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*** hng ***elNémo ID: 24012217345632109Job options:ID = 24012217345632109 JOBID = hng USERID = unknown PRIVAT = 0 NMODES = 5 DQMIN = -100 DQMAX = 100 DQSTEP = 20 DOGRAPHS = on DOPROJMODS = 0 DORMSD = 0 NRBL = 0 CUTOFF = 0 CAONLY = 0 Input data for this run:HEADER hng HEADER HYDROLASE 05-FEB-90 1TGL TITLE A SERINE PROTEASE TRIAD FORMS THE CATALYTIC CENTRE OF A TITLE 2 TRIACYLGLYCEROL LIPASE COMPND MOL_ID: 1; COMPND 2 MOLECULE: TRIACYL-GLYCEROL ACYLHYDROLASE; COMPND 3 CHAIN: A; COMPND 4 EC: 3.1.1.3; COMPND 5 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: RHIZOMUCOR MIEHEI; SOURCE 3 ORGANISM_COMMON: MUCOR MIEHEI; SOURCE 4 ORGANISM_TAXID: 4839 KEYWDS HYDROLASE, CARBOXYLIC ESTERASE EXPDTA X-RAY DIFFRACTION AUTHOR L.BRADY,A.M.BRZOZOWSKI,Z.S.DEREWENDA,E.J.DODSON,G.G.DODSON, AUTHOR 2 S.P.TOLLEY,J.P.TURKENBURG,L.CHRISTIANSEN,B.HUGE-JENSEN,L.NORSKOV, AUTHOR 3 L.THIM REVDAT 5 29-FEB-12 1TGL 1 JRNL VERSN REVDAT 4 24-FEB-09 1TGL 1 VERSN REVDAT 3 01-APR-03 1TGL 1 JRNL REVDAT 2 15-JAN-91 1TGL 1 SOURCE REVDAT 1 15-OCT-90 1TGL 0 JRNL AUTH L.BRADY,A.M.BRZOZOWSKI,Z.S.DEREWENDA,E.DODSON,G.DODSON, JRNL AUTH 2 S.TOLLEY,J.P.TURKENBURG,L.CHRISTIANSEN,B.HUGE-JENSEN, JRNL AUTH 3 L.NORSKOV,L.THIM,U.MENGE JRNL TITL A SERINE PROTEASE TRIAD FORMS THE CATALYTIC CENTRE OF A JRNL TITL 2 TRIACYLGLYCEROL LIPASE. JRNL REF NATURE V. 343 767 1990 JRNL REFN ISSN 0028-0836 JRNL PMID 2304552 JRNL DOI 10.1038/343767A0 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH E.BOEL,B.HUGE-JENSEN,M.CHRISTENSEN,L.THIM,N.P.FIIL REMARK 1 TITL RHIZOMUCOR MIEHEI TRIGLYCERIDE LIPASE IS SYNTHESIZED AS A REMARK 1 TITL 2 PRECURSOR REMARK 1 REF LIPIDS V. 23 701 1988 REMARK 1 REFN ISSN 0024-4201 REMARK 2 REMARK 2 RESOLUTION. 1.90 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PROLSQ REMARK 3 AUTHORS : KONNERT,HENDRICKSON REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 7.50 REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL REMARK 3 COMPLETENESS FOR RANGE (%) : NULL REMARK 3 NUMBER OF REFLECTIONS : NULL REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 CROSS-VALIDATION METHOD : NULL REMARK 3 FREE R VALUE TEST SET SELECTION : NULL REMARK 3 R VALUE (WORKING + TEST SET) : 0.138 REMARK 3 R VALUE (WORKING SET) : NULL REMARK 3 FREE R VALUE : NULL REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL REMARK 3 FREE R VALUE TEST SET COUNT : NULL REMARK 3 REMARK 3 FIT/AGREEMENT OF MODEL WITH ALL DATA. REMARK 3 R VALUE (WORKING + TEST SET, NO CUTOFF) : NULL REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : NULL REMARK 3 FREE R VALUE (NO CUTOFF) : NULL REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : NULL REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : NULL REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 286 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 0 REMARK 3 SOLVENT ATOMS : 0 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : NULL REMARK 3 B22 (A**2) : NULL REMARK 3 B33 (A**2) : NULL REMARK 3 B12 (A**2) : NULL REMARK 3 B13 (A**2) : NULL REMARK 3 B23 (A**2) : NULL REMARK 3 REMARK 3 ESTIMATED COORDINATE ERROR. REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL REMARK 3 ESD FROM SIGMAA (A) : NULL REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. REMARK 3 DISTANCE RESTRAINTS. RMS SIGMA REMARK 3 BOND LENGTH (A) : NULL ; NULL REMARK 3 ANGLE DISTANCE (A) : NULL ; NULL REMARK 3 INTRAPLANAR 1-4 DISTANCE (A) : NULL ; NULL REMARK 3 H-BOND OR METAL COORDINATION (A) : NULL ; NULL REMARK 3 REMARK 3 PLANE RESTRAINT (A) : NULL ; NULL REMARK 3 CHIRAL-CENTER RESTRAINT (A**3) : NULL ; NULL REMARK 3 REMARK 3 NON-BONDED CONTACT RESTRAINTS. REMARK 3 SINGLE TORSION (A) : NULL ; NULL REMARK 3 MULTIPLE TORSION (A) : NULL ; NULL REMARK 3 H-BOND (X...Y) (A) : NULL ; NULL REMARK 3 H-BOND (X-H...Y) (A) : NULL ; NULL REMARK 3 REMARK 3 CONFORMATIONAL TORSION ANGLE RESTRAINTS. REMARK 3 SPECIFIED (DEGREES) : NULL ; NULL REMARK 3 PLANAR (DEGREES) : NULL ; NULL REMARK 3 STAGGERED (DEGREES) : NULL ; NULL REMARK 3 TRANSVERSE (DEGREES) : NULL ; NULL REMARK 3 REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1TGL COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : NULL REMARK 200 TEMPERATURE (KELVIN) : NULL REMARK 200 PH : NULL REMARK 200 NUMBER OF CRYSTALS USED : NULL REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : NULL REMARK 200 RADIATION SOURCE : NULL REMARK 200 BEAMLINE : NULL REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : NULL REMARK 200 WAVELENGTH OR RANGE (A) : NULL REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : NULL REMARK 200 DETECTOR MANUFACTURER : NULL REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL REMARK 200 DATA SCALING SOFTWARE : NULL REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : NULL REMARK 200 RESOLUTION RANGE HIGH (A) : NULL REMARK 200 RESOLUTION RANGE LOW (A) : NULL REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : NULL REMARK 200 DATA REDUNDANCY : NULL REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : NULL REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL 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: NULL REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL REMARK 200 SOFTWARE USED: NULL REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 50.82 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.50 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: NULL REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X+1/2,-Y,Z+1/2 REMARK 290 3555 -X,Y+1/2,-Z+1/2 REMARK 290 4555 X+1/2,-Y+1/2,-Z REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 35.80000 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 27.50000 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 37.50000 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 27.50000 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 35.80000 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 37.50000 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 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 A 1 REMARK 465 ILE A 2 REMARK 465 ASN A 3 REMARK 465 GLY A 4 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 GLY A 5 N C O REMARK 470 ILE A 6 N C O CB CG1 CG2 CD1 REMARK 470 ARG A 7 N C O CB CG CD NE REMARK 470 ARG A 7 CZ NH1 NH2 REMARK 470 ALA A 8 N C O CB REMARK 470 ALA A 9 N C O CB REMARK 470 THR A 10 N C O CB OG1 CG2 REMARK 470 SER A 11 N C O CB OG REMARK 470 GLN A 12 N C O CB CG CD OE1 REMARK 470 GLN A 12 NE2 REMARK 470 GLU A 13 N C O CB CG CD OE1 REMARK 470 GLU A 13 OE2 REMARK 470 ILE A 14 N C O CB CG1 CG2 CD1 REMARK 470 ASN A 15 N C O CB CG OD1 ND2 REMARK 470 GLU A 16 N C O CB CG CD OE1 REMARK 470 GLU A 16 OE2 REMARK 470 LEU A 17 N C O CB CG CD1 CD2 REMARK 470 THR A 18 N C O CB OG1 CG2 REMARK 470 TYR A 19 N C O CB CG CD1 CD2 REMARK 470 TYR A 19 CE1 CE2 CZ OH REMARK 470 TYR A 20 N C O CB CG CD1 CD2 REMARK 470 TYR A 20 CE1 CE2 CZ OH REMARK 470 THR A 21 N C O CB OG1 CG2 REMARK 470 THR A 22 N C O CB OG1 CG2 REMARK 470 LEU A 23 N C O CB CG CD1 CD2 REMARK 470 SER A 24 N C O CB OG REMARK 470 ALA A 25 N C O CB REMARK 470 ASN A 26 N C O CB CG OD1 ND2 REMARK 470 SER A 27 N C O CB OG REMARK 470 TYR A 28 N C O CB CG CD1 CD2 REMARK 470 TYR A 28 CE1 CE2 CZ OH REMARK 470 CYS A 29 N C O CB SG REMARK 470 ARG A 30 N C O CB CG CD NE REMARK 470 ARG A 30 CZ NH1 NH2 REMARK 470 THR A 31 N C O CB OG1 CG2 REMARK 470 VAL A 32 N C O CB CG1 CG2 REMARK 470 ILE A 33 N C O CB CG1 CG2 CD1 REMARK 470 PRO A 34 N C O CB CG CD REMARK 470 GLY A 35 N C O REMARK 470 ALA A 36 N C O CB REMARK 470 THR A 37 N C O CB OG1 CG2 REMARK 470 TRP A 38 N C O CB CG CD1 CD2 REMARK 470 TRP A 38 NE1 CE2 CE3 CZ2 CZ3 CH2 REMARK 470 ASP A 39 N C O CB CG OD1 OD2 REMARK 470 CYS A 40 N C O CB SG REMARK 470 ILE A 41 N C O CB CG1 CG2 CD1 REMARK 470 HIS A 42 N C O CB CG ND1 CD2 REMARK 470 HIS A 42 CE1 NE2 REMARK 470 CYS A 43 N C O CB SG REMARK 470 ASP A 44 N C O CB CG OD1 OD2 REMARK 470 ALA A 45 N C O CB REMARK 470 THR A 46 N C O CB OG1 CG2 REMARK 470 GLU A 47 N C O CB CG CD OE1 REMARK 470 GLU A 47 OE2 REMARK 470 ASP A 48 N C O CB CG OD1 OD2 REMARK 470 LEU A 49 N C O CB CG CD1 CD2 REMARK 470 LYS A 50 N C O CB CG CD CE REMARK 470 LYS A 50 NZ REMARK 470 ILE A 51 N C O CB CG1 CG2 CD1 REMARK 470 ILE A 52 N C O CB CG1 CG2 CD1 REMARK 470 LYS A 53 N C O CB CG CD CE REMARK 470 LYS A 53 NZ REMARK 470 THR A 54 N C O CB OG1 CG2 REMARK 470 TRP A 55 N C O CB CG CD1 CD2 REMARK 470 TRP A 55 NE1 CE2 CE3 CZ2 CZ3 CH2 REMARK 470 SER A 56 N C O CB OG REMARK 470 THR A 57 N C O CB OG1 CG2 REMARK 470 LEU A 58 N C O CB CG CD1 CD2 REMARK 470 ILE A 59 N C O CB CG1 CG2 CD1 REMARK 470 TYR A 60 N C O CB CG CD1 CD2 REMARK 470 TYR A 60 CE1 CE2 CZ OH REMARK 470 ASP A 61 N C O CB CG OD1 OD2 REMARK 470 THR A 62 N C O CB OG1 CG2 REMARK 470 ASN A 63 N C O CB CG OD1 ND2 REMARK 470 ALA A 64 N C O CB REMARK 470 MET A 65 N C O CB CG SD CE REMARK 470 VAL A 66 N C O CB CG1 CG2 REMARK 470 ALA A 67 N C O CB REMARK 470 ARG A 68 N C O CB CG CD NE REMARK 470 ARG A 68 CZ NH1 NH2 REMARK 470 GLY A 69 N C O REMARK 470 ASP A 70 N C O CB CG OD1 OD2 REMARK 470 SER A 71 N C O CB OG REMARK 470 GLU A 72 N C O CB CG CD OE1 REMARK 470 GLU A 72 OE2 REMARK 470 LYS A 73 N C O CB CG CD CE REMARK 470 LYS A 73 NZ REMARK 470 THR A 74 N C O CB OG1 CG2 REMARK 470 ILE A 75 N C O CB CG1 CG2 CD1 REMARK 470 TYR A 76 N C O CB CG CD1 CD2 REMARK 470 TYR A 76 CE1 CE2 CZ OH REMARK 470 ILE A 77 N C O CB CG1 CG2 CD1 REMARK 470 VAL A 78 N C O CB CG1 CG2 REMARK 470 PHE A 79 N C O CB CG CD1 CD2 REMARK 470 PHE A 79 CE1 CE2 CZ REMARK 470 ARG A 80 N C O CB CG CD NE REMARK 470 ARG A 80 CZ NH1 NH2 REMARK 470 GLY A 81 N C O REMARK 470 SER A 82 N C O CB OG REMARK 470 SER A 83 N C O CB OG REMARK 470 SER A 84 N C O CB OG REMARK 470 ILE A 85 N C O CB CG1 CG2 CD1 REMARK 470 ARG A 86 N C O CB CG CD NE REMARK 470 ARG A 86 CZ NH1 NH2 REMARK 470 ASN A 87 N C O CB CG OD1 ND2 REMARK 470 TRP A 88 N C O CB CG CD1 CD2 REMARK 470 TRP A 88 NE1 CE2 CE3 CZ2 CZ3 CH2 REMARK 470 ILE A 89 N C O CB CG1 CG2 CD1 REMARK 470 ALA A 90 N C O CB REMARK 470 ASP A 91 N C O CB CG OD1 OD2 REMARK 470 LEU A 92 N C O CB CG CD1 CD2 REMARK 470 THR A 93 N C O CB OG1 CG2 REMARK 470 PHE A 94 N C O CB CG CD1 CD2 REMARK 470 PHE A 94 CE1 CE2 CZ REMARK 470 VAL A 95 N C O CB CG1 CG2 REMARK 470 PRO A 96 N C O CB CG CD REMARK 470 VAL A 97 N C O CB CG1 CG2 REMARK 470 SER A 98 N C O CB OG REMARK 470 TYR A 99 N C O CB CG CD1 CD2 REMARK 470 TYR A 99 CE1 CE2 CZ OH REMARK 470 PRO A 100 N C O CB CG CD REMARK 470 PRO A 101 N C O CB CG CD REMARK 470 VAL A 102 N C O CB CG1 CG2 REMARK 470 SER A 103 N C O CB OG REMARK 470 GLY A 104 N C O REMARK 470 THR A 105 N C O CB OG1 CG2 REMARK 470 LYS A 106 N C O CB CG CD CE REMARK 470 LYS A 106 NZ REMARK 470 VAL A 107 N C O CB CG1 CG2 REMARK 470 HIS A 108 N C O CB CG ND1 CD2 REMARK 470 HIS A 108 CE1 NE2 REMARK 470 LYS A 109 N C O CB CG CD CE REMARK 470 LYS A 109 NZ REMARK 470 GLY A 110 N C O REMARK 470 PHE A 111 N C O CB CG CD1 CD2 REMARK 470 PHE A 111 CE1 CE2 CZ REMARK 470 LEU A 112 N C O CB CG CD1 CD2 REMARK 470 ASP A 113 N C O CB CG OD1 OD2 REMARK 470 SER A 114 N C O CB OG REMARK 470 TYR A 115 N C O CB CG CD1 CD2 REMARK 470 TYR A 115 CE1 CE2 CZ OH REMARK 470 GLY A 116 N C O REMARK 470 GLU A 117 N C O CB CG CD OE1 REMARK 470 GLU A 117 OE2 REMARK 470 VAL A 118 N C O CB CG1 CG2 REMARK 470 GLN A 119 N C O CB CG CD OE1 REMARK 470 GLN A 119 NE2 REMARK 470 ASN A 120 N C O CB CG OD1 ND2 REMARK 470 GLU A 121 N C O CB CG CD OE1 REMARK 470 GLU A 121 OE2 REMARK 470 LEU A 122 N C O CB CG CD1 CD2 REMARK 470 VAL A 123 N C O CB CG1 CG2 REMARK 470 ALA A 124 N C O CB REMARK 470 THR A 125 N C O CB OG1 CG2 REMARK 470 VAL A 126 N C O CB CG1 CG2 REMARK 470 LEU A 127 N C O CB CG CD1 CD2 REMARK 470 ASP A 128 N C O CB CG OD1 OD2 REMARK 470 GLN A 129 N C O CB CG CD OE1 REMARK 470 GLN A 129 NE2 REMARK 470 PHE A 130 N C O CB CG CD1 CD2 REMARK 470 PHE A 130 CE1 CE2 CZ REMARK 470 LYS A 131 N C O CB CG CD CE REMARK 470 LYS A 131 NZ REMARK 470 GLN A 132 N C O CB CG CD OE1 REMARK 470 GLN A 132 NE2 REMARK 470 TYR A 133 N C O CB CG CD1 CD2 REMARK 470 TYR A 133 CE1 CE2 CZ OH REMARK 470 PRO A 134 N C O CB CG CD REMARK 470 SER A 135 N C O CB OG REMARK 470 TYR A 136 N C O CB CG CD1 CD2 REMARK 470 TYR A 136 CE1 CE2 CZ OH REMARK 470 LYS A 137 N C O CB CG CD CE REMARK 470 LYS A 137 NZ REMARK 470 VAL A 138 N C O CB CG1 CG2 REMARK 470 ALA A 139 N C O CB REMARK 470 VAL A 140 N C O CB CG1 CG2 REMARK 470 THR A 141 N C O CB OG1 CG2 REMARK 470 GLY A 142 N C O REMARK 470 HIS A 143 N C O CB CG ND1 CD2 REMARK 470 HIS A 143 CE1 NE2 REMARK 470 LEU A 145 N C O CB CG CD1 CD2 REMARK 470 GLY A 146 N C O REMARK 470 GLY A 147 N C O REMARK 470 ALA A 148 N C O CB REMARK 470 THR A 149 N C O CB OG1 CG2 REMARK 470 ALA A 150 N C O CB REMARK 470 LEU A 151 N C O CB CG CD1 CD2 REMARK 470 LEU A 152 N C O CB CG CD1 CD2 REMARK 470 CYS A 153 N C O CB SG REMARK 470 ALA A 154 N C O CB REMARK 470 LEU A 155 N C O CB CG CD1 CD2 REMARK 470 ASP A 156 N C O CB CG OD1 OD2 REMARK 470 LEU A 157 N C O CB CG CD1 CD2 REMARK 470 TYR A 158 N C O CB CG CD1 CD2 REMARK 470 TYR A 158 CE1 CE2 CZ OH REMARK 470 GLN A 159 N C O CB CG CD OE1 REMARK 470 GLN A 159 NE2 REMARK 470 ARG A 160 N C O CB CG CD NE REMARK 470 ARG A 160 CZ NH1 NH2 REMARK 470 GLU A 161 N C O CB CG CD OE1 REMARK 470 GLU A 161 OE2 REMARK 470 GLU A 162 N C O CB CG CD OE1 REMARK 470 GLU A 162 OE2 REMARK 470 GLY A 163 N C O REMARK 470 LEU A 164 N C O CB CG CD1 CD2 REMARK 470 SER A 165 N C O CB OG REMARK 470 SER A 166 N C O CB OG REMARK 470 SER A 167 N C O CB OG REMARK 470 ASN A 168 N C O CB CG OD1 ND2 REMARK 470 LEU A 169 N C O CB CG CD1 CD2 REMARK 470 PHE A 170 N C O CB CG CD1 CD2 REMARK 470 PHE A 170 CE1 CE2 CZ REMARK 470 LEU A 171 N C O CB CG CD1 CD2 REMARK 470 TYR A 172 N C O CB CG CD1 CD2 REMARK 470 TYR A 172 CE1 CE2 CZ OH REMARK 470 THR A 173 N C O CB OG1 CG2 REMARK 470 GLN A 174 N C O CB CG CD OE1 REMARK 470 GLN A 174 NE2 REMARK 470 GLY A 175 N C O REMARK 470 GLN A 176 N C O CB CG CD OE1 REMARK 470 GLN A 176 NE2 REMARK 470 PRO A 177 N C O CB CG CD REMARK 470 ARG A 178 N C O CB CG CD NE REMARK 470 ARG A 178 CZ NH1 NH2 REMARK 470 VAL A 179 N C O CB CG1 CG2 REMARK 470 GLY A 180 N C O REMARK 470 ASN A 181 N C O CB CG OD1 ND2 REMARK 470 PRO A 182 N C O CB CG CD REMARK 470 ALA A 183 N C O CB REMARK 470 PHE A 184 N C O CB CG CD1 CD2 REMARK 470 PHE A 184 CE1 CE2 CZ REMARK 470 ALA A 185 N C O CB REMARK 470 ASN A 186 N C O CB CG OD1 ND2 REMARK 470 TYR A 187 N C O CB CG CD1 CD2 REMARK 470 TYR A 187 CE1 CE2 CZ OH REMARK 470 VAL A 188 N C O CB CG1 CG2 REMARK 470 VAL A 189 N C O CB CG1 CG2 REMARK 470 SER A 190 N C O CB OG REMARK 470 THR A 191 N C O CB OG1 CG2 REMARK 470 GLY A 192 N C O REMARK 470 ILE A 193 N C O CB CG1 CG2 CD1 REMARK 470 PRO A 194 N C O CB CG CD REMARK 470 TYR A 195 N C O CB CG CD1 CD2 REMARK 470 TYR A 195 CE1 CE2 CZ OH REMARK 470 ARG A 196 N C O CB CG CD NE REMARK 470 ARG A 196 CZ NH1 NH2 REMARK 470 ARG A 197 N C O CB CG CD NE REMARK 470 ARG A 197 CZ NH1 NH2 REMARK 470 THR A 198 N C O CB OG1 CG2 REMARK 470 VAL A 199 N C O CB CG1 CG2 REMARK 470 ASN A 200 N C O CB CG OD1 ND2 REMARK 470 GLU A 201 N C O CB CG CD OE1 REMARK 470 GLU A 201 OE2 REMARK 470 ARG A 202 N C O CB CG CD NE REMARK 470 ARG A 202 CZ NH1 NH2 REMARK 470 ILE A 204 N C O CB CG1 CG2 CD1 REMARK 470 VAL A 205 N C O CB CG1 CG2 REMARK 470 PRO A 206 N C O CB CG CD REMARK 470 HIS A 207 N C O CB CG ND1 CD2 REMARK 470 HIS A 207 CE1 NE2 REMARK 470 LEU A 208 N C O CB CG CD1 CD2 REMARK 470 PRO A 209 N C O CB CG CD REMARK 470 PRO A 210 N C O CB CG CD REMARK 470 ALA A 211 N C O CB REMARK 470 ALA A 212 N C O CB REMARK 470 PHE A 213 N C O CB CG CD1 CD2 REMARK 470 PHE A 213 CE1 CE2 CZ REMARK 470 GLY A 214 N C O REMARK 470 PHE A 215 N C O CB CG CD1 CD2 REMARK 470 PHE A 215 CE1 CE2 CZ REMARK 470 LEU A 216 N C O CB CG CD1 CD2 REMARK 470 HIS A 217 N C O CB CG ND1 CD2 REMARK 470 HIS A 217 CE1 NE2 REMARK 470 ALA A 218 N C O CB REMARK 470 GLY A 219 N C O REMARK 470 SER A 220 N C O CB OG REMARK 470 GLU A 221 N C O CB CG CD OE1 REMARK 470 GLU A 221 OE2 REMARK 470 TYR A 222 N C O CB CG CD1 CD2 REMARK 470 TYR A 222 CE1 CE2 CZ OH REMARK 470 TRP A 223 N C O CB CG CD1 CD2 REMARK 470 TRP A 223 NE1 CE2 CE3 CZ2 CZ3 CH2 REMARK 470 ILE A 224 N C O CB CG1 CG2 CD1 REMARK 470 THR A 225 N C O CB OG1 CG2 REMARK 470 ASP A 226 N C O CB CG OD1 OD2 REMARK 470 ASN A 227 N C O CB CG OD1 ND2 REMARK 470 SER A 228 N C O CB OG REMARK 470 PRO A 229 N C O CB CG CD REMARK 470 GLU A 230 N C O CB CG CD OE1 REMARK 470 GLU A 230 OE2 REMARK 470 THR A 231 N C O CB OG1 CG2 REMARK 470 VAL A 232 N C O CB CG1 CG2 REMARK 470 GLN A 233 N C O CB CG CD OE1 REMARK 470 GLN A 233 NE2 REMARK 470 VAL A 234 N C O CB CG1 CG2 REMARK 470 CYS A 235 N C O CB SG REMARK 470 THR A 236 N C O CB OG1 CG2 REMARK 470 SER A 237 N C O CB OG REMARK 470 ASP A 238 N C O CB CG OD1 OD2 REMARK 470 LEU A 239 N C O CB CG CD1 CD2 REMARK 470 GLU A 240 N C O CB CG CD OE1 REMARK 470 GLU A 240 OE2 REMARK 470 THR A 241 N C O CB OG1 CG2 REMARK 470 SER A 242 N C O CB OG REMARK 470 ASP A 243 N C O CB CG OD1 OD2 REMARK 470 CYS A 244 N C O CB SG REMARK 470 SER A 245 N C O CB OG REMARK 470 ASN A 246 N C O CB CG OD1 ND2 REMARK 470 SER A 247 N C O CB OG REMARK 470 ILE A 248 N C O CB CG1 CG2 CD1 REMARK 470 VAL A 249 N C O CB CG1 CG2 REMARK 470 PRO A 250 N C O CB CG CD REMARK 470 PHE A 251 N C O CB CG CD1 CD2 REMARK 470 PHE A 251 CE1 CE2 CZ REMARK 470 THR A 252 N C O CB OG1 CG2 REMARK 470 SER A 253 N C O CB OG REMARK 470 VAL A 254 N C O CB CG1 CG2 REMARK 470 LEU A 255 N C O CB CG CD1 CD2 REMARK 470 ASP A 256 N C O CB CG OD1 OD2 REMARK 470 LEU A 258 N C O CB CG CD1 CD2 REMARK 470 SER A 259 N C O CB OG REMARK 470 TYR A 260 N C O CB CG CD1 CD2 REMARK 470 TYR A 260 CE1 CE2 CZ OH REMARK 470 PHE A 261 N C O CB CG CD1 CD2 REMARK 470 PHE A 261 CE1 CE2 CZ REMARK 470 GLY A 262 N C O REMARK 470 ILE A 263 N C O CB CG1 CG2 CD1 REMARK 470 ASN A 264 N C O CB CG OD1 ND2 REMARK 470 THR A 265 N C O CB OG1 CG2 REMARK 470 GLY A 266 N C O REMARK 470 LEU A 267 N C O CB CG CD1 CD2 REMARK 470 CYS A 268 N C O CB SG REMARK 470 SER A 269 N C O CB OG 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 SER A 144 CB SER A 144 OG 0.078 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND ANGLES REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1) REMARK 500 REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999 REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996 REMARK 500 REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3 REMARK 500 SER A 144 N - CA - CB ANGL. DEV. = -13.2 DEGREES REMARK 500 ASP A 203 CB - CG - OD2 ANGL. DEV. = 5.7 DEGREES REMARK 500 REMARK 500 REMARK: NULL REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: CAT REMARK 800 EVIDENCE_CODE: AUTHOR REMARK 800 SITE_DESCRIPTION: CATALYTIC SITE REMARK 999 REMARK 999 SEQUENCE REMARK 999 RESIDUE 156 IN THIS ENTRY IS ASP AS IDENTIFIED BY ELECTRON REMARK 999 DENSITY. IN THE PAPER CITED AS REFERENCE 2 ABOVE IT WAS REMARK 999 INCORRECTLY ASSIGNED AS GLY. DBREF 1TGL A 1 268 UNP P19515 LIP_RHIMI 95 362 SEQADV 1TGL ASN A 3 UNP P19515 ASP 97 CONFLICT SEQADV 1TGL ASN A 181 UNP P19515 ASP 275 CONFLICT SEQADV 1TGL SER A 220 UNP P19515 GLU 314 CONFLICT SEQRES 1 A 269 SER ILE ASN GLY GLY ILE ARG ALA ALA THR SER GLN GLU SEQRES 2 A 269 ILE ASN GLU LEU THR TYR TYR THR THR LEU SER ALA ASN SEQRES 3 A 269 SER TYR CYS ARG THR VAL ILE PRO GLY ALA THR TRP ASP SEQRES 4 A 269 CYS ILE HIS CYS ASP ALA THR GLU ASP LEU LYS ILE ILE SEQRES 5 A 269 LYS THR TRP SER THR LEU ILE TYR ASP THR ASN ALA MET SEQRES 6 A 269 VAL ALA ARG GLY ASP SER GLU LYS THR ILE TYR ILE VAL SEQRES 7 A 269 PHE ARG GLY SER SER SER ILE ARG ASN TRP ILE ALA ASP SEQRES 8 A 269 LEU THR PHE VAL PRO VAL SER TYR PRO PRO VAL SER GLY SEQRES 9 A 269 THR LYS VAL HIS LYS GLY PHE LEU ASP SER TYR GLY GLU SEQRES 10 A 269 VAL GLN ASN GLU LEU VAL ALA THR VAL LEU ASP GLN PHE SEQRES 11 A 269 LYS GLN TYR PRO SER TYR LYS VAL ALA VAL THR GLY HIS SEQRES 12 A 269 SER LEU GLY GLY ALA THR ALA LEU LEU CYS ALA LEU ASP SEQRES 13 A 269 LEU TYR GLN ARG GLU GLU GLY LEU SER SER SER ASN LEU SEQRES 14 A 269 PHE LEU TYR THR GLN GLY GLN PRO ARG VAL GLY ASN PRO SEQRES 15 A 269 ALA PHE ALA ASN TYR VAL VAL SER THR GLY ILE PRO TYR SEQRES 16 A 269 ARG ARG THR VAL ASN GLU ARG ASP ILE VAL PRO HIS LEU SEQRES 17 A 269 PRO PRO ALA ALA PHE GLY PHE LEU HIS ALA GLY SER GLU SEQRES 18 A 269 TYR TRP ILE THR ASP ASN SER PRO GLU THR VAL GLN VAL SEQRES 19 A 269 CYS THR SER ASP LEU GLU THR SER ASP CYS SER ASN SER SEQRES 20 A 269 ILE VAL PRO PHE THR SER VAL LEU ASP HIS LEU SER TYR SEQRES 21 A 269 PHE GLY ILE ASN THR GLY LEU CYS SER SITE 1 CAT 3 SER A 144 ASP A 203 HIS A 257 CRYST1 71.600 75.000 55.000 90.00 90.00 90.00 P 21 21 21 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 0.013970 0.000000 0.000000 0.00000 SCALE2 0.000000 0.013330 0.000000 0.00000 SCALE3 0.000000 0.000000 0.018180 0.00000 ATOM 1 CA GLY A 5 13.925 43.914 34.149 1.00 30.83 C ATOM 2 CA ILE A 6 10.897 46.114 33.628 1.00 28.05 C ATOM 3 CA ARG A 7 10.292 47.316 29.997 1.00 22.20 C ATOM 4 CA ALA A 8 7.533 48.273 27.704 1.00 25.99 C ATOM 5 CA ALA A 9 6.193 45.721 25.162 1.00 22.00 C ATOM 6 CA THR A 10 6.655 46.709 21.469 1.00 22.34 C ATOM 7 CA SER A 11 4.052 47.172 19.034 1.00 27.66 C ATOM 8 CA GLN A 12 4.779 43.808 17.426 1.00 24.82 C ATOM 9 CA GLU A 13 4.668 42.153 20.825 1.00 21.47 C ATOM 10 CA ILE A 14 1.137 43.523 21.411 1.00 21.30 C ATOM 11 CA ASN A 15 0.124 42.314 18.006 1.00 20.77 C ATOM 12 CA GLU A 16 1.139 38.781 18.621 1.00 21.37 C ATOM 13 CA LEU A 17 -0.301 38.561 22.117 1.00 15.40 C ATOM 14 CA THR A 18 -3.804 39.932 20.779 1.00 14.28 C ATOM 15 CA TYR A 19 -3.585 37.118 17.947 1.00 12.99 C ATOM 16 CA TYR A 20 -3.261 34.473 20.669 1.00 11.89 C ATOM 17 CA THR A 21 -5.864 36.125 22.857 1.00 10.93 C ATOM 18 CA THR A 22 -8.338 35.900 19.719 1.00 11.94 C ATOM 19 CA LEU A 23 -7.712 32.205 19.302 1.00 18.09 C ATOM 20 CA SER A 24 -8.388 31.804 23.138 1.00 17.35 C ATOM 21 CA ALA A 25 -11.573 33.979 22.916 1.00 16.26 C ATOM 22 CA ASN A 26 -12.851 32.121 19.757 1.00 15.10 C ATOM 23 CA SER A 27 -12.626 28.754 21.631 1.00 9.73 C ATOM 24 CA TYR A 28 -15.602 29.642 23.809 1.00 16.12 C ATOM 25 CA CYS A 29 -18.000 29.729 20.698 1.00 15.71 C ATOM 26 CA ARG A 30 -19.964 26.458 20.350 1.00 16.04 C ATOM 27 CA THR A 31 -19.571 26.519 16.523 1.00 15.36 C ATOM 28 CA VAL A 32 -15.741 26.539 16.877 1.00 18.21 C ATOM 29 CA ILE A 33 -15.639 23.714 19.693 1.00 16.33 C ATOM 30 CA PRO A 34 -17.151 21.427 19.180 1.00 20.79 C ATOM 31 CA GLY A 35 -18.705 22.728 15.897 1.00 14.69 C ATOM 32 CA ALA A 36 -15.271 22.669 14.402 1.00 18.63 C ATOM 33 CA THR A 37 -16.000 25.743 11.980 1.00 16.67 C ATOM 34 CA TRP A 38 -14.784 29.405 12.093 1.00 11.83 C ATOM 35 CA ASP A 39 -18.538 30.612 12.240 1.00 17.64 C ATOM 36 CA CYS A 40 -18.157 33.498 14.761 1.00 16.05 C ATOM 37 CA ILE A 41 -17.805 37.251 14.802 1.00 24.86 C ATOM 38 CA HIS A 42 -14.086 37.432 15.382 1.00 23.54 C ATOM 39 CA CYS A 43 -13.336 34.240 13.599 1.00 19.11 C ATOM 40 CA ASP A 44 -12.328 36.103 10.642 1.00 19.97 C ATOM 41 CA ALA A 45 -8.718 36.673 12.268 1.00 21.64 C ATOM 42 CA THR A 46 -8.073 32.786 12.308 1.00 20.30 C ATOM 43 CA GLU A 47 -10.328 31.658 9.563 1.00 23.42 C ATOM 44 CA ASP A 48 -7.492 30.479 7.395 1.00 21.91 C ATOM 45 CA LEU A 49 -6.317 27.847 9.959 1.00 19.20 C ATOM 46 CA LYS A 50 -7.271 24.314 9.094 1.00 17.02 C ATOM 47 CA ILE A 51 -9.160 22.768 12.199 1.00 22.52 C ATOM 48 CA ILE A 52 -7.667 19.221 12.556 1.00 17.17 C ATOM 49 CA LYS A 53 -9.694 18.122 15.475 1.00 19.32 C ATOM 50 CA THR A 54 -11.798 19.271 18.542 1.00 18.12 C ATOM 51 CA TRP A 55 -12.640 17.590 21.798 1.00 15.14 C ATOM 52 CA SER A 56 -15.327 18.227 24.579 1.00 18.94 C ATOM 53 CA THR A 57 -14.414 15.507 27.206 1.00 15.74 C ATOM 54 CA LEU A 58 -17.149 13.881 29.337 1.00 21.56 C ATOM 55 CA ILE A 59 -16.130 14.053 32.891 1.00 19.08 C ATOM 56 CA TYR A 60 -14.077 17.209 33.133 1.00 18.83 C ATOM 57 CA ASP A 61 -15.673 18.911 29.969 1.00 15.86 C ATOM 58 CA THR A 62 -12.115 19.813 28.694 1.00 15.43 C ATOM 59 CA ASN A 63 -12.726 21.711 25.317 1.00 9.71 C ATOM 60 CA ALA A 64 -9.721 21.988 23.133 1.00 11.25 C ATOM 61 CA MET A 65 -8.594 21.883 19.584 1.00 16.34 C ATOM 62 CA VAL A 66 -5.768 21.350 17.161 1.00 13.18 C ATOM 63 CA ALA A 67 -5.485 23.638 14.114 1.00 13.54 C ATOM 64 CA ARG A 68 -2.807 24.032 11.451 1.00 16.84 C ATOM 65 CA GLY A 69 -1.802 27.344 9.686 1.00 16.61 C ATOM 66 CA ASP A 70 0.333 26.613 6.569 1.00 20.31 C ATOM 67 CA SER A 71 1.009 30.112 5.600 1.00 24.72 C ATOM 68 CA GLU A 72 1.976 30.785 9.352 1.00 23.24 C ATOM 69 CA LYS A 73 3.808 27.457 9.480 1.00 21.36 C ATOM 70 CA THR A 74 2.487 26.772 12.963 1.00 13.67 C ATOM 71 CA ILE A 75 0.602 24.009 14.483 1.00 16.15 C ATOM 72 CA TYR A 76 -1.791 25.562 17.092 1.00 14.43 C ATOM 73 CA ILE A 77 -3.115 23.966 20.300 1.00 10.19 C ATOM 74 CA VAL A 78 -6.063 25.928 21.972 1.00 12.38 C ATOM 75 CA PHE A 79 -7.650 25.214 25.359 1.00 12.37 C ATOM 76 CA ARG A 80 -11.009 26.767 26.361 1.00 10.42 C ATOM 77 CA GLY A 81 -11.613 27.998 29.900 1.00 10.86 C ATOM 78 CA SER A 82 -14.837 27.135 31.921 1.00 15.38 C ATOM 79 CA SER A 83 -18.225 27.228 30.266 1.00 19.00 C ATOM 80 CA SER A 84 -19.596 29.140 33.335 1.00 24.94 C ATOM 81 CA ILE A 85 -16.655 31.397 34.339 1.00 22.50 C ATOM 82 CA ARG A 86 -18.180 33.358 37.187 1.00 24.85 C ATOM 83 CA ASN A 87 -19.112 30.368 39.067 1.00 25.72 C ATOM 84 CA TRP A 88 -15.853 28.702 38.176 1.00 22.70 C ATOM 85 CA ILE A 89 -14.105 31.613 39.938 1.00 20.92 C ATOM 86 CA ALA A 90 -16.516 31.741 42.829 1.00 27.86 C ATOM 87 CA ASP A 91 -15.914 27.969 43.521 1.00 31.59 C ATOM 88 CA LEU A 92 -12.226 27.430 42.630 1.00 30.95 C ATOM 89 CA THR A 93 -10.556 25.406 45.515 1.00 29.49 C ATOM 90 CA PHE A 94 -6.834 24.253 45.159 1.00 26.66 C ATOM 91 CA VAL A 95 -5.793 20.646 46.067 1.00 25.72 C ATOM 92 CA PRO A 96 -2.028 20.356 45.715 1.00 23.77 C ATOM 93 CA VAL A 97 -0.961 16.846 44.597 1.00 19.80 C ATOM 94 CA SER A 98 2.301 15.453 43.283 1.00 22.40 C ATOM 95 CA TYR A 99 3.015 16.271 39.677 1.00 15.50 C ATOM 96 CA PRO A 100 4.042 12.892 38.263 1.00 20.12 C ATOM 97 CA PRO A 101 6.798 13.694 35.778 1.00 15.94 C ATOM 98 CA VAL A 102 8.935 15.653 38.153 1.00 13.40 C ATOM 99 CA SER A 103 9.543 14.315 41.591 1.00 17.92 C ATOM 100 CA GLY A 104 9.392 16.903 44.410 1.00 22.87 C ATOM 101 CA THR A 105 6.852 19.240 42.608 1.00 17.74 C ATOM 102 CA LYS A 106 3.136 19.696 43.303 1.00 14.52 C ATOM 103 CA VAL A 107 0.258 21.078 40.945 1.00 12.04 C ATOM 104 CA HIS A 108 -3.423 21.561 41.790 1.00 13.56 C ATOM 105 CA LYS A 109 -5.113 18.289 41.029 1.00 14.96 C ATOM 106 CA GLY A 110 -8.079 19.757 39.264 1.00 11.57 C ATOM 107 CA PHE A 111 -5.834 21.104 36.342 1.00 16.15 C ATOM 108 CA LEU A 112 -4.038 17.725 36.039 1.00 14.30 C ATOM 109 CA ASP A 113 -7.456 15.891 35.901 1.00 17.53 C ATOM 110 CA SER A 114 -8.660 18.390 33.142 1.00 17.48 C ATOM 111 CA TYR A 115 -5.623 17.846 30.966 1.00 18.27 C ATOM 112 CA GLY A 116 -5.419 14.130 31.842 1.00 11.87 C ATOM 113 CA GLU A 117 -8.796 13.577 30.251 1.00 19.01 C ATOM 114 CA VAL A 118 -7.682 14.842 26.557 1.00 17.00 C ATOM 115 CA GLN A 119 -3.989 14.084 26.827 1.00 13.70 C ATOM 116 CA ASN A 120 -3.685 10.939 24.889 1.00 22.64 C ATOM 117 CA GLU A 121 -5.659 11.624 21.868 1.00 19.42 C ATOM 118 CA LEU A 122 -4.505 15.307 21.720 1.00 18.80 C ATOM 119 CA VAL A 123 -0.815 14.635 21.924 1.00 19.23 C ATOM 120 CA ALA A 124 -1.191 11.844 19.271 1.00 25.39 C ATOM 121 CA THR A 125 -2.892 14.233 16.835 1.00 21.34 C ATOM 122 CA VAL A 126 -0.204 16.850 17.514 1.00 21.42 C ATOM 123 CA LEU A 127 2.699 14.463 16.887 1.00 19.01 C ATOM 124 CA ASP A 128 1.039 13.145 13.721 1.00 20.93 C ATOM 125 CA GLN A 129 0.814 16.748 12.441 1.00 17.73 C ATOM 126 CA PHE A 130 4.342 17.588 13.531 1.00 18.14 C ATOM 127 CA LYS A 131 5.660 14.357 11.877 1.00 31.06 C ATOM 128 CA GLN A 132 3.970 15.594 8.530 1.00 26.37 C ATOM 129 CA TYR A 133 5.217 19.256 8.980 1.00 23.36 C ATOM 130 CA PRO A 134 8.529 18.944 11.029 1.00 26.37 C ATOM 131 CA SER A 135 9.497 22.381 9.955 1.00 28.18 C ATOM 132 CA TYR A 136 6.600 24.153 11.715 1.00 21.38 C ATOM 133 CA LYS A 137 6.471 25.651 15.088 1.00 17.59 C ATOM 134 CA VAL A 138 3.929 24.456 17.891 1.00 16.26 C ATOM 135 CA ALA A 139 2.055 27.260 19.645 1.00 14.77 C ATOM 136 CA VAL A 140 -0.037 26.503 22.857 1.00 17.55 C ATOM 137 CA THR A 141 -2.563 29.126 24.105 1.00 9.15 C ATOM 138 CA GLY A 142 -5.487 29.279 26.603 1.00 7.98 C ATOM 139 CA HIS A 143 -7.414 31.776 28.793 1.00 7.26 C ATOM 140 N SER A 144 -7.783 31.634 31.155 1.00 9.56 N ATOM 141 CA SER A 144 -8.375 31.319 32.465 1.00 11.28 C ATOM 142 C SER A 144 -7.953 29.865 32.770 1.00 13.66 C ATOM 143 O SER A 144 -6.807 29.461 32.783 1.00 10.69 O ATOM 144 CB SER A 144 -9.901 31.541 32.057 1.00 7.43 C ATOM 145 OG SER A 144 -10.534 31.442 33.409 1.00 10.40 O ATOM 146 CA LEU A 145 -8.722 27.454 33.208 1.00 13.41 C ATOM 147 CA GLY A 146 -7.590 26.930 29.516 1.00 8.26 C ATOM 148 CA GLY A 147 -4.248 28.697 30.431 1.00 7.91 C ATOM 149 CA ALA A 148 -3.577 26.177 33.278 1.00 12.16 C ATOM 150 CA THR A 149 -4.322 23.244 30.867 1.00 9.10 C ATOM 151 CA ALA A 150 -2.209 24.947 28.081 1.00 13.47 C ATOM 152 CA LEU A 151 0.850 25.041 30.516 1.00 13.26 C ATOM 153 CA LEU A 152 0.517 21.311 31.469 1.00 10.89 C ATOM 154 CA CYS A 153 0.092 20.401 27.725 1.00 8.80 C ATOM 155 CA ALA A 154 3.259 22.218 26.662 1.00 8.27 C ATOM 156 CA LEU A 155 5.291 20.577 29.461 1.00 12.32 C ATOM 157 CA ASP A 156 3.886 17.182 28.396 1.00 15.52 C ATOM 158 CA LEU A 157 4.961 17.838 24.826 1.00 14.03 C ATOM 159 CA TYR A 158 8.480 18.831 25.783 1.00 18.36 C ATOM 160 CA GLN A 159 8.890 15.789 28.096 1.00 19.50 C ATOM 161 CA ARG A 160 7.800 13.261 25.185 1.00 28.11 C ATOM 162 CA GLU A 161 11.214 14.518 23.681 1.00 46.20 C ATOM 163 CA GLU A 162 10.121 14.090 20.104 1.00 37.82 C ATOM 164 CA GLY A 163 11.646 16.886 18.427 1.00 24.45 C ATOM 165 CA LEU A 164 9.561 19.653 20.320 1.00 20.99 C ATOM 166 CA SER A 165 12.020 21.836 22.433 1.00 24.41 C ATOM 167 CA SER A 166 12.645 25.426 23.554 1.00 24.36 C ATOM 168 CA SER A 167 13.336 26.433 19.978 1.00 23.84 C ATOM 169 CA ASN A 168 10.006 25.512 18.289 1.00 15.37 C ATOM 170 CA LEU A 169 7.416 25.212 21.142 1.00 12.16 C ATOM 171 CA PHE A 170 5.799 28.583 22.446 1.00 16.73 C ATOM 172 CA LEU A 171 3.144 28.989 25.254 1.00 11.92 C ATOM 173 CA TYR A 172 0.836 32.034 25.533 1.00 10.41 C ATOM 174 CA THR A 173 -1.622 32.220 28.350 1.00 13.93 C ATOM 175 CA GLN A 174 -4.288 34.911 29.303 1.00 13.92 C ATOM 176 CA GLY A 175 -5.708 35.406 32.814 1.00 5.84 C ATOM 177 CA GLN A 176 -4.087 32.030 34.048 1.00 9.98 C ATOM 178 CA PRO A 177 -4.240 31.106 37.801 1.00 11.68 C ATOM 179 CA ARG A 178 -1.091 29.721 39.373 1.00 15.97 C ATOM 180 CA VAL A 179 -0.737 25.876 38.685 1.00 16.78 C ATOM 181 CA GLY A 180 2.063 24.655 41.100 1.00 14.07 C ATOM 182 CA ASN A 181 4.434 25.355 43.913 1.00 12.77 C ATOM 183 CA PRO A 182 7.893 26.965 43.725 1.00 15.64 C ATOM 184 CA ALA A 183 9.498 23.638 42.948 1.00 17.08 C ATOM 185 CA PHE A 184 7.195 23.166 39.851 1.00 17.19 C ATOM 186 CA ALA A 185 7.721 26.844 38.713 1.00 15.50 C ATOM 187 CA ASN A 186 11.528 26.310 38.631 1.00 11.79 C ATOM 188 CA TYR A 187 11.120 23.189 36.792 1.00 7.23 C ATOM 189 CA VAL A 188 9.071 25.090 34.175 1.00 6.19 C ATOM 190 CA VAL A 189 11.773 27.805 33.887 1.00 14.49 C ATOM 191 CA SER A 190 14.412 24.901 33.403 1.00 16.51 C ATOM 192 CA THR A 191 12.730 23.833 30.099 1.00 13.10 C ATOM 193 CA GLY A 192 13.584 27.194 28.612 1.00 10.50 C ATOM 194 CA ILE A 193 10.219 27.102 26.636 1.00 12.09 C ATOM 195 CA PRO A 194 9.294 30.765 25.655 1.00 15.68 C ATOM 196 CA TYR A 195 6.179 31.491 27.904 1.00 15.91 C ATOM 197 CA ARG A 196 4.263 34.817 27.673 1.00 10.99 C ATOM 198 CA ARG A 197 1.897 35.100 30.648 1.00 14.06 C ATOM 199 CA THR A 198 -0.528 38.064 29.880 1.00 11.44 C ATOM 200 CA VAL A 199 -2.572 39.660 32.839 1.00 10.88 C ATOM 201 CA ASN A 200 -5.263 42.300 32.023 1.00 13.06 C ATOM 202 CA GLU A 201 -5.007 45.020 34.682 1.00 13.30 C ATOM 203 CA ARG A 202 -6.552 44.037 37.992 1.00 15.03 C ATOM 204 N ASP A 203 -7.252 41.941 36.845 1.00 10.84 N ATOM 205 CA ASP A 203 -7.751 40.547 36.794 1.00 7.86 C ATOM 206 C ASP A 203 -7.376 39.813 38.081 1.00 8.94 C ATOM 207 O ASP A 203 -6.162 39.554 38.448 1.00 11.20 O ATOM 208 CB ASP A 203 -7.173 39.920 35.507 1.00 7.77 C ATOM 209 CG ASP A 203 -7.795 38.524 35.338 1.00 7.68 C ATOM 210 OD1 ASP A 203 -7.645 37.964 34.233 1.00 14.09 O ATOM 211 OD2 ASP A 203 -8.575 38.009 36.154 1.00 10.19 O ATOM 212 CA ILE A 204 -8.176 38.574 39.967 1.00 9.04 C ATOM 213 CA VAL A 205 -7.493 34.975 38.432 1.00 12.14 C ATOM 214 CA PRO A 206 -3.576 35.365 38.019 1.00 9.40 C ATOM 215 CA HIS A 207 -3.596 36.090 41.822 1.00 12.49 C ATOM 216 CA LEU A 208 -5.379 32.768 42.695 1.00 14.14 C ATOM 217 CA PRO A 209 -4.691 30.827 44.897 1.00 22.55 C ATOM 218 CA PRO A 210 -3.705 33.394 47.415 1.00 30.88 C ATOM 219 CA ALA A 211 -0.039 34.168 47.582 1.00 38.31 C ATOM 220 CA ALA A 212 -0.211 32.858 51.058 1.00 36.35 C ATOM 221 CA PHE A 213 -1.090 29.246 49.955 1.00 28.57 C ATOM 222 CA GLY A 214 2.356 28.557 48.504 1.00 25.81 C ATOM 223 CA PHE A 215 1.897 28.328 44.677 1.00 12.62 C ATOM 224 CA LEU A 216 4.169 30.654 42.333 1.00 17.81 C ATOM 225 CA HIS A 217 4.008 31.595 38.723 1.00 11.10 C ATOM 226 CA ALA A 218 6.733 30.925 36.106 1.00 9.70 C ATOM 227 CA GLY A 219 6.555 32.557 32.669 1.00 12.98 C ATOM 228 CA SER A 220 7.410 36.265 31.723 1.00 16.16 C ATOM 229 CA GLU A 221 4.634 38.566 32.795 1.00 14.09 C ATOM 230 CA TYR A 222 3.085 41.006 30.094 1.00 13.32 C ATOM 231 CA TRP A 223 0.684 43.244 32.247 1.00 8.64 C ATOM 232 CA ILE A 224 -1.845 45.430 30.169 1.00 15.98 C ATOM 233 CA THR A 225 -1.856 48.420 32.414 1.00 14.37 C ATOM 234 CA ASP A 226 -4.057 50.583 29.940 1.00 26.01 C ATOM 235 CA ASN A 227 -6.483 50.091 27.161 1.00 32.96 C ATOM 236 CA SER A 228 -6.443 53.186 25.430 1.00 44.20 C ATOM 237 CA PRO A 229 -3.876 53.254 23.873 1.00 31.34 C ATOM 238 CA GLU A 230 -3.048 49.913 24.810 1.00 28.54 C ATOM 239 CA THR A 231 -0.170 49.779 27.106 1.00 18.60 C ATOM 240 CA VAL A 232 1.849 46.683 28.310 1.00 17.26 C ATOM 241 CA GLN A 233 4.601 46.481 31.016 1.00 17.39 C ATOM 242 CA VAL A 234 6.867 43.472 30.759 1.00 17.72 C ATOM 243 CA CYS A 235 8.529 41.973 33.892 1.00 16.83 C ATOM 244 CA THR A 236 11.256 39.932 32.034 1.00 15.65 C ATOM 245 CA SER A 237 11.998 37.587 35.009 1.00 18.76 C ATOM 246 CA ASP A 238 10.857 34.027 34.239 1.00 21.57 C ATOM 247 CA LEU A 239 9.585 33.687 37.830 1.00 18.97 C ATOM 248 CA GLU A 240 6.914 35.681 39.511 1.00 22.87 C ATOM 249 CA THR A 241 7.858 39.279 40.664 1.00 23.75 C ATOM 250 CA SER A 242 6.286 41.988 42.658 1.00 26.35 C ATOM 251 CA ASP A 243 6.644 44.452 39.989 1.00 19.64 C ATOM 252 CA CYS A 244 3.778 43.845 37.582 1.00 18.49 C ATOM 253 CA SER A 245 0.252 42.878 38.476 1.00 13.72 C ATOM 254 CA ASN A 246 1.042 41.702 41.864 1.00 13.32 C ATOM 255 CA SER A 247 1.482 45.462 42.620 1.00 18.72 C ATOM 256 CA ILE A 248 -2.366 46.103 42.842 1.00 18.24 C ATOM 257 CA VAL A 249 -3.145 43.243 45.204 1.00 14.69 C ATOM 258 CA PRO A 250 -5.552 42.987 46.979 1.00 16.54 C ATOM 259 CA PHE A 251 -7.611 45.419 44.943 1.00 9.57 C ATOM 260 CA THR A 252 -8.590 43.093 42.126 1.00 18.23 C ATOM 261 CA SER A 253 -11.322 42.966 39.475 1.00 14.74 C ATOM 262 CA VAL A 254 -13.544 40.143 38.343 1.00 15.70 C ATOM 263 CA LEU A 255 -14.656 41.981 35.134 1.00 6.85 C ATOM 264 CA ASP A 256 -10.947 42.464 34.078 1.00 10.51 C ATOM 265 N HIS A 257 -11.161 40.013 33.999 1.00 11.49 N ATOM 266 CA HIS A 257 -10.855 38.647 33.530 1.00 10.96 C ATOM 267 C HIS A 257 -11.459 38.369 32.178 1.00 12.37 C ATOM 268 O HIS A 257 -10.980 37.709 31.219 1.00 13.62 O ATOM 269 CB HIS A 257 -11.506 37.585 34.559 1.00 11.73 C ATOM 270 CG HIS A 257 -11.004 36.217 34.238 1.00 21.65 C ATOM 271 ND1 HIS A 257 -9.618 35.987 34.048 1.00 13.23 N ATOM 272 CD2 HIS A 257 -11.599 35.019 34.057 1.00 15.49 C ATOM 273 CE1 HIS A 257 -9.426 34.639 33.859 1.00 15.72 C ATOM 274 NE2 HIS A 257 -10.588 34.058 33.902 1.00 17.92 N ATOM 275 CA LEU A 258 -13.476 38.763 30.838 1.00 12.41 C ATOM 276 CA SER A 259 -11.888 41.210 28.308 1.00 20.72 C ATOM 277 CA TYR A 260 -8.141 41.089 27.027 1.00 13.94 C ATOM 278 CA PHE A 261 -7.175 43.667 24.392 1.00 12.10 C ATOM 279 CA GLY A 262 -10.621 44.681 24.119 1.00 21.63 C ATOM 280 CA ILE A 263 -11.799 41.001 23.136 1.00 19.85 C ATOM 281 CA ASN A 264 -14.510 39.416 25.212 1.00 17.49 C ATOM 282 CA THR A 265 -12.682 36.310 26.666 1.00 13.27 C ATOM 283 CA GLY A 266 -15.268 33.921 28.238 1.00 17.28 C ATOM 284 CA LEU A 267 -18.434 34.844 26.305 1.00 28.43 C ATOM 285 CA CYS A 268 -17.658 34.513 22.650 1.00 38.86 C ATOM 286 CA SER A 269 -19.124 38.030 22.975 1.00 57.89 C TER 287 SER A 269 MASTER 598 1 0 0 0 0 1 6 286 1 0 21 END If you find results from this site helpful for your research, please cite one of our papers:
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