 LEUII 45 ILEII 51 -1 O GLUII 46 N ARGII 38 SHEET 6 AC6 6 LYSII 58 TYRII 60 -1 O TYRII 59 N VALII 50 SHEET 1 AC7 4 LEUII 11 VALII 12 0 SHEET 2 AC7 4 THRII 111 VALII 115 1 O THRII 114 N VALII 12 SHEET 3 AC7 4 ALAII 92 GLUII 99 -1 N ALAII 92 O VALII 113 SHEET 4 AC7 4 PHEII 104 TRPII 107 -1 O VALII 106 N ARGII 98 SHEET 1 AC8 3 LEUII 145 TYRII 149 0 SHEET 2 AC8 3 TYRII 180 SERII 183 -1 O TYRII 180 N TYRII 149 SHEET 3 AC8 3 VALII 173 LEUII 174 -1 N VALII 173 O SERII 181 SHEET 1 AC9 3 VALBB 51 GLUBB 55 0 SHEET 2 AC9 3 SERBB 66 ARGBB 72 -1 O THRBB 68 N GLUBB 55 SHEET 3 AC9 3 SERBB 98 LYSBB 102 -1 O TYRBB 99 N LEUBB 69 SHEET 1 AD1 5 ASNBB 60 LEUBB 62 0 SHEET 2 AD1 5 VALBB 124 LEUBB 129 1 O LEUBB 129 N VALBB 61 SHEET 3 AD1 5 GLYBB 109 THRBB 115 -1 N TYRBB 111 O VALBB 124 SHEET 4 AD1 5 ILEBB 82 HISBB 86 -1 N GLNBB 83 O GLNBB 114 SHEET 5 AD1 5 ASNBB 89 LEUBB 90 -1 O ASNBB 89 N HISBB 86 SHEET 1 AD2 3 LEUBB 133 GLNBB 136 0 SHEET 2 AD2 3 ILEBB 148 SERBB 154 -1 O ARGBB 151 N GLNBB 136 SHEET 3 AD2 3 ASNBB 180 ILEBB 183 -1 O PHEBB 181 N LEUBB 150 SHEET 1 AD3 5 GLUBB 141 PHEBB 142 0 SHEET 2 AD3 5 VALBB 210 VALBB 214 1 O THRBB 213 N PHEBB 142 SHEET 3 AD3 5 GLYBB 192 ILEBB 200 -1 N GLYBB 192 O ILEBB 212 SHEET 4 AD3 5 LEUBB 160 GLNBB 167 -1 N PHEBB 166 O HISBB 195 SHEET 5 AD3 5 LYSBB 170 SERBB 175 -1 O LYSBB 172 N PHEBB 165 SHEET 1 AD4 4 GLUBB 141 PHEBB 142 0 SHEET 2 AD4 4 VALBB 210 VALBB 214 1 O THRBB 213 N PHEBB 142 SHEET 3 AD4 4 GLYBB 192 ILEBB 200 -1 N GLYBB 192 O ILEBB 212 SHEET 4 AD4 4 THRBB 203 SERBB 206 -1 O TYRBB 205 N GLYBB 198 SSBOND 1 CYSHH 22 CYSHH 96 1555 1555 2.07 SSBOND 2 CYSHH 144 CYSHH 200 1555 1555 2.03 SSBOND 3 CYSMM 22 CYSMM 90 1555 1555 2.07 SSBOND 4 CYSMM 140 CYSMM 199 1555 1555 2.04 SSBOND 5 CYSAA 71 CYSAA 113 1555 1555 2.05 SSBOND 6 CYSAA 152 CYSAA 196 1555 1555 2.07 SSBOND 7 CYSLL 22 CYSLL 90 1555 1555 2.06 SSBOND 8 CYSLL 140 CYSLL 199 1555 1555 2.04 SSBOND 9 CYSII 22 CYSII 96 1555 1555 2.07 SSBOND 10 CYSBB 71 CYSBB 113 1555 1555 2.06 SSBOND 11 CYSBB 152 CYSBB 196 1555 1555 2.07 LINK ND2 ASNAA 187 C1 NAGAA 301 1555 1555 1.45 LINK ND2 ASNBB 187 C1 NAG A 1 1555 1555 1.45 LINK O4 NAG A 1 C1 NAG A 2 1555 1555 1.35 CISPEP 1 PHEHH 150 PROHH 151 0 -5.20 CISPEP 2 GLUHH 152 PROHH 153 0 -4.42 CISPEP 3 TYRMM 146 PROMM 147 0 0.53 CISPEP 4 GLUAA 55 PROAA 56 0 -10.92 CISPEP 5 TYRLL 146 PROLL 147 0 -2.10 CISPEP 6 PHEII 150 PROII 151 0 -16.86 CISPEP 7 GLUII 152 PROII 153 0 -7.57 CISPEP 8 GLUBB 55 PROBB 56 0 -5.96 CRYST1 95.728 95.728 186.038 90.00 90.00 90.00 P 43 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 0.010446 0.000000 0.000000 0.00000 SCALE2 0.000000 0.010446 0.000000 0.00000 SCALE3 0.000000 0.000000 0.005375 0.00000