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HEADER LYASE 16-OCT-00 1E9I TITLE ENOLASE FROM E.COLI COMPND MOL_ID: 1; COMPND 2 MOLECULE: ENOLASE; COMPND 3 CHAIN: A, B, C, D; COMPND 4 SYNONYM: 2-PHOSPHOGLYCERATE DEHYDRATASE, 2-PHOSPHO-D- COMPND 5 GLYCERATE HYDRO-LYASE; COMPND 6 EC: 4.2.1.11; COMPND 7 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI; SOURCE 3 GENE: ENO; SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 5 EXPRESSION_SYSTEM_STRAIN: BL21(DE3); SOURCE 6 EXPRESSION_SYSTEM_PLASMID: PET11A KEYWDS DEGRADOSOME, LYASE EXPDTA X-RAY DIFFRACTION AUTHOR K.KUHNEL,A.J.CARPOUSIS,B.LUISI REVDAT 3 01-APR-03 1E9I 1 JRNL REVDAT 2 26-NOV-01 1E9I 1 JRNL REVDAT 1 15-MAR-01 1E9I 0 JRNL AUTH K.KUHNEL,B.F.LUISI JRNL TITL CRYSTAL STRUCTURE OF THE ESCHERICHIA COLI RNA JRNL TITL 2 DEGRADOSOME COMPONENT ENOLASE. JRNL REF J.MOL.BIOL. V. 313 583 2001 JRNL REFN ASTM JMOBAK UK ISSN 0022-2836 REMARK 1 REMARK 2 REMARK 2 RESOLUTION. 2.48 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : CNS 0.9 REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE- REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU, REMARK 3 : READ,RICE,SIMONSON,WARREN REMARK 3 REMARK 3 REFINEMENT TARGET : NULL REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.48 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 27.97 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000 REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 93.8 REMARK 3 NUMBER OF REFLECTIONS : 63664 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 SET) : 0.229 REMARK 3 FREE R VALUE : 0.276 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.100 REMARK 3 FREE R VALUE TEST SET COUNT : 6458 REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.003 REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : 10 REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.47 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.56 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 72.70 REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 4500 REMARK 3 BIN R VALUE (WORKING SET) : 0.2600 REMARK 3 BIN FREE R VALUE : 0.3180 REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 9.40 REMARK 3 BIN FREE R VALUE TEST SET COUNT : 466 REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.015 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 12340 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 5 REMARK 3 SOLVENT ATOMS : NULL REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 33.00 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 49.10 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : -7.96000 REMARK 3 B22 (A**2) : 19.94000 REMARK 3 B33 (A**2) : -11.98000 REMARK 3 B12 (A**2) : 0.00000 REMARK 3 B13 (A**2) : 6.63000 REMARK 3 B23 (A**2) : 0.00000 REMARK 3 REMARK 3 ESTIMATED COORDINATE ERROR. REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.34 REMARK 3 ESD FROM SIGMAA (A) : 0.24 REMARK 3 LOW RESOLUTION CUTOFF (A) : 27.00 REMARK 3 REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR. REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.42 REMARK 3 ESD FROM C-V SIGMAA (A) : 0.38 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. REMARK 3 BOND LENGTHS (A) : 0.007 REMARK 3 BOND ANGLES (DEGREES) : 1.10 REMARK 3 DIHEDRAL ANGLES (DEGREES) : 22.00 REMARK 3 IMPROPER ANGLES (DEGREES) : 0.76 REMARK 3 REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED REMARK 3 REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA REMARK 3 MAIN-CHAIN BOND (A**2) : 3.250 ; 1.500 REMARK 3 MAIN-CHAIN ANGLE (A**2) : 4.260 ; 2.000 REMARK 3 SIDE-CHAIN BOND (A**2) : 0.000 ; 2.000 REMARK 3 SIDE-CHAIN ANGLE (A**2) : 0.000 ; 2.500 REMARK 3 REMARK 3 BULK SOLVENT MODELING. REMARK 3 METHOD USED : FLAT MODEL REMARK 3 KSOL : 0.33 REMARK 3 BSOL : 37.75 REMARK 3 REMARK 3 NCS MODEL : NULL REMARK 3 REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL REMARK 3 REMARK 3 PARAMETER FILE 1 : PROTEIN_REP.PARAM REMARK 3 PARAMETER FILE 2 : WATER_REP.PARAM REMARK 3 PARAMETER FILE 3 : ION.PARAM REMARK 3 PARAMETER FILE 4 : NULL REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP REMARK 3 TOPOLOGY FILE 2 : WATER.TOP REMARK 3 TOPOLOGY FILE 3 : ION.TOP REMARK 3 TOPOLOGY FILE 4 : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1E9I COMPLIES WITH FORMAT V. 3.0, 1-DEC-2006 REMARK 4 REMARK 4 THIS IS THE REMEDIATED VERSION OF THIS PDB ENTRY. REMARK 4 REMEDIATED DATA FILE REVISION 3.101 (2007-05-31) REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY EBI . REMARK 100 THE EBI ID CODE IS EBI-5431 . REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 15-FEB-1999 REMARK 200 TEMPERATURE (KELVIN) : 100.0 REMARK 200 PH : 7.00 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : ELETTRA REMARK 200 BEAMLINE : 5.2R REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.472 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : MIRRORS REMARK 200 REMARK 200 DETECTOR TYPE : IP REMARK 200 DETECTOR MANUFACTURER : MAR345 REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO REMARK 200 DATA SCALING SOFTWARE : SCALEPACK REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 63664 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.480 REMARK 200 RESOLUTION RANGE LOW (A) : 27.970 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 3.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 98.3 REMARK 200 DATA REDUNDANCY : 4.000 REMARK 200 R MERGE (I) : 0.05300 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 33.0000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.47 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.56 REMARK 200 COMPLETENESS FOR SHELL (%) : 90.0 REMARK 200 DATA REDUNDANCY IN SHELL : 4.00 REMARK 200 R MERGE FOR SHELL (I) : 0.10700 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 10.000 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: AMORE REMARK 200 STARTING MODEL: PDB ENTRY 1EBG REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 53.10 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.65 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: PH 7 REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,Y,-Z REMARK 290 3555 1/2+X,1/2+Y,Z REMARK 290 4555 1/2-X,1/2+Y,-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 0.00000 REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 53.94150 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 75.00300 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 53.94150 REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 75.00300 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 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT REMARK 300 WHICH CONSISTS OF 4 CHAIN(S). SEE REMARK 350 FOR REMARK 300 INFORMATION ON GENERATING THE BIOLOGICAL MOLECULE(S). REMARK 350 REMARK 350 GENERATING THE BIOMOLECULE 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 APPLY THE FOLLOWING TO CHAINS: A, B, W, X, Y, Z 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 BIOMOLECULE: 2 REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D 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 ALA A 431 REMARK 465 ALA B 431 REMARK 465 PHE C 251 REMARK 465 TYR C 252 REMARK 465 LYS C 253 REMARK 465 GLY C 429 REMARK 465 GLN C 430 REMARK 465 ALA C 431 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 LYS A 2 CG CD CE NZ REMARK 470 GLN A 76 CG CD OE1 NE2 REMARK 470 ILE A 94 CG1 CG2 CD1 REMARK 470 LYS A 197 CG CD CE NZ REMARK 470 GLU A 235 CG CD OE1 OE2 REMARK 470 GLU A 270 CG CD OE1 OE2 REMARK 470 GLU A 278 CG CD OE1 OE2 REMARK 470 LYS A 324 CG CD CE NZ REMARK 470 GLU A 328 CG CD OE1 OE2 REMARK 470 GLU A 417 CG CD OE1 OE2 REMARK 470 LYS B 55 CG CD CE NZ REMARK 470 LYS B 142 CG CD CE NZ REMARK 470 ASN B 162 CG OD1 ND2 REMARK 470 LYS B 176 CG CD CE NZ REMARK 470 GLU B 180 CG CD OE1 OE2 REMARK 470 LYS B 194 CG CD CE NZ REMARK 470 LYS B 197 CG CD CE NZ REMARK 470 LYS B 199 CG CD CE NZ REMARK 470 GLU B 220 CG CD OE1 OE2 REMARK 470 LYS B 230 CG CD CE NZ REMARK 470 LYS B 238 CG CD CE NZ REMARK 470 SER B 249 OG REMARK 470 LYS B 253 CG CD CE NZ REMARK 470 ASP B 254 CG OD1 OD2 REMARK 470 LYS B 256 CG CD CE NZ REMARK 470 VAL B 258 CG1 CG2 REMARK 470 ASN B 264 CG OD1 ND2 REMARK 470 LYS B 265 CG CD CE NZ REMARK 470 PHE B 267 CG CD1 CD2 CE1 CE2 CZ REMARK 470 THR B 268 OG1 CG2 REMARK 470 GLU B 270 CG CD OE1 OE2 REMARK 470 GLU B 271 CG CD OE1 OE2 REMARK 470 THR B 273 OG1 CG2 REMARK 470 GLU B 278 CG CD OE1 OE2 REMARK 470 LYS B 281 CG CD CE NZ REMARK 470 TYR B 302 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 LYS B 305 CG CD CE NZ REMARK 470 LYS B 310 CG CD CE NZ REMARK 470 LYS B 327 CG CD CE NZ REMARK 470 GLU B 328 CG CD OE1 OE2 REMARK 470 LYS B 332 CG CD CE NZ REMARK 470 LYS B 359 CG CD CE NZ REMARK 470 GLU B 417 CG CD OE1 OE2 REMARK 470 LYS C 55 CG CD CE NZ REMARK 470 ASP C 160 CG OD1 OD2 REMARK 470 ASN C 161 CG OD1 ND2 REMARK 470 ASN C 162 CG OD1 ND2 REMARK 470 ASP C 164 CG OD1 OD2 REMARK 470 ILE C 165 CG1 CG2 CD1 REMARK 470 GLN C 166 CG CD OE1 NE2 REMARK 470 LYS C 176 CG CD CE NZ REMARK 470 LYS C 197 CG CD CE NZ REMARK 470 LYS C 199 CG CD CE NZ REMARK 470 ASN C 214 CG OD1 ND2 REMARK 470 SER C 217 OG REMARK 470 LYS C 230 CG CD CE NZ REMARK 470 LEU C 236 CG CD1 CD2 REMARK 470 LYS C 238 CG CD CE NZ REMARK 470 CYS C 246 SG REMARK 470 ASP C 254 CG OD1 OD2 REMARK 470 LYS C 256 CG CD CE NZ REMARK 470 TYR C 257 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 VAL C 258 CG1 CG2 REMARK 470 GLU C 262 CG CD OE1 OE2 REMARK 470 ASN C 264 CG OD1 ND2 REMARK 470 LYS C 265 CG CD CE NZ REMARK 470 PHE C 267 CG CD1 CD2 CE1 CE2 CZ REMARK 470 SER C 269 OG REMARK 470 GLU C 270 CG CD OE1 OE2 REMARK 470 GLU C 271 CG CD OE1 OE2 REMARK 470 THR C 273 OG1 CG2 REMARK 470 HIS C 274 CG ND1 CD2 CE1 NE2 REMARK 470 GLU C 277 CG CD OE1 OE2 REMARK 470 GLU C 278 CG CD OE1 OE2 REMARK 470 LYS C 281 CG CD CE NZ REMARK 470 GLN C 282 CG CD OE1 NE2 REMARK 470 LEU C 292 CG CD1 CD2 REMARK 470 GLU C 294 CG CD OE1 OE2 REMARK 470 TRP C 297 CG CD1 CD2 NE1 CE2 CE3 CZ2 REMARK 470 TRP C 297 CZ3 CH2 REMARK 470 PHE C 300 CG CD1 CD2 CE1 CE2 CZ REMARK 470 TYR C 302 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 GLN C 303 CG CD OE1 NE2 REMARK 470 LYS C 305 CG CD CE NZ REMARK 470 VAL C 306 CG1 CG2 REMARK 470 LEU C 313 CG CD1 CD2 REMARK 470 GLU C 331 CG CD OE1 OE2 REMARK 470 ASN C 336 CG OD1 ND2 REMARK 470 LYS C 359 CG CD CE NZ REMARK 470 LYS C 425 CG CD CE NZ REMARK 470 LYS D 2 CG CD CE NZ REMARK 470 GLU D 27 CG CD OE1 OE2 REMARK 470 LYS D 55 CG CD CE NZ REMARK 470 LYS D 142 CG CD CE NZ REMARK 470 ASP D 160 CG OD1 OD2 REMARK 470 LYS D 197 CG CD CE NZ REMARK 470 LYS D 230 CG CD CE NZ REMARK 470 LYS D 253 CG CD CE NZ REMARK 470 LYS D 256 CG CD CE NZ REMARK 470 GLU D 262 CG CD OE1 OE2 REMARK 470 LYS D 265 CG CD CE NZ 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 REMARK 500 O HOH X 81 O HOH Z 142 2.08 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS REMARK 500 REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15 REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375 REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS. REMARK 500 REMARK 500 DISTANCE CUTOFF: REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE REMARK 500 O HOH W 14 O HOH W 14 2656 1.17 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),F6.3) REMARK 500 REMARK 500 EXPECTED VALUES: ENGH AND HUBER, 1991 REMARK 500 REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION REMARK 500 MET A 150 SD MET A 150 CE 0.044 REMARK 500 MET A 357 SD MET A 357 CE -0.047 REMARK 500 MET A 396 SD MET A 396 CE -0.045 REMARK 500 MET B 33 SD MET B 33 CE -0.042 REMARK 500 MET C 357 SD MET C 357 CE -0.059 REMARK 500 MET D 184 SD MET D 184 CE -0.059 REMARK 500 MET D 244 CG MET D 244 SD 0.040 REMARK 500 MET D 396 CG MET D 396 SD 0.045 REMARK 500 MET D 396 SD MET D 396 CE -0.051 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: ENGH AND HUBER, 1991 REMARK 500 REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3 REMARK 500 PRO A 140 N - CA - C ANGL. DEV. = 5.9 DEGREES REMARK 500 GLY A 141 N - CA - C ANGL. DEV. = 5.6 DEGREES REMARK 500 VAL A 147 N - CA - C ANGL. DEV. = -6.5 DEGREES REMARK 500 PRO A 148 N - CA - C ANGL. DEV. = 5.8 DEGREES REMARK 500 MET A 149 N - CA - C ANGL. DEV. = -9.4 DEGREES REMARK 500 MET A 150 N - CA - C ANGL. DEV. = 6.0 DEGREES REMARK 500 GLY A 216 N - CA - C ANGL. DEV. = 5.4 DEGREES REMARK 500 ALA A 243 N - CA - C ANGL. DEV. = -5.6 DEGREES REMARK 500 ALA A 247 N - CA - C ANGL. DEV. = -5.4 DEGREES REMARK 500 THR A 268 N - CA - C ANGL. DEV. = -7.7 DEGREES REMARK 500 GLY A 308 N - CA - C ANGL. DEV. = 6.2 DEGREES REMARK 500 GLY A 346 N - CA - C ANGL. DEV. = 6.4 DEGREES REMARK 500 GLY A 394 N - CA - C ANGL. DEV. = 6.7 DEGREES REMARK 500 TYR A 421 N - CA - C ANGL. DEV. = -6.5 DEGREES REMARK 500 GLY B 72 N - CA - C ANGL. DEV. = 5.1 DEGREES REMARK 500 MET B 149 N - CA - C ANGL. DEV. = -5.2 DEGREES REMARK 500 ASN B 151 N - CA - C ANGL. DEV. = -5.3 DEGREES REMARK 500 GLY B 346 N - CA - C ANGL. DEV. = 5.5 DEGREES REMARK 500 GLU C 49 N - CA - C ANGL. DEV. = -5.2 DEGREES REMARK 500 PRO C 73 N - CA - C ANGL. DEV. = 5.1 DEGREES REMARK 500 GLY C 98 N - CA - C ANGL. DEV. = 5.0 DEGREES REMARK 500 VAL C 147 N - CA - C ANGL. DEV. = -5.0 DEGREES REMARK 500 PRO C 148 N - CA - C ANGL. DEV. = 5.9 DEGREES REMARK 500 MET C 149 N - CA - C ANGL. DEV. = -5.7 DEGREES REMARK 500 GLY C 346 N - CA - C ANGL. DEV. = 5.9 DEGREES REMARK 500 SER C 368 N - CA - C ANGL. DEV. = 5.0 DEGREES REMARK 500 TYR C 421 N - CA - C ANGL. DEV. = -5.5 DEGREES REMARK 500 VAL D 147 N - CA - C ANGL. DEV. = -6.8 DEGREES REMARK 500 PRO D 148 N - CA - C ANGL. DEV. = 6.6 DEGREES REMARK 500 MET D 149 N - CA - C ANGL. DEV. = -7.2 DEGREES REMARK 500 MET D 150 N - CA - C ANGL. DEV. = 5.0 DEGREES REMARK 500 GLN D 166 N - CA - C ANGL. DEV. = 5.8 DEGREES REMARK 500 GLU D 167 N - CA - C ANGL. DEV. = 5.1 DEGREES REMARK 500 PHE D 168 N - CA - C ANGL. DEV. = -6.1 DEGREES REMARK 500 MET D 169 N - CA - C ANGL. DEV. = 5.3 DEGREES REMARK 500 THR D 241 N - CA - C ANGL. DEV. = -5.1 DEGREES REMARK 500 THR D 268 N - CA - C ANGL. DEV. = -6.7 DEGREES REMARK 500 GLY D 308 N - CA - C ANGL. DEV. = 6.6 DEGREES REMARK 500 ASP D 309 N - CA - C ANGL. DEV. = 5.7 DEGREES REMARK 500 GLY D 346 N - CA - C ANGL. DEV. = 6.0 DEGREES REMARK 500 HIS D 369 N - CA - C ANGL. DEV. = -5.1 DEGREES REMARK 500 GLY D 394 N - CA - C ANGL. DEV. = 6.1 DEGREES REMARK 500 TYR D 421 N - CA - C ANGL. DEV. = -5.6 DEGREES 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 M RES CSSEQI PSI PHI REMARK 500 ARG C 398 120.07 76.58 DBREF 1E9I A 1 431 UNP P0A6P9 ENO_ECOLI 1 431 DBREF 1E9I B 1 431 UNP P0A6P9 ENO_ECOLI 1 431 DBREF 1E9I C 1 431 UNP P0A6P9 ENO_ECOLI 1 431 DBREF 1E9I D 1 431 UNP P0A6P9 ENO_ECOLI 1 431 SEQRES 1 A 431 SER LYS ILE VAL LYS ILE ILE GLY ARG GLU ILE ILE ASP SEQRES 2 A 431 SER ARG GLY ASN PRO THR VAL GLU ALA GLU VAL HIS LEU SEQRES 3 A 431 GLU GLY GLY PHE VAL GLY MET ALA ALA ALA PRO SER GLY SEQRES 4 A 431 ALA SER THR GLY SER ARG GLU ALA LEU GLU LEU ARG ASP SEQRES 5 A 431 GLY ASP LYS SER ARG PHE LEU GLY LYS GLY VAL THR LYS SEQRES 6 A 431 ALA VAL ALA ALA VAL ASN GLY PRO ILE ALA GLN ALA LEU SEQRES 7 A 431 ILE GLY LYS ASP ALA LYS ASP GLN ALA GLY ILE ASP LYS SEQRES 8 A 431 ILE MET ILE ASP LEU ASP GLY THR GLU ASN LYS SER LYS SEQRES 9 A 431 PHE GLY ALA ASN ALA ILE LEU ALA VAL SER LEU ALA ASN SEQRES 10 A 431 ALA LYS ALA ALA ALA ALA ALA LYS GLY MET PRO LEU TYR SEQRES 11 A 431 GLU HIS ILE ALA GLU LEU ASN GLY THR PRO GLY LYS TYR SEQRES 12 A 431 SER MET PRO VAL PRO MET MET ASN ILE ILE ASN GLY GLY SEQRES 13 A 431 GLU HIS ALA ASP ASN ASN VAL ASP ILE GLN GLU PHE MET SEQRES 14 A 431 ILE GLN PRO VAL GLY ALA LYS THR VAL LYS GLU ALA ILE SEQRES 15 A 431 ARG MET GLY SER GLU VAL PHE HIS HIS LEU ALA LYS VAL SEQRES 16 A 431 LEU LYS ALA LYS GLY MET ASN THR ALA VAL GLY ASP GLU SEQRES 17 A 431 GLY GLY TYR ALA PRO ASN LEU GLY SER ASN ALA GLU ALA SEQRES 18 A 431 LEU ALA VAL ILE ALA GLU ALA VAL LYS ALA ALA GLY TYR SEQRES 19 A 431 GLU LEU GLY LYS ASP ILE THR LEU ALA MET ASP CYS ALA SEQRES 20 A 431 ALA SER GLU PHE TYR LYS ASP GLY LYS TYR VAL LEU ALA SEQRES 21 A 431 GLY GLU GLY ASN LYS ALA PHE THR SER GLU GLU PHE THR SEQRES 22 A 431 HIS PHE LEU GLU GLU LEU THR LYS GLN TYR PRO ILE VAL SEQRES 23 A 431 SER ILE GLU ASP GLY LEU ASP GLU SER ASP TRP ASP GLY SEQRES 24 A 431 PHE ALA TYR GLN THR LYS VAL LEU GLY ASP LYS ILE GLN SEQRES 25 A 431 LEU VAL GLY ASP ASP LEU PHE VAL THR ASN THR LYS ILE SEQRES 26 A 431 LEU LYS GLU GLY ILE GLU LYS GLY ILE ALA ASN SER ILE SEQRES 27 A 431 LEU ILE LYS PHE ASN GLN ILE GLY SER LEU THR GLU THR SEQRES 28 A 431 LEU ALA ALA ILE LYS MET ALA LYS ASP ALA GLY TYR THR SEQRES 29 A 431 ALA VAL ILE SER HIS ARG SER GLY GLU THR GLU ASP ALA SEQRES 30 A 431 THR ILE ALA ASP LEU ALA VAL GLY THR ALA ALA GLY GLN SEQRES 31 A 431 ILE LYS THR GLY SER MET SER ARG SER ASP ARG VAL ALA SEQRES 32 A 431 LYS TYR ASN GLN LEU ILE ARG ILE GLU GLU ALA LEU GLY SEQRES 33 A 431 GLU LYS ALA PRO TYR ASN GLY ARG LYS GLU ILE LYS GLY SEQRES 34 A 431 GLN ALA SEQRES 1 B 431 SER LYS ILE VAL LYS ILE ILE GLY ARG GLU ILE ILE ASP SEQRES 2 B 431 SER ARG GLY ASN PRO THR VAL GLU ALA GLU VAL HIS LEU SEQRES 3 B 431 GLU GLY GLY PHE VAL GLY MET ALA ALA ALA PRO SER GLY SEQRES 4 B 431 ALA SER THR GLY SER ARG GLU ALA LEU GLU LEU ARG ASP SEQRES 5 B 431 GLY ASP LYS SER ARG PHE LEU GLY LYS GLY VAL THR LYS SEQRES 6 B 431 ALA VAL ALA ALA VAL ASN GLY PRO ILE ALA GLN ALA LEU SEQRES 7 B 431 ILE GLY LYS ASP ALA LYS ASP GLN ALA GLY ILE ASP LYS SEQRES 8 B 431 ILE MET ILE ASP LEU ASP GLY THR GLU ASN LYS SER LYS SEQRES 9 B 431 PHE GLY ALA ASN ALA ILE LEU ALA VAL SER LEU ALA ASN SEQRES 10 B 431 ALA LYS ALA ALA ALA ALA ALA LYS GLY MET PRO LEU TYR SEQRES 11 B 431 GLU HIS ILE ALA GLU LEU ASN GLY THR PRO GLY LYS TYR SEQRES 12 B 431 SER MET PRO VAL PRO MET MET ASN ILE ILE ASN GLY GLY SEQRES 13 B 431 GLU HIS ALA ASP ASN ASN VAL ASP ILE GLN GLU PHE MET SEQRES 14 B 431 ILE GLN PRO VAL GLY ALA LYS THR VAL LYS GLU ALA ILE SEQRES 15 B 431 ARG MET GLY SER GLU VAL PHE HIS HIS LEU ALA LYS VAL SEQRES 16 B 431 LEU LYS ALA LYS GLY MET ASN THR ALA VAL GLY ASP GLU SEQRES 17 B 431 GLY GLY TYR ALA PRO ASN LEU GLY SER ASN ALA GLU ALA SEQRES 18 B 431 LEU ALA VAL ILE ALA GLU ALA VAL LYS ALA ALA GLY TYR SEQRES 19 B 431 GLU LEU GLY LYS ASP ILE THR LEU ALA MET ASP CYS ALA SEQRES 20 B 431 ALA SER GLU PHE TYR LYS ASP GLY LYS TYR VAL LEU ALA SEQRES 21 B 431 GLY GLU GLY ASN LYS ALA PHE THR SER GLU GLU PHE THR SEQRES 22 B 431 HIS PHE LEU GLU GLU LEU THR LYS GLN TYR PRO ILE VAL SEQRES 23 B 431 SER ILE GLU ASP GLY LEU ASP GLU SER ASP TRP ASP GLY SEQRES 24 B 431 PHE ALA TYR GLN THR LYS VAL LEU GLY ASP LYS ILE GLN SEQRES 25 B 431 LEU VAL GLY ASP ASP LEU PHE VAL THR ASN THR LYS ILE SEQRES 26 B 431 LEU LYS GLU GLY ILE GLU LYS GLY ILE ALA ASN SER ILE SEQRES 27 B 431 LEU ILE LYS PHE ASN GLN ILE GLY SER LEU THR GLU THR SEQRES 28 B 431 LEU ALA ALA ILE LYS MET ALA LYS ASP ALA GLY TYR THR SEQRES 29 B 431 ALA VAL ILE SER HIS ARG SER GLY GLU THR GLU ASP ALA SEQRES 30 B 431 THR ILE ALA ASP LEU ALA VAL GLY THR ALA ALA GLY GLN SEQRES 31 B 431 ILE LYS THR GLY SER MET SER ARG SER ASP ARG VAL ALA SEQRES 32 B 431 LYS TYR ASN GLN LEU ILE ARG ILE GLU GLU ALA LEU GLY SEQRES 33 B 431 GLU LYS ALA PRO TYR ASN GLY ARG LYS GLU ILE LYS GLY SEQRES 34 B 431 GLN ALA SEQRES 1 C 431 SER LYS ILE VAL LYS ILE ILE GLY ARG GLU ILE ILE ASP SEQRES 2 C 431 SER ARG GLY ASN PRO THR VAL GLU ALA GLU VAL HIS LEU SEQRES 3 C 431 GLU GLY GLY PHE VAL GLY MET ALA ALA ALA PRO SER GLY SEQRES 4 C 431 ALA SER THR GLY SER ARG GLU ALA LEU GLU LEU ARG ASP SEQRES 5 C 431 GLY ASP LYS SER ARG PHE LEU GLY LYS GLY VAL THR LYS SEQRES 6 C 431 ALA VAL ALA ALA VAL ASN GLY PRO ILE ALA GLN ALA LEU SEQRES 7 C 431 ILE GLY LYS ASP ALA LYS ASP GLN ALA GLY ILE ASP LYS SEQRES 8 C 431 ILE MET ILE ASP LEU ASP GLY THR GLU ASN LYS SER LYS SEQRES 9 C 431 PHE GLY ALA ASN ALA ILE LEU ALA VAL SER LEU ALA ASN SEQRES 10 C 431 ALA LYS ALA ALA ALA ALA ALA LYS GLY MET PRO LEU TYR SEQRES 11 C 431 GLU HIS ILE ALA GLU LEU ASN GLY THR PRO GLY LYS TYR SEQRES 12 C 431 SER MET PRO VAL PRO MET MET ASN ILE ILE ASN GLY GLY SEQRES 13 C 431 GLU HIS ALA ASP ASN ASN VAL ASP ILE GLN GLU PHE MET SEQRES 14 C 431 ILE GLN PRO VAL GLY ALA LYS THR VAL LYS GLU ALA ILE SEQRES 15 C 431 ARG MET GLY SER GLU VAL PHE HIS HIS LEU ALA LYS VAL SEQRES 16 C 431 LEU LYS ALA LYS GLY MET ASN THR ALA VAL GLY ASP GLU SEQRES 17 C 431 GLY GLY TYR ALA PRO ASN LEU GLY SER ASN ALA GLU ALA SEQRES 18 C 431 LEU ALA VAL ILE ALA GLU ALA VAL LYS ALA ALA GLY TYR SEQRES 19 C 431 GLU LEU GLY LYS ASP ILE THR LEU ALA MET ASP CYS ALA SEQRES 20 C 431 ALA SER GLU PHE TYR LYS ASP GLY LYS TYR VAL LEU ALA SEQRES 21 C 431 GLY GLU GLY ASN LYS ALA PHE THR SER GLU GLU PHE THR SEQRES 22 C 431 HIS PHE LEU GLU GLU LEU THR LYS GLN TYR PRO ILE VAL SEQRES 23 C 431 SER ILE GLU ASP GLY LEU ASP GLU SER ASP TRP ASP GLY SEQRES 24 C 431 PHE ALA TYR GLN THR LYS VAL LEU GLY ASP LYS ILE GLN SEQRES 25 C 431 LEU VAL GLY ASP ASP LEU PHE VAL THR ASN THR LYS ILE SEQRES 26 C 431 LEU LYS GLU GLY ILE GLU LYS GLY ILE ALA ASN SER ILE SEQRES 27 C 431 LEU ILE LYS PHE ASN GLN ILE GLY SER LEU THR GLU THR SEQRES 28 C 431 LEU ALA ALA ILE LYS MET ALA LYS ASP ALA GLY TYR THR SEQRES 29 C 431 ALA VAL ILE SER HIS ARG SER GLY GLU THR GLU ASP ALA SEQRES 30 C 431 THR ILE ALA ASP LEU ALA VAL GLY THR ALA ALA GLY GLN SEQRES 31 C 431 ILE LYS THR GLY SER MET SER ARG SER ASP ARG VAL ALA SEQRES 32 C 431 LYS TYR ASN GLN LEU ILE ARG ILE GLU GLU ALA LEU GLY SEQRES 33 C 431 GLU LYS ALA PRO TYR ASN GLY ARG LYS GLU ILE LYS GLY SEQRES 34 C 431 GLN ALA SEQRES 1 D 431 SER LYS ILE VAL LYS ILE ILE GLY ARG GLU ILE ILE ASP SEQRES 2 D 431 SER ARG GLY ASN PRO THR VAL GLU ALA GLU VAL HIS LEU SEQRES 3 D 431 GLU GLY GLY PHE VAL GLY MET ALA ALA ALA PRO SER GLY SEQRES 4 D 431 ALA SER THR GLY SER ARG GLU ALA LEU GLU LEU ARG ASP SEQRES 5 D 431 GLY ASP LYS SER ARG PHE LEU GLY LYS GLY VAL THR LYS SEQRES 6 D 431 ALA VAL ALA ALA VAL ASN GLY PRO ILE ALA GLN ALA LEU SEQRES 7 D 431 ILE GLY LYS ASP ALA LYS ASP GLN ALA GLY ILE ASP LYS SEQRES 8 D 431 ILE MET ILE ASP LEU ASP GLY THR GLU ASN LYS SER LYS SEQRES 9 D 431 PHE GLY ALA ASN ALA ILE LEU ALA VAL SER LEU ALA ASN SEQRES 10 D 431 ALA LYS ALA ALA ALA ALA ALA LYS GLY MET PRO LEU TYR SEQRES 11 D 431 GLU HIS ILE ALA GLU LEU ASN GLY THR PRO GLY LYS TYR SEQRES 12 D 431 SER MET PRO VAL PRO MET MET ASN ILE ILE ASN GLY GLY SEQRES 13 D 431 GLU HIS ALA ASP ASN ASN VAL ASP ILE GLN GLU PHE MET SEQRES 14 D 431 ILE GLN PRO VAL GLY ALA LYS THR VAL LYS GLU ALA ILE SEQRES 15 D 431 ARG MET GLY SER GLU VAL PHE HIS HIS LEU ALA LYS VAL SEQRES 16 D 431 LEU LYS ALA LYS GLY MET ASN THR ALA VAL GLY ASP GLU SEQRES 17 D 431 GLY GLY TYR ALA PRO ASN LEU GLY SER ASN ALA GLU ALA SEQRES 18 D 431 LEU ALA VAL ILE ALA GLU ALA VAL LYS ALA ALA GLY TYR SEQRES 19 D 431 GLU LEU GLY LYS ASP ILE THR LEU ALA MET ASP CYS ALA SEQRES 20 D 431 ALA SER GLU PHE TYR LYS ASP GLY LYS TYR VAL LEU ALA SEQRES 21 D 431 GLY GLU GLY ASN LYS ALA PHE THR SER GLU GLU PHE THR SEQRES 22 D 431 HIS PHE LEU GLU GLU LEU THR LYS GLN TYR PRO ILE VAL SEQRES 23 D 431 SER ILE GLU ASP GLY LEU ASP GLU SER ASP TRP ASP GLY SEQRES 24 D 431 PHE ALA TYR GLN THR LYS VAL LEU GLY ASP LYS ILE GLN SEQRES 25 D 431 LEU VAL GLY ASP ASP LEU PHE VAL THR ASN THR LYS ILE SEQRES 26 D 431 LEU LYS GLU GLY ILE GLU LYS GLY ILE ALA ASN SER ILE SEQRES 27 D 431 LEU ILE LYS PHE ASN GLN ILE GLY SER LEU THR GLU THR SEQRES 28 D 431 LEU ALA ALA ILE LYS MET ALA LYS ASP ALA GLY TYR THR SEQRES 29 D 431 ALA VAL ILE SER HIS ARG SER GLY GLU THR GLU ASP ALA SEQRES 30 D 431 THR ILE ALA ASP LEU ALA VAL GLY THR ALA ALA GLY GLN SEQRES 31 D 431 ILE LYS THR GLY SER MET SER ARG SER ASP ARG VAL ALA SEQRES 32 D 431 LYS TYR ASN GLN LEU ILE ARG ILE GLU GLU ALA LEU GLY SEQRES 33 D 431 GLU LYS ALA PRO TYR ASN GLY ARG LYS GLU ILE LYS GLY SEQRES 34 D 431 GLN ALA HET MG A1431 1 HET MG B1431 1 HET MG C1429 1 HET MG D1432 1 HET MG D1433 1 HET SO4 D1434 5 HETNAM MG MAGNESIUM ION HETNAM SO4 SULFATE ION FORMUL 5 MG 5(MG 2+) FORMUL 10 SO4 O4 S 2- FORMUL 11 HOH *506(H2 O) HELIX 1 1 ARG A 57 LYS A 61 5 5 HELIX 2 2 VAL A 63 GLY A 72 1 10 HELIX 3 3 GLY A 72 ILE A 79 1 8 HELIX 4 4 ASP A 85 GLY A 98 1 14 HELIX 5 5 GLY A 106 LYS A 125 1 20 HELIX 6 6 PRO A 128 GLY A 138 1 11 HELIX 7 7 GLY A 156 ALA A 159 5 4 HELIX 8 8 THR A 177 LYS A 199 1 23 HELIX 9 9 SER A 217 ALA A 232 1 16 HELIX 10 10 ALA A 247 GLU A 250 5 4 HELIX 11 11 THR A 268 TYR A 283 1 16 HELIX 12 12 ASP A 296 GLY A 308 1 13 HELIX 13 13 ASN A 322 LYS A 332 1 11 HELIX 14 14 LYS A 341 ILE A 345 5 5 HELIX 15 15 SER A 347 GLY A 362 1 16 HELIX 16 16 ALA A 377 THR A 386 1 10 HELIX 17 17 ARG A 398 GLY A 416 1 19 HELIX 18 18 GLU A 417 ALA A 419 5 3 HELIX 19 19 ASN A 422 ILE A 427 5 6 HELIX 20 20 ARG B 57 LYS B 61 5 5 HELIX 21 21 VAL B 63 GLY B 72 1 10 HELIX 22 22 GLY B 72 ALA B 77 1 6 HELIX 23 23 ASP B 85 GLY B 98 1 14 HELIX 24 24 GLY B 106 LYS B 125 1 20 HELIX 25 25 PRO B 128 ASN B 137 1 10 HELIX 26 26 GLY B 156 ALA B 159 5 4 HELIX 27 27 THR B 177 LYS B 199 1 23 HELIX 28 28 SER B 217 ALA B 232 1 16 HELIX 29 29 ALA B 247 GLU B 250 5 4 HELIX 30 30 ALA B 260 GLY B 263 5 4 HELIX 31 31 THR B 268 TYR B 283 1 16 HELIX 32 32 ASP B 296 LEU B 307 1 12 HELIX 33 33 ASN B 322 LYS B 332 1 11 HELIX 34 34 LYS B 341 GLY B 346 1 6 HELIX 35 35 SER B 347 ASP B 360 1 14 HELIX 36 36 ALA B 377 THR B 386 1 10 HELIX 37 37 ARG B 398 GLY B 416 1 19 HELIX 38 38 GLU B 417 ALA B 419 5 3 HELIX 39 39 ASN B 422 GLU B 426 5 5 HELIX 40 40 ARG C 57 LYS C 61 5 5 HELIX 41 41 VAL C 63 GLY C 72 1 10 HELIX 42 42 GLY C 72 ILE C 79 1 8 HELIX 43 43 ASP C 85 GLY C 98 1 14 HELIX 44 44 GLY C 106 LYS C 125 1 20 HELIX 45 45 PRO C 128 ASN C 137 1 10 HELIX 46 46 GLY C 156 ALA C 159 5 4 HELIX 47 47 THR C 177 ALA C 198 1 22 HELIX 48 48 SER C 217 GLY C 233 1 17 HELIX 49 49 THR C 268 TYR C 283 1 16 HELIX 50 50 ASP C 296 LEU C 307 1 12 HELIX 51 51 ASN C 322 LYS C 332 1 11 HELIX 52 52 LYS C 341 GLY C 346 1 6 HELIX 53 53 SER C 347 ALA C 361 1 15 HELIX 54 54 ALA C 377 ALA C 387 1 11 HELIX 55 55 ARG C 398 GLY C 416 1 19 HELIX 56 56 GLU C 417 ALA C 419 5 3 HELIX 57 57 ASN C 422 ILE C 427 5 6 HELIX 58 58 ARG D 57 LYS D 61 5 5 HELIX 59 59 VAL D 63 GLY D 72 1 10 HELIX 60 60 GLY D 72 ILE D 79 1 8 HELIX 61 61 ASP D 85 GLY D 98 1 14 HELIX 62 62 GLY D 106 LYS D 125 1 20 HELIX 63 63 PRO D 128 ASN D 137 1 10 HELIX 64 64 GLY D 156 ALA D 159 5 4 HELIX 65 65 THR D 177 ALA D 198 1 22 HELIX 66 66 ALA D 219 GLY D 233 1 15 HELIX 67 67 ALA D 247 GLU D 250 5 4 HELIX 68 68 THR D 268 TYR D 283 1 16 HELIX 69 69 ASP D 296 GLY D 308 1 13 HELIX 70 70 ASN D 322 LYS D 332 1 11 HELIX 71 71 LYS D 341 GLY D 346 1 6 HELIX 72 72 SER D 347 ALA D 361 1 15 HELIX 73 73 ALA D 377 THR D 386 1 10 HELIX 74 74 ARG D 398 GLY D 416 1 19 HELIX 75 75 GLU D 417 ALA D 419 5 3 HELIX 76 76 ASN D 422 ILE D 427 5 6 SHEET 1 A 3 ILE A 3 ILE A 6 0 SHEET 2 A 3 PRO A 18 LEU A 26 -1 O HIS A 25 N VAL A 4 SHEET 3 A 3 ARG A 9 ILE A 12 -1 O ARG A 9 N GLU A 21 SHEET 1 A1 3 ILE A 3 ILE A 6 0 SHEET 2 A1 3 PRO A 18 LEU A 26 -1 O HIS A 25 N VAL A 4 SHEET 3 A1 3 VAL A 31 ALA A 35 -1 O GLY A 32 N VAL A 24 SHEET 1 B 9 VAL A 147 PRO A 148 0 SHEET 2 B 9 GLY A 389 LYS A 392 1 O GLY A 389 N VAL A 147 SHEET 3 B 9 THR A 364 SER A 368 1 O ALA A 365 N GLN A 390 SHEET 4 B 9 SER A 337 ILE A 340 1 O ILE A 338 N VAL A 366 SHEET 5 B 9 GLN A 312 GLY A 315 1 O GLY A 315 N LEU A 339 SHEET 6 B 9 ILE A 285 GLU A 289 1 O VAL A 286 N GLN A 312 SHEET 7 B 9 THR A 241 ASP A 245 1 O LEU A 242 N VAL A 286 SHEET 8 B 9 GLU A 167 GLN A 171 -1 O GLU A 167 N ASP A 245 SHEET 9 B 9 MET A 150 ASN A 154 -1 O MET A 150 N ILE A 170 SHEET 1 C 3 TYR A 252 LYS A 253 0 SHEET 2 C 3 LYS A 256 LEU A 259 -1 O LYS A 256 N LYS A 253 SHEET 3 C 3 LYS A 265 PHE A 267 -1 O LYS A 265 N LEU A 259 SHEET 1 D 3 ILE B 3 ILE B 12 0 SHEET 2 D 3 PRO B 18 LEU B 26 -1 O THR B 19 N ILE B 11 SHEET 3 D 3 PHE B 30 ALA B 35 -1 O PHE B 30 N LEU B 26 SHEET 1 E 9 VAL B 147 PRO B 148 0 SHEET 2 E 9 GLN B 390 LYS B 392 1 N ILE B 391 O VAL B 147 SHEET 3 E 9 THR B 364 SER B 368 1 O ILE B 367 N LYS B 392 SHEET 4 E 9 SER B 337 ILE B 340 1 O ILE B 338 N VAL B 366 SHEET 5 E 9 GLN B 312 GLY B 315 1 O LEU B 313 N SER B 337 SHEET 6 E 9 ILE B 285 GLU B 289 1 O VAL B 286 N GLN B 312 SHEET 7 E 9 THR B 241 ASP B 245 1 O LEU B 242 N VAL B 286 SHEET 8 E 9 GLU B 167 GLN B 171 -1 O GLU B 167 N ASP B 245 SHEET 9 E 9 MET B 150 ASN B 154 -1 O MET B 150 N ILE B 170 SHEET 1 F 3 TYR B 252 LYS B 253 0 SHEET 2 F 3 LYS B 256 LEU B 259 -1 O LYS B 256 N LYS B 253 SHEET 3 F 3 LYS B 265 PHE B 267 -1 O LYS B 265 N LEU B 259 SHEET 1 G 3 ILE C 3 ILE C 12 0 SHEET 2 G 3 PRO C 18 LEU C 26 -1 O THR C 19 N ILE C 11 SHEET 3 G 3 VAL C 31 ALA C 35 -1 O GLY C 32 N VAL C 24 SHEET 1 H 9 VAL C 147 PRO C 148 0 SHEET 2 H 9 GLY C 389 LYS C 392 1 O GLY C 389 N VAL C 147 SHEET 3 H 9 THR C 364 SER C 368 1 O ALA C 365 N GLN C 390 SHEET 4 H 9 SER C 337 ILE C 340 1 O ILE C 338 N VAL C 366 SHEET 5 H 9 GLN C 312 GLY C 315 1 O GLY C 315 N LEU C 339 SHEET 6 H 9 ILE C 285 GLU C 289 1 O VAL C 286 N GLN C 312 SHEET 7 H 9 THR C 241 ASP C 245 1 O LEU C 242 N VAL C 286 SHEET 8 H 9 GLU C 167 GLN C 171 -1 O GLU C 167 N ASP C 245 SHEET 9 H 9 MET C 150 ASN C 154 -1 O MET C 150 N ILE C 170 SHEET 1 I 2 TYR C 257 VAL C 258 0 SHEET 2 I 2 ALA C 266 PHE C 267 -1 O PHE C 267 N TYR C 257 SHEET 1 J 3 ILE D 3 ILE D 12 0 SHEET 2 J 3 PRO D 18 LEU D 26 -1 O THR D 19 N ILE D 11 SHEET 3 J 3 VAL D 31 ALA D 35 -1 O GLY D 32 N VAL D 24 SHEET 1 K 9 VAL D 147 PRO D 148 0 SHEET 2 K 9 GLY D 389 LYS D 392 1 O GLY D 389 N VAL D 147 SHEET 3 K 9 THR D 364 SER D 368 1 O ALA D 365 N GLN D 390 SHEET 4 K 9 SER D 337 ILE D 340 1 O ILE D 338 N VAL D 366 SHEET 5 K 9 GLN D 312 GLY D 315 1 O GLY D 315 N LEU D 339 SHEET 6 K 9 ILE D 285 GLU D 289 1 O VAL D 286 N GLN D 312 SHEET 7 K 9 THR D 241 ASP D 245 1 O LEU D 242 N VAL D 286 SHEET 8 K 9 GLU D 167 GLN D 171 -1 O GLU D 167 N ASP D 245 SHEET 9 K 9 MET D 150 ASN D 154 -1 O MET D 150 N ILE D 170 SHEET 1 L 3 TYR D 252 LYS D 253 0 SHEET 2 L 3 LYS D 256 VAL D 258 0 SHEET 3 L 3 ALA D 266 PHE D 267 0 LINK MG MG A1431 OD2 ASP A 316 LINK MG MG A1431 O HOH Z 56 LINK MG MG A1431 OD2 ASP A 245 LINK MG MG A1431 OE2 GLU A 289 LINK MG MG A1431 O HOH Z 84 LINK MG MG A1431 O HOH Z 99 LINK MG MG B1431 OD2 ASP B 245 LINK MG MG B1431 OE2 GLU B 289 LINK MG MG B1431 OD2 ASP B 316 LINK MG MG B1431 O HOH Y 86 LINK MG MG B1431 O HOH Y 87 LINK MG MG C1429 O HOH X 99 LINK MG MG C1429 OE2 GLU C 289 LINK MG MG C1429 O HOH Z 142 LINK MG MG C1429 O HOH X 81 LINK MG MG D1432 OE2 GLU D 289 LINK MG MG D1432 OD2 ASP D 316 LINK MG MG D1432 O HOH W 82 LINK MG MG D1432 O HOH Z 147 LINK MG MG D1432 OD2 ASP D 245 LINK MG MG D1433 O HOH W 109 LINK MG MG D1433 O2 SO4 D1434 LINK MG MG D1433 O HOH W 108 LINK MG MG D1433 O SER D 41 LINK MG MG D1433 OG SER D 41 CRYST1 107.883 150.006 127.411 90.00 109.18 90.00 C 1 2 1 4 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 0.009269 0.000000 0.003224 0.00000 SCALE2 0.000000 0.006666 0.000000 0.00000 SCALE3 0.000000 0.000000 0.008310 0.00000 MTRIX1 1 -0.959910 -0.067360 -0.272100 51.40480 1 MTRIX2 1 -0.068800 -0.884390 0.461660 -5.53899 1 MTRIX3 1 -0.271740 0.461870 0.844300 8.97248 1 MTRIX1 2 0.993810 0.103560 0.040220 -11.81620 1 MTRIX2 2 -0.099570 0.669630 0.735990 42.34035 1 MTRIX3 2 0.049290 -0.735440 0.675790 29.33316 1 MTRIX1 3 -0.971780 -0.152240 -0.180200 38.67458 1 MTRIX2 3 -0.149470 -0.193590 0.969630 40.00534 1 MTRIX3 3 -0.182500 0.969200 0.165370 43.63807 1