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HEADER LYASE 08-FEB-06 2FYM TITLE CRYSTAL STRUCTURE OF E. COLI ENOLASE COMPLEXED WITH THE TITLE 2 MINIMAL BINDING SEGMENT OF RNASE E. COMPND MOL_ID: 1; COMPND 2 MOLECULE: ENOLASE; COMPND 3 CHAIN: A, C, D, F; 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; COMPND 8 MOL_ID: 2; COMPND 9 MOLECULE: RIBONUCLEASE E; COMPND 10 CHAIN: B, E; COMPND 11 FRAGMENT: RESIDUES 833-850; COMPND 12 SYNONYM: RNASE E; COMPND 13 EC: 3.1.4.-; COMPND 14 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI; SOURCE 3 ORGANISM_COMMON: BACTERIA; SOURCE 4 GENE: ENO; SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 6 EXPRESSION_SYSTEM_COMMON: BACTERIA; SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3); SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET11A; SOURCE 10 MOL_ID: 2; SOURCE 11 SYNTHETIC: YES; SOURCE 12 OTHER_DETAILS: THE E. COLI RNASE E PEPTIDE WAS SYNTHESIZED. KEYWDS RNA DEGRADOSOME, ENOLASE, RNASE E EXPDTA X-RAY DIFFRACTION AUTHOR V.CHANDRAN,B.F.LUISI REVDAT 2 11-APR-06 2FYM 1 JRNL REVDAT 1 28-FEB-06 2FYM 0 JRNL AUTH V.CHANDRAN,B.F.LUISI JRNL TITL RECOGNITION OF ENOLASE IN THE ESCHERICHIA COLI RNA JRNL TITL 2 DEGRADOSOME JRNL REF J.MOL.BIOL. V. 358 8 2006 JRNL REFN ASTM JMOBAK UK ISSN 0022-2836 REMARK 1 REMARK 2 REMARK 2 RESOLUTION. 1.60 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : REFMAC 5.2.0005 REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON REMARK 3 REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.60 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.99 REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL REMARK 3 COMPLETENESS FOR RANGE (%) : 90.9 REMARK 3 NUMBER OF REFLECTIONS : 205585 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) : 0.167 REMARK 3 R VALUE (WORKING SET) : 0.165 REMARK 3 FREE R VALUE : 0.201 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000 REMARK 3 FREE R VALUE TEST SET COUNT : 10847 REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : 20 REMARK 3 BIN RESOLUTION RANGE HIGH : 1.60 REMARK 3 BIN RESOLUTION RANGE LOW : 1.64 REMARK 3 REFLECTION IN BIN (WORKING SET) : 15113 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 91.22 REMARK 3 BIN R VALUE (WORKING SET) : 0.2010 REMARK 3 BIN FREE R VALUE SET COUNT : 820 REMARK 3 BIN FREE R VALUE : 0.2640 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 ALL ATOMS : 14807 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 20.67 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : -0.02000 REMARK 3 B22 (A**2) : -0.02000 REMARK 3 B33 (A**2) : 0.03000 REMARK 3 B12 (A**2) : 0.00000 REMARK 3 B13 (A**2) : -0.01000 REMARK 3 B23 (A**2) : 0.00000 REMARK 3 REMARK 3 ESTIMATED OVERALL COORDINATE ERROR. REMARK 3 ESU BASED ON R VALUE (A): 0.125 REMARK 3 ESU BASED ON FREE R VALUE (A): 0.091 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.052 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.234 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.968 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.954 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 13050 ; 0.009 ; 0.022 REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 17604 ; 1.157 ; 1.969 REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1744 ; 5.413 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 517 ;40.267 ;25.745 REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 2277 ;12.064 ;15.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 46 ;18.674 ;15.000 REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 2013 ; 0.083 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 9690 ; 0.004 ; 0.020 REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 7024 ; 0.194 ; 0.200 REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 9218 ; 0.302 ; 0.200 REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 1764 ; 0.137 ; 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): 69 ; 0.171 ; 0.200 REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 78 ; 0.147 ; 0.200 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): 8843 ; 0.844 ; 1.500 REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 13607 ; 1.237 ; 2.000 REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 4702 ; 2.697 ; 3.000 REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 3994 ; 3.078 ; 4.500 REMARK 3 REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT REMARK 3 RIGID-BOND RESTRAINTS (A**2): 13545 ; 2.495 ; 3.000 REMARK 3 SPHERICITY; FREE ATOMS (A**2): 1934 ; 3.556 ; 3.000 REMARK 3 SPHERICITY; BONDED ATOMS (A**2): 12873 ; 2.843 ; 3.000 REMARK 3 REMARK 3 NCS RESTRAINTS STATISTICS REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : 0 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 0 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: HYDROGENS HAVE BEEN ADDED IN THE REMARK 3 RIDING POSITIONS REMARK 4 REMARK 4 2FYM 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 3.100 (2007-03-17) REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB. REMARK 100 THE RCSB ID CODE IS RCSB036466. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 08-MAY-2004; 24-FEB-2004; 09- REMARK 200 MAR-2004; 08-MAY-2004 REMARK 200 TEMPERATURE (KELVIN) : 100; 100; 100; 100 REMARK 200 PH : 7.0; 8.2; 6.0; 7.5 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y; Y; N; Y REMARK 200 RADIATION SOURCE : ESRF; ESRF; ROTATING ANODE; REMARK 200 ESRF REMARK 200 BEAMLINE : ID14-4; ID29; ID14-4 REMARK 200 X-RAY GENERATOR MODEL : NULL; RIGAKU REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M; M; M; M REMARK 200 WAVELENGTH OR RANGE (A) : 1.0; 0.9782; 1.54; 1.0 REMARK 200 MONOCHROMATOR : GE(220) CRYSTAL; SI(111) REMARK 200 CRYSTAL; GE(220) CRYSTAL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : Q315R ADSC DETECTOR; ADSC REMARK 200 Q210 2D; IMAGE PLATE; Q315R REMARK 200 ADSC DETECTOR REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4; ADSC QUANTUM REMARK 200 4; RIGAKU RAXIS IV; ADSC REMARK 200 QUANTUM 4 REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO REMARK 200 DATA SCALING SOFTWARE : HKL REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 216432 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.600 REMARK 200 RESOLUTION RANGE LOW (A) : 20.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 91.1 REMARK 200 DATA REDUNDANCY : 10.300 REMARK 200 R MERGE (I) : 0.03400 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 13.7000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.63 REMARK 200 COMPLETENESS FOR SHELL (%) : 94.3 REMARK 200 DATA REDUNDANCY IN SHELL : 16.51 REMARK 200 R MERGE FOR SHELL (I) : 0.25300 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 2.450 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH; SINGLE WAVELENGTH; REMARK 200 SINGLE WAVELENGTH; SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: MOLREP REMARK 200 STARTING MODEL: ENOLASE STRUCTURE 1E9I REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 50.11 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.47 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 2.4M SODIUM MALONATE, PH 7.0, VAPOR REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 298.0K. 40% MPEG 550, REMARK 280 0.1M HEPES, PH 8.2, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE REMARK 280 298.0K. 8% PEG 4K, 0.2 M IMIDAZOLE MALEATE, PH 6.0, VAPOR REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 298.0K. 27% PEG 600, 0.1M REMARK 280 HEPES, PH 7.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE REMARK 280 298.0K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -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 62.10050 REMARK 290 SMTRY3 2 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 6 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, C 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: D, E, F 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 ILE B 16 REMARK 465 VAL B 17 REMARK 465 ARG B 18 REMARK 465 GLY C 263 REMARK 465 ASN C 264 REMARK 465 LYS C 265 REMARK 465 ALA C 431 REMARK 465 GLY D 261 REMARK 465 GLU D 262 REMARK 465 GLY D 263 REMARK 465 ALA D 431 REMARK 465 ILE E 16 REMARK 465 VAL E 17 REMARK 465 ARG E 18 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 LYS A 5 CG CD CE NZ REMARK 470 GLU A 235 CG CD OE1 OE2 REMARK 470 LYS A 256 CG CD CE NZ REMARK 470 ASN A 264 CG OD1 ND2 REMARK 470 LYS A 265 CG CD CE NZ REMARK 470 GLN A 282 CG CD OE1 NE2 REMARK 470 LYS A 310 CG CD CE NZ REMARK 470 LYS A 324 CG CD CE NZ REMARK 470 GLU A 331 CG CD OE1 OE2 REMARK 470 LYS C 305 CG CD CE NZ REMARK 470 GLU C 417 CG CD OE1 OE2 REMARK 470 GLU D 100 CG CD OE1 OE2 REMARK 470 ASP D 160 CG OD1 OD2 REMARK 470 ASN D 162 CG OD1 ND2 REMARK 470 LYS D 197 CG CD CE NZ REMARK 470 LYS D 253 CG CD CE NZ REMARK 470 ASP D 254 CG OD1 OD2 REMARK 470 ASN D 264 CG OD1 ND2 REMARK 470 GLU D 278 CG CD OE1 OE2 REMARK 470 LYS D 305 CG CD CE NZ REMARK 470 LYS D 324 CG CD CE NZ REMARK 470 GLU D 417 CG CD OE1 OE2 REMARK 470 LYS F 2 CG CD CE NZ REMARK 470 GLN F 76 CG CD OE1 NE2 REMARK 470 LYS F 265 CG CD CE NZ REMARK 470 LYS F 310 CG CD CE NZ REMARK 470 LYS F 324 CG CD CE NZ REMARK 470 LYS F 359 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 OG SER F 249 O HOH 1932 1.93 REMARK 500 O HOH 410 O HOH 1940 1.94 REMARK 500 O HOH 485 O HOH 1934 1.98 REMARK 500 O HOH 1236 O HOH 1933 2.11 REMARK 500 O HOH 324 O HOH 1938 2.16 REMARK 500 O HOH 941 O HOH 1937 2.17 REMARK 500 O HOH 303 O HOH 1926 2.18 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 GLU C 375 CB GLU C 375 CG 0.060 REMARK 500 GLU D 375 CB GLU D 375 CG 0.076 REMARK 500 PRO F 18 CB PRO F 18 CG -0.062 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 GLU A 375 CA - CB - CG ANGL. DEV. = 7.6 DEGREES REMARK 500 LYS C 392 N - CA - C ANGL. DEV. = -7.2 DEGREES REMARK 500 LEU F 236 CA - CB - CG ANGL. DEV. = 7.2 DEGREES REMARK 500 LEU F 236 CB - CG - CD2 ANGL. DEV. = 7.4 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 A 398 123.79 78.01 REMARK 500 ARG C 398 123.72 75.67 REMARK 500 ARG D 398 123.00 75.87 REMARK 500 ARG F 398 126.88 75.30 REMARK 525 REMARK 525 SOLVENT REMARK 525 THE FOLLOWING SOLVENT MOLECULES LIE FARTHER THAN EXPECTED REMARK 525 FROM THE PROTEIN OR NUCLEIC ACID MOLECULE AND MAY BE REMARK 525 ASSOCIATED WITH A SYMMETRY RELATED MOLECULE (M=MODEL REMARK 525 NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE REMARK 525 NUMBER; I=INSERTION CODE): REMARK 525 REMARK 525 M RES CSSEQI REMARK 525 HOH 748 DISTANCE = 5.72 ANGSTROMS REMARK 525 HOH 807 DISTANCE = 5.26 ANGSTROMS REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1E9I RELATED DB: PDB REMARK 900 THE SAME PROTEIN COMPLEXED WITH MINIMAL BINDING PEPTIDE REMARK 900 FROM RNASE E. DBREF 2FYM A 1 431 UNP P0A6P9 ENO_ECOLI 1 431 DBREF 2FYM C 1 431 UNP P0A6P9 ENO_ECOLI 1 431 DBREF 2FYM D 1 431 UNP P0A6P9 ENO_ECOLI 1 431 DBREF 2FYM F 1 431 UNP P0A6P9 ENO_ECOLI 1 431 DBREF 2FYM B 1 18 UNP P21513 RNE_ECOLI 833 850 DBREF 2FYM E 1 18 UNP P21513 RNE_ECOLI 833 850 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 18 ALA SER PRO GLU LEU ALA SER GLY LYS VAL TRP ILE ARG SEQRES 2 B 18 TYR PRO ILE VAL ARG 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 SEQRES 1 E 18 ALA SER PRO GLU LEU ALA SER GLY LYS VAL TRP ILE ARG SEQRES 2 E 18 TYR PRO ILE VAL ARG SEQRES 1 F 431 SER LYS ILE VAL LYS ILE ILE GLY ARG GLU ILE ILE ASP SEQRES 2 F 431 SER ARG GLY ASN PRO THR VAL GLU ALA GLU VAL HIS LEU SEQRES 3 F 431 GLU GLY GLY PHE VAL GLY MET ALA ALA ALA PRO SER GLY SEQRES 4 F 431 ALA SER THR GLY SER ARG GLU ALA LEU GLU LEU ARG ASP SEQRES 5 F 431 GLY ASP LYS SER ARG PHE LEU GLY LYS GLY VAL THR LYS SEQRES 6 F 431 ALA VAL ALA ALA VAL ASN GLY PRO ILE ALA GLN ALA LEU SEQRES 7 F 431 ILE GLY LYS ASP ALA LYS ASP GLN ALA GLY ILE ASP LYS SEQRES 8 F 431 ILE MET ILE ASP LEU ASP GLY THR GLU ASN LYS SER LYS SEQRES 9 F 431 PHE GLY ALA ASN ALA ILE LEU ALA VAL SER LEU ALA ASN SEQRES 10 F 431 ALA LYS ALA ALA ALA ALA ALA LYS GLY MET PRO LEU TYR SEQRES 11 F 431 GLU HIS ILE ALA GLU LEU ASN GLY THR PRO GLY LYS TYR SEQRES 12 F 431 SER MET PRO VAL PRO MET MET ASN ILE ILE ASN GLY GLY SEQRES 13 F 431 GLU HIS ALA ASP ASN ASN VAL ASP ILE GLN GLU PHE MET SEQRES 14 F 431 ILE GLN PRO VAL GLY ALA LYS THR VAL LYS GLU ALA ILE SEQRES 15 F 431 ARG MET GLY SER GLU VAL PHE HIS HIS LEU ALA LYS VAL SEQRES 16 F 431 LEU LYS ALA LYS GLY MET ASN THR ALA VAL GLY ASP GLU SEQRES 17 F 431 GLY GLY TYR ALA PRO ASN LEU GLY SER ASN ALA GLU ALA SEQRES 18 F 431 LEU ALA VAL ILE ALA GLU ALA VAL LYS ALA ALA GLY TYR SEQRES 19 F 431 GLU LEU GLY LYS ASP ILE THR LEU ALA MET ASP CYS ALA SEQRES 20 F 431 ALA SER GLU PHE TYR LYS ASP GLY LYS TYR VAL LEU ALA SEQRES 21 F 431 GLY GLU GLY ASN LYS ALA PHE THR SER GLU GLU PHE THR SEQRES 22 F 431 HIS PHE LEU GLU GLU LEU THR LYS GLN TYR PRO ILE VAL SEQRES 23 F 431 SER ILE GLU ASP GLY LEU ASP GLU SER ASP TRP ASP GLY SEQRES 24 F 431 PHE ALA TYR GLN THR LYS VAL LEU GLY ASP LYS ILE GLN SEQRES 25 F 431 LEU VAL GLY ASP ASP LEU PHE VAL THR ASN THR LYS ILE SEQRES 26 F 431 LEU LYS GLU GLY ILE GLU LYS GLY ILE ALA ASN SER ILE SEQRES 27 F 431 LEU ILE LYS PHE ASN GLN ILE GLY SER LEU THR GLU THR SEQRES 28 F 431 LEU ALA ALA ILE LYS MET ALA LYS ASP ALA GLY TYR THR SEQRES 29 F 431 ALA VAL ILE SER HIS ARG SER GLY GLU THR GLU ASP ALA SEQRES 30 F 431 THR ILE ALA ASP LEU ALA VAL GLY THR ALA ALA GLY GLN SEQRES 31 F 431 ILE LYS THR GLY SER MET SER ARG SER ASP ARG VAL ALA SEQRES 32 F 431 LYS TYR ASN GLN LEU ILE ARG ILE GLU GLU ALA LEU GLY SEQRES 33 F 431 GLU LYS ALA PRO TYR ASN GLY ARG LYS GLU ILE LYS GLY SEQRES 34 F 431 GLN ALA HET MG A1431 1 HET MG C1431 1 HET MG D1431 1 HET MG F1431 1 HETNAM MG MAGNESIUM ION FORMUL 7 MG 4(MG 2+) FORMUL 11 HOH *1930(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 ASN A 137 1 10 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 ALA A 260 GLY A 263 5 4 HELIX 12 12 THR A 268 TYR A 283 1 16 HELIX 13 13 ASP A 296 GLY A 308 1 13 HELIX 14 14 ASN A 322 LYS A 332 1 11 HELIX 15 15 LYS A 341 ILE A 345 5 5 HELIX 16 16 SER A 347 ALA A 361 1 15 HELIX 17 17 ALA A 377 THR A 386 1 10 HELIX 18 18 ARG A 398 GLY A 416 1 19 HELIX 19 19 GLU A 417 ALA A 419 5 3 HELIX 20 20 ASN A 422 ILE A 427 5 6 HELIX 21 21 SER B 2 SER B 7 1 6 HELIX 22 22 ARG C 57 LYS C 61 5 5 HELIX 23 23 VAL C 63 GLY C 72 1 10 HELIX 24 24 GLY C 72 ILE C 79 1 8 HELIX 25 25 ASP C 85 GLY C 98 1 14 HELIX 26 26 GLY C 106 LYS C 125 1 20 HELIX 27 27 PRO C 128 GLY C 138 1 11 HELIX 28 28 GLY C 156 ALA C 159 5 4 HELIX 29 29 THR C 177 LYS C 199 1 23 HELIX 30 30 SER C 217 ALA C 232 1 16 HELIX 31 31 ALA C 247 GLU C 250 5 4 HELIX 32 32 THR C 268 TYR C 283 1 16 HELIX 33 33 ASP C 296 GLY C 308 1 13 HELIX 34 34 ASN C 322 GLY C 333 1 12 HELIX 35 35 LYS C 341 GLY C 346 1 6 HELIX 36 36 SER C 347 ALA C 361 1 15 HELIX 37 37 ALA C 377 THR C 386 1 10 HELIX 38 38 ARG C 398 GLY C 416 1 19 HELIX 39 39 GLU C 417 ALA C 419 5 3 HELIX 40 40 ASN C 422 ILE C 427 5 6 HELIX 41 41 ARG D 57 LYS D 61 5 5 HELIX 42 42 VAL D 63 GLY D 72 1 10 HELIX 43 43 GLY D 72 ILE D 79 1 8 HELIX 44 44 ASP D 85 GLY D 98 1 14 HELIX 45 45 GLY D 106 LYS D 125 1 20 HELIX 46 46 PRO D 128 ASN D 137 1 10 HELIX 47 47 GLY D 156 ALA D 159 5 4 HELIX 48 48 THR D 177 LYS D 199 1 23 HELIX 49 49 SER D 217 ALA D 232 1 16 HELIX 50 50 ALA D 247 GLU D 250 5 4 HELIX 51 51 THR D 268 TYR D 283 1 16 HELIX 52 52 ASP D 296 GLY D 308 1 13 HELIX 53 53 ASN D 322 LYS D 332 1 11 HELIX 54 54 LYS D 341 GLY D 346 1 6 HELIX 55 55 SER D 347 GLY D 362 1 16 HELIX 56 56 ALA D 377 THR D 386 1 10 HELIX 57 57 ARG D 398 GLY D 416 1 19 HELIX 58 58 GLU D 417 ALA D 419 5 3 HELIX 59 59 ASN D 422 ILE D 427 5 6 HELIX 60 60 SER E 2 SER E 7 1 6 HELIX 61 61 ARG F 57 LYS F 61 5 5 HELIX 62 62 VAL F 63 GLY F 72 1 10 HELIX 63 63 GLY F 72 ILE F 79 1 8 HELIX 64 64 ASP F 85 GLY F 98 1 14 HELIX 65 65 GLY F 106 LYS F 125 1 20 HELIX 66 66 PRO F 128 ASN F 137 1 10 HELIX 67 67 GLY F 156 ALA F 159 5 4 HELIX 68 68 THR F 177 LYS F 199 1 23 HELIX 69 69 SER F 217 ALA F 232 1 16 HELIX 70 70 ALA F 247 GLU F 250 5 4 HELIX 71 71 THR F 268 TYR F 283 1 16 HELIX 72 72 ASP F 296 GLY F 308 1 13 HELIX 73 73 ASN F 322 LYS F 332 1 11 HELIX 74 74 LYS F 341 GLY F 346 1 6 HELIX 75 75 SER F 347 ALA F 361 1 15 HELIX 76 76 ALA F 377 THR F 386 1 10 HELIX 77 77 ARG F 398 GLY F 416 1 19 HELIX 78 78 GLU F 417 ALA F 419 5 3 HELIX 79 79 ASN F 422 ILE F 427 5 6 SHEET 1 A 3 ILE A 3 ILE A 12 0 SHEET 2 A 3 PRO A 18 LEU A 26 -1 O HIS A 25 N LYS A 5 SHEET 3 A 3 VAL A 31 ALA A 35 -1 O ALA A 34 N ALA A 22 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 N ILE A 367 O LYS A 392 SHEET 4 B 9 SER A 337 ILE A 340 1 N ILE A 340 O VAL A 366 SHEET 5 B 9 GLN A 312 GLY A 315 1 N GLY A 315 O LEU A 339 SHEET 6 B 9 ILE A 285 GLU A 289 1 N ILE A 288 O GLN A 312 SHEET 7 B 9 THR A 241 ASP A 245 1 N MET A 244 O GLU A 289 SHEET 8 B 9 GLU A 167 GLN A 171 -1 N MET A 169 O ALA A 243 SHEET 9 B 9 MET A 150 ASN A 154 -1 N MET A 150 O ILE A 170 SHEET 1 C 3 TYR A 252 LYS A 253 0 SHEET 2 C 3 LYS A 256 VAL A 258 -1 O LYS A 256 N LYS A 253 SHEET 3 C 3 ALA A 266 PHE A 267 -1 O PHE A 267 N TYR A 257 SHEET 1 D 3 ILE C 3 ILE C 12 0 SHEET 2 D 3 PRO C 18 LEU C 26 -1 O HIS C 25 N LYS C 5 SHEET 3 D 3 VAL C 31 ALA C 35 -1 O ALA C 34 N ALA C 22 SHEET 1 E 9 VAL C 147 PRO C 148 0 SHEET 2 E 9 GLY C 389 LYS C 392 1 O GLY C 389 N VAL C 147 SHEET 3 E 9 THR C 364 SER C 368 1 N ILE C 367 O LYS C 392 SHEET 4 E 9 SER C 337 ILE C 340 1 N ILE C 340 O VAL C 366 SHEET 5 E 9 GLN C 312 GLY C 315 1 N GLY C 315 O LEU C 339 SHEET 6 E 9 ILE C 285 GLU C 289 1 N ILE C 288 O GLN C 312 SHEET 7 E 9 THR C 241 ASP C 245 1 N MET C 244 O GLU C 289 SHEET 8 E 9 GLU C 167 GLN C 171 -1 N MET C 169 O ALA C 243 SHEET 9 E 9 MET C 150 ASN C 154 -1 N MET C 150 O ILE C 170 SHEET 1 F 2 TYR C 252 LYS C 253 0 SHEET 2 F 2 LYS C 256 TYR C 257 -1 O LYS C 256 N LYS C 253 SHEET 1 G 3 ILE D 3 ILE D 12 0 SHEET 2 G 3 PRO D 18 LEU D 26 -1 O HIS D 25 N LYS D 5 SHEET 3 G 3 VAL D 31 ALA D 35 -1 O ALA D 34 N ALA D 22 SHEET 1 H 9 VAL D 147 PRO D 148 0 SHEET 2 H 9 GLY D 389 LYS D 392 1 O GLY D 389 N VAL D 147 SHEET 3 H 9 THR D 364 SER D 368 1 N ILE D 367 O LYS D 392 SHEET 4 H 9 SER D 337 ILE D 340 1 N ILE D 340 O SER D 368 SHEET 5 H 9 GLN D 312 GLY D 315 1 N GLY D 315 O LEU D 339 SHEET 6 H 9 ILE D 285 GLU D 289 1 N ILE D 288 O GLN D 312 SHEET 7 H 9 THR D 241 ASP D 245 1 N LEU D 242 O VAL D 286 SHEET 8 H 9 GLU D 167 GLN D 171 -1 N MET D 169 O ALA D 243 SHEET 9 H 9 MET D 150 ASN D 154 -1 N MET D 150 O ILE D 170 SHEET 1 I 3 TYR D 252 LYS D 253 0 SHEET 2 I 3 LYS D 256 LEU D 259 -1 O LYS D 256 N LYS D 253 SHEET 3 I 3 LYS D 265 PHE D 267 -1 O PHE D 267 N TYR D 257 SHEET 1 J 3 ILE F 3 ILE F 12 0 SHEET 2 J 3 PRO F 18 LEU F 26 -1 O HIS F 25 N VAL F 4 SHEET 3 J 3 VAL F 31 ALA F 35 -1 O ALA F 34 N ALA F 22 SHEET 1 K 9 VAL F 147 PRO F 148 0 SHEET 2 K 9 GLY F 389 LYS F 392 1 O GLY F 389 N VAL F 147 SHEET 3 K 9 THR F 364 SER F 368 1 N ILE F 367 O LYS F 392 SHEET 4 K 9 SER F 337 ILE F 340 1 N ILE F 340 O VAL F 366 SHEET 5 K 9 GLN F 312 GLY F 315 1 N GLY F 315 O SER F 337 SHEET 6 K 9 ILE F 285 GLU F 289 1 N ILE F 288 O GLN F 312 SHEET 7 K 9 THR F 241 ASP F 245 1 N LEU F 242 O VAL F 286 SHEET 8 K 9 GLU F 167 GLN F 171 -1 N MET F 169 O ALA F 243 SHEET 9 K 9 MET F 150 ASN F 154 -1 N MET F 150 O ILE F 170 SHEET 1 L 3 TYR F 252 LYS F 253 0 SHEET 2 L 3 LYS F 256 LEU F 259 -1 O LYS F 256 N LYS F 253 SHEET 3 L 3 LYS F 265 PHE F 267 -1 O PHE F 267 N TYR F 257 LINK MG MG A1431 OD2 ASP A 245 LINK MG MG A1431 OE2 GLU A 289 LINK MG MG A1431 OD2 ASP A 316 LINK MG MG C1431 OD2 ASP C 245 LINK MG MG C1431 OE2 GLU C 289 LINK MG MG C1431 OD2 ASP C 316 LINK MG MG D1431 OD2 ASP D 245 LINK MG MG D1431 OE2 GLU D 289 LINK MG MG D1431 OD2 ASP D 316 LINK MG MG F1431 OD2 ASP F 245 LINK MG MG F1431 OE2 GLU F 289 LINK MG MG F1431 OD2 ASP F 316 CRYST1 77.054 124.201 96.076 90.00 90.58 90.00 P 1 21 1 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 0.012978 0.000000 0.000131 0.00000 SCALE2 0.000000 0.008051 0.000000 0.00000 SCALE3 0.000000 0.000000 0.010409 0.00000