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HEADER HYDROLASE 23-SEP-03 1R1D
TITLE STRUCTURE OF A CARBOXYLESTERASE FROM BACILLUS
TITLE 2 STEAROTHERMOPHILUS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CARBOXYLESTERASE;
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 3.1.1.1;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BACILLUS STEAROTHERMOPHILUS;
SOURCE 3 ORGANISM_COMMON: BACTERIA;
SOURCE 4 GENE: EST;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_COMMON: BACTERIA
KEYWDS STRUCTURAL GENOMICS, MCSG, CARBOXYLESTERASE, BACILLUS
KEYWDS 2 STEAROTHERMOPHILUS
EXPDTA X-RAY DIFFRACTION
AUTHOR M.E.CUFF,M.ZHOU,F.COLLART,A.JOACHIMIAK
REVDAT 1 02-MAR-04 1R1D 0
JRNL AUTH M.E.CUFF,M.ZHOU,F.COLLART,A.JOACHIMIAK
JRNL TITL STRUCTURE OF A CARBOXYLESTERASE FROM BACILLUS
JRNL TITL 2 STEAROTHERMOPHILUS
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1
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 : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 27.28
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) (%) : 94.9
REMARK 3 NUMBER OF REFLECTIONS : 47271
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) : 0.205
REMARK 3 FREE R VALUE : 0.245
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2362
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.005
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 8
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.09
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 90.00
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 5261
REMARK 3 BIN R VALUE (WORKING SET) : 0.3080
REMARK 3 BIN FREE R VALUE : 0.2970
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.90
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 271
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.018
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3953
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 30
REMARK 3 SOLVENT ATOMS : 658
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 20.50
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 37.58
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 20.81000
REMARK 3 B22 (A**2) : -14.13000
REMARK 3 B33 (A**2) : -6.68000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.23
REMARK 3 ESD FROM SIGMAA (A) : 0.30
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.28
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.32
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 1.30
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : 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 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : CNS BULK SOLVENT MODEL USED
REMARK 3 KSOL : 0.32
REMARK 3 BSOL : 52.52
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 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1R1D COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-OCT-2003.
REMARK 100 THE RCSB ID CODE IS RCSB020319.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 02-JUL-2003
REMARK 200 TEMPERATURE (KELVIN) : 150.0
REMARK 200 PH : 7.50
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 19ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97923
REMARK 200 MONOCHROMATOR : SAGITALLY FOCUSSED SI(111)
REMARK 200 OPTICS : SBC2
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : CUSTOM-MADE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DTCOLLECT AND HKL2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 47271
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900
REMARK 200 RESOLUTION RANGE LOW (A) : 27.280
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 94.9
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: SAD
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: SOLVE AND AUTOSHARP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): NULL
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): NULL
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: AMMONIUM SULFATE, PEG 3350, HEPES,
REMARK 280 PH 7.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 294K
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 1/2-X,-Y,1/2+Z
REMARK 290 3555 -X,1/2+Y,1/2-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 33.96100
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 65.29100
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 40.84150
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 65.29100
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 33.96100
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 40.84150
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 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT
REMARK 300 WHICH CONSISTS OF 2 CHAIN(S). THE BIOLOGICAL UNIT IS
REMARK 300 UNKNOWN.
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 MSE A 0
REMARK 465 MSE A 1
REMARK 465 LYS A 2
REMARK 465 ILE A 3
REMARK 465 VAL A 4
REMARK 465 MSE B 0
REMARK 465 MSE B 1
REMARK 465 LYS B 2
REMARK 465 ILE B 3
REMARK 465 VAL B 4
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 458 O HOH 610 2.12
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 VAL B 72 CB VAL B 72 CG2 0.066
REMARK 500 ARG B 174 CG ARG B 174 CD 0.068
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 218 N - CA - C ANGL. DEV. = 8.0 DEGREES
REMARK 500 GLN B 228 N - CA - C ANGL. DEV. = 9.4 DEGREES
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 433 DISTANCE = 5.26 ANGSTROMS
REMARK 525 HOH 542 DISTANCE = 5.05 ANGSTROMS
REMARK 525 HOH 551 DISTANCE = 5.24 ANGSTROMS
REMARK 525 HOH 591 DISTANCE = 5.48 ANGSTROMS
DBREF 1R1D A 0 246 SWS Q06174 EST_BACST 1 247
DBREF 1R1D B 0 246 SWS Q06174 EST_BACST 1 247
SEQADV 1R1D GLN A 77 SWS Q06174 GLU 78 CONFLICT
SEQADV 1R1D ARG A 154 SWS Q06174 LYS 155 CONFLICT
SEQADV 1R1D ALA A 175 SWS Q06174 ASP 176 CONFLICT
SEQADV 1R1D VAL A 180 SWS Q06174 ILE 181 CONFLICT
SEQADV 1R1D GLN B 77 SWS Q06174 GLU 78 CONFLICT
SEQADV 1R1D ARG B 154 SWS Q06174 LYS 155 CONFLICT
SEQADV 1R1D ALA B 175 SWS Q06174 ASP 176 CONFLICT
SEQADV 1R1D VAL B 180 SWS Q06174 ILE 181 CONFLICT
SEQRES 1 A 247 MSE MSE LYS ILE VAL PRO PRO LYS PRO PHE PHE PHE GLU
SEQRES 2 A 247 ALA GLY GLU ARG ALA VAL LEU LEU LEU HIS GLY PHE THR
SEQRES 3 A 247 GLY ASN SER ALA ASP VAL ARG MSE LEU GLY ARG PHE LEU
SEQRES 4 A 247 GLU SER LYS GLY TYR THR CYS HIS ALA PRO ILE TYR LYS
SEQRES 5 A 247 GLY HIS GLY VAL PRO PRO GLU GLU LEU VAL HIS THR GLY
SEQRES 6 A 247 PRO ASP ASP TRP TRP GLN ASP VAL MSE ASN GLY TYR GLN
SEQRES 7 A 247 PHE LEU LYS ASN LYS GLY TYR GLU LYS ILE ALA VAL ALA
SEQRES 8 A 247 GLY LEU SER LEU GLY GLY VAL PHE SER LEU LYS LEU GLY
SEQRES 9 A 247 TYR THR VAL PRO ILE GLU GLY ILE VAL THR MSE CYS ALA
SEQRES 10 A 247 PRO MSE TYR ILE LYS SER GLU GLU THR MSE TYR GLU GLY
SEQRES 11 A 247 VAL LEU GLU TYR ALA ARG GLU TYR LYS LYS ARG GLU GLY
SEQRES 12 A 247 LYS SER GLU GLU GLN ILE GLU GLN GLU MSE GLU ARG PHE
SEQRES 13 A 247 LYS GLN THR PRO MSE LYS THR LEU LYS ALA LEU GLN GLU
SEQRES 14 A 247 LEU ILE ALA ASP VAL ARG ALA HIS LEU ASP LEU VAL TYR
SEQRES 15 A 247 ALA PRO THR PHE VAL VAL GLN ALA ARG HIS ASP GLU MSE
SEQRES 16 A 247 ILE ASN PRO ASP SER ALA ASN ILE ILE TYR ASN GLU ILE
SEQRES 17 A 247 GLU SER PRO VAL LYS GLN ILE LYS TRP TYR GLU GLN SER
SEQRES 18 A 247 GLY HIS VAL ILE THR LEU ASP GLN GLU LYS ASP GLN LEU
SEQRES 19 A 247 HIS GLU ASP ILE TYR ALA PHE LEU GLU SER LEU ASP TRP
SEQRES 1 B 247 MSE MSE LYS ILE VAL PRO PRO LYS PRO PHE PHE PHE GLU
SEQRES 2 B 247 ALA GLY GLU ARG ALA VAL LEU LEU LEU HIS GLY PHE THR
SEQRES 3 B 247 GLY ASN SER ALA ASP VAL ARG MSE LEU GLY ARG PHE LEU
SEQRES 4 B 247 GLU SER LYS GLY TYR THR CYS HIS ALA PRO ILE TYR LYS
SEQRES 5 B 247 GLY HIS GLY VAL PRO PRO GLU GLU LEU VAL HIS THR GLY
SEQRES 6 B 247 PRO ASP ASP TRP TRP GLN ASP VAL MSE ASN GLY TYR GLN
SEQRES 7 B 247 PHE LEU LYS ASN LYS GLY TYR GLU LYS ILE ALA VAL ALA
SEQRES 8 B 247 GLY LEU SER LEU GLY GLY VAL PHE SER LEU LYS LEU GLY
SEQRES 9 B 247 TYR THR VAL PRO ILE GLU GLY ILE VAL THR MSE CYS ALA
SEQRES 10 B 247 PRO MSE TYR ILE LYS SER GLU GLU THR MSE TYR GLU GLY
SEQRES 11 B 247 VAL LEU GLU TYR ALA ARG GLU TYR LYS LYS ARG GLU GLY
SEQRES 12 B 247 LYS SER GLU GLU GLN ILE GLU GLN GLU MSE GLU ARG PHE
SEQRES 13 B 247 LYS GLN THR PRO MSE LYS THR LEU LYS ALA LEU GLN GLU
SEQRES 14 B 247 LEU ILE ALA ASP VAL ARG ALA HIS LEU ASP LEU VAL TYR
SEQRES 15 B 247 ALA PRO THR PHE VAL VAL GLN ALA ARG HIS ASP GLU MSE
SEQRES 16 B 247 ILE ASN PRO ASP SER ALA ASN ILE ILE TYR ASN GLU ILE
SEQRES 17 B 247 GLU SER PRO VAL LYS GLN ILE LYS TRP TYR GLU GLN SER
SEQRES 18 B 247 GLY HIS VAL ILE THR LEU ASP GLN GLU LYS ASP GLN LEU
SEQRES 19 B 247 HIS GLU ASP ILE TYR ALA PHE LEU GLU SER LEU ASP TRP
MODRES 1R1D MSE A 33 MET SELENOMETHIONINE
MODRES 1R1D MSE A 73 MET SELENOMETHIONINE
MODRES 1R1D MSE A 114 MET SELENOMETHIONINE
MODRES 1R1D MSE A 118 MET SELENOMETHIONINE
MODRES 1R1D MSE A 126 MET SELENOMETHIONINE
MODRES 1R1D MSE A 152 MET SELENOMETHIONINE
MODRES 1R1D MSE A 160 MET SELENOMETHIONINE
MODRES 1R1D MSE A 194 MET SELENOMETHIONINE
MODRES 1R1D MSE B 33 MET SELENOMETHIONINE
MODRES 1R1D MSE B 73 MET SELENOMETHIONINE
MODRES 1R1D MSE B 114 MET SELENOMETHIONINE
MODRES 1R1D MSE B 118 MET SELENOMETHIONINE
MODRES 1R1D MSE B 126 MET SELENOMETHIONINE
MODRES 1R1D MSE B 152 MET SELENOMETHIONINE
MODRES 1R1D MSE B 160 MET SELENOMETHIONINE
MODRES 1R1D MSE B 194 MET SELENOMETHIONINE
HET MSE A 33 8
HET MSE A 73 8
HET MSE A 114 16
HET MSE A 118 8
HET MSE A 126 8
HET MSE A 152 8
HET MSE A 160 8
HET MSE A 194 16
HET MSE B 33 16
HET MSE B 73 8
HET MSE B 114 16
HET MSE B 118 8
HET MSE B 126 8
HET MSE B 152 8
HET MSE B 160 8
HET MSE B 194 16
HET EPE 701 15
HET EPE 702 15
HETNAM MSE SELENOMETHIONINE
HETNAM EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID
HETSYN EPE HEPES
FORMUL 1 MSE 16(C5 H11 N1 O2 SE1)
FORMUL 3 EPE 2(C8 H18 N2 O4 S1)
FORMUL 5 HOH *658(H2 O1)
HELIX 1 1 ASN A 27 ASP A 30 5 4
HELIX 2 2 VAL A 31 LYS A 41 1 11
HELIX 3 3 PRO A 56 LEU A 60 5 5
HELIX 4 4 GLY A 64 LYS A 82 1 19
HELIX 5 5 SER A 93 TYR A 104 1 12
HELIX 6 6 SER A 122 GLU A 141 1 20
HELIX 7 7 SER A 144 GLN A 157 1 14
HELIX 8 8 THR A 162 HIS A 176 1 15
HELIX 9 9 LEU A 177 VAL A 180 5 4
HELIX 10 10 ASP A 198 ILE A 207 1 10
HELIX 11 11 VAL A 223 ASP A 227 5 5
HELIX 12 12 GLU A 229 SER A 243 1 15
HELIX 13 13 SER B 28 LYS B 41 1 14
HELIX 14 14 PRO B 56 VAL B 61 1 6
HELIX 15 15 GLY B 64 LYS B 82 1 19
HELIX 16 16 SER B 93 TYR B 104 1 12
HELIX 17 17 SER B 122 GLU B 141 1 20
HELIX 18 18 SER B 144 LYS B 156 1 13
HELIX 19 19 THR B 162 HIS B 176 1 15
HELIX 20 20 LEU B 177 VAL B 180 5 4
HELIX 21 21 ASP B 198 ILE B 207 1 10
HELIX 22 22 VAL B 223 ASP B 227 5 5
HELIX 23 23 GLU B 229 SER B 243 1 15
SHEET 1 A 7 PHE A 9 PHE A 11 0
SHEET 2 A 7 THR A 44 ALA A 47 -1 O ALA A 47 N PHE A 9
SHEET 3 A 7 ALA A 17 LEU A 21 1 N VAL A 18 O THR A 44
SHEET 4 A 7 ILE A 87 LEU A 92 1 O ALA A 88 N ALA A 17
SHEET 5 A 7 ILE A 111 MSE A 114 1 O VAL A 112 N VAL A 89
SHEET 6 A 7 THR A 184 ALA A 189 1 O VAL A 187 N THR A 113
SHEET 7 A 7 LYS A 212 TYR A 217 1 O GLN A 213 N VAL A 186
SHEET 1 B 7 PHE B 9 PHE B 11 0
SHEET 2 B 7 THR B 44 ALA B 47 -1 O CYS B 45 N PHE B 11
SHEET 3 B 7 ALA B 17 LEU B 21 1 N VAL B 18 O THR B 44
SHEET 4 B 7 ILE B 87 LEU B 92 1 O ALA B 88 N LEU B 19
SHEET 5 B 7 ILE B 111 MSE B 114 1 O MSE B 114 N GLY B 91
SHEET 6 B 7 THR B 184 ALA B 189 1 O VAL B 187 N THR B 113
SHEET 7 B 7 LYS B 212 TYR B 217 1 O GLN B 213 N VAL B 186
CRYST1 67.922 81.683 130.582 90.00 90.00 90.00 P 21 21 21 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 0.014723 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012242 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007658 0.00000
TER 1973 TRP A 246
TER 3955 TRP B 246
MASTER 266 0 18 23 14 0 0 6 4641 2 198 38
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