| 2B61-pdb | HEADER TRANSFERASE 29-SEP-05 2B61
TITLE CRYSTAL STRUCTURE OF HOMOSERINE TRANSACETYLASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HOMOSERINE O-ACETYLTRANSFERASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: HOMOSERINE O-TRANS-ACETYLASE, HOMOSERINE
COMPND 5 TRANSACETYLASE, HTA;
COMPND 6 EC: 2.3.1.31;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HAEMOPHILUS INFLUENZAE;
SOURCE 3 ORGANISM_COMMON: BACTERIA;
SOURCE 4 GENE: METX, MET2;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_COMMON: BACTERIA;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: B834;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET28+HOM2
KEYWDS ACYL-ENZYME, ASPARTATE PATHWAY, COENZYME A, STRUCTURE-
KEYWDS 2 FUNCTION STUDIES, ALPHA-BETA HYDROLASE FOLD
EXPDTA X-RAY DIFFRACTION
AUTHOR I.A.MIRZA,I.NAZI,M.KORCZYNSKA,G.D.WRIGHT,A.M.BERGHUIS
REVDAT 1 15-NOV-05 2B61 0
JRNL AUTH I.A.MIRZA,I.NAZI,M.KORCZYNSKA,G.D.WRIGHT,
JRNL AUTH 2 A.M.BERGHUIS
JRNL TITL CRYSTAL STRUCTURE OF HOMOSERINE TRANSACETYLASE
JRNL TITL 2 FROM HAEMOPHILUS INFLUENZAE REVEALS A NEW FAMILY
JRNL TITL 3 OF ALPHA/BETA-HYDROLASES.
JRNL REF BIOCHEMISTRY 2005
JRNL REFN ASTM BICHAW US ISSN 0006-2960
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 1.65 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) : 1.65
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.8
REMARK 3 NUMBER OF REFLECTIONS : 57586
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) : 0.164
REMARK 3 R VALUE (WORKING SET) : 0.163
REMARK 3 FREE R VALUE : 0.187
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 3071
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH : 1.65
REMARK 3 BIN RESOLUTION RANGE LOW : 1.69
REMARK 3 REFLECTION IN BIN (WORKING SET) : 4195
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.51
REMARK 3 BIN R VALUE (WORKING SET) : 0.1980
REMARK 3 BIN FREE R VALUE SET COUNT : 243
REMARK 3 BIN FREE R VALUE : 0.2240
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 ALL ATOMS : 3272
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 20.71
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.38000
REMARK 3 B22 (A**2) : 0.38000
REMARK 3 B33 (A**2) : -0.58000
REMARK 3 B12 (A**2) : 0.19000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.075
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.075
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.044
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.243
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.968
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.960
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2921 ; 0.010 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3965 ; 1.155 ; 1.949
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 364 ; 5.482 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 145 ;37.289 ;24.621
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 468 ;12.244 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 12 ; 6.180 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 417 ; 0.084 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2293 ; 0.005 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1387 ; 0.191 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 2053 ; 0.311 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 327 ; 0.113 ; 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): 54 ; 0.147 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 29 ; 0.141 ; 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): 1837 ; 0.841 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2866 ; 1.247 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1251 ; 2.038 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1099 ; 2.926 ; 4.500
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : 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 : 1.40
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 2B61 COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 10-OCT-2005.
REMARK 100 THE RCSB ID CODE IS RCSB034718.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 27-AUG-2005
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 7.50
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X8C
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97880
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : CBASS
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 57586
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.650
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.8
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) : 1.65
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.5
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: SOLVE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 56.20
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.90
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG8000, HEPES, PH 7.5, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 323K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,1/3+Z
REMARK 290 3555 -X+Y,-X,2/3+Z
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,2/3-Z
REMARK 290 6555 -X,-X+Y,1/3-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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 40.08767
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 80.17533
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 80.17533
REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 40.08767
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 1 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
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 BIOMT1 2 -0.500000 -0.866025 0.000000 0.00000
REMARK 350 BIOMT2 2 -0.866025 0.500000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 40.08767
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH 386 LIES ON A SPECIAL POSITION.
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 GLY A -18
REMARK 465 SER A -17
REMARK 465 SER A -16
REMARK 465 HIS A -15
REMARK 465 HIS A -14
REMARK 465 HIS A -13
REMARK 465 HIS A -12
REMARK 465 HIS A -11
REMARK 465 HIS A -10
REMARK 465 SER A -9
REMARK 465 SER A -8
REMARK 465 GLY A -7
REMARK 465 LEU A -6
REMARK 465 VAL A -5
REMARK 465 PRO A -4
REMARK 465 ARG A -3
REMARK 465 GLY A -2
REMARK 465 SER A -1
REMARK 465 HIS A 0
REMARK 465 MET A 1
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 188 O HOH 440 1.97
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 LEU A 273 CA - CB - CG ANGL. DEV. = 7.2 DEGREES
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THE SEQUENCE IS OBTAINED FROM WILD TYPE H.INFLUENZAE 49824
REMARK 999 AND THE CONFLICTS ARE DUE TO DIFFERENT STRAIN.
DBREF 2B61 A 1 358 GB 53732708 ZP_00154944 1 358
SEQADV 2B61 GLY A -18 GB 53732708 CLONING ARTIFACT
SEQADV 2B61 SER A -17 GB 53732708 CLONING ARTIFACT
SEQADV 2B61 SER A -16 GB 53732708 CLONING ARTIFACT
SEQADV 2B61 HIS A -15 GB 53732708 HIS TAG
SEQADV 2B61 HIS A -14 GB 53732708 HIS TAG
SEQADV 2B61 HIS A -13 GB 53732708 HIS TAG
SEQADV 2B61 HIS A -12 GB 53732708 HIS TAG
SEQADV 2B61 HIS A -11 GB 53732708 HIS TAG
SEQADV 2B61 HIS A -10 GB 53732708 HIS TAG
SEQADV 2B61 SER A -9 GB 53732708 CLONING ARTIFACT
SEQADV 2B61 SER A -8 GB 53732708 CLONING ARTIFACT
SEQADV 2B61 GLY A -7 GB 53732708 CLONING ARTIFACT
SEQADV 2B61 LEU A -6 GB 53732708 CLONING ARTIFACT
SEQADV 2B61 VAL A -5 GB 53732708 CLONING ARTIFACT
SEQADV 2B61 PRO A -4 GB 53732708 CLONING ARTIFACT
SEQADV 2B61 ARG A -3 GB 53732708 CLONING ARTIFACT
SEQADV 2B61 GLY A -2 GB 53732708 CLONING ARTIFACT
SEQADV 2B61 SER A -1 GB 53732708 CLONING ARTIFACT
SEQADV 2B61 HIS A 0 GB 53732708 CLONING ARTIFACT
SEQADV 2B61 MSE A 17 GB 53732708 MET 17 MODIFIED RESIDUE
SEQADV 2B61 MSE A 69 GB 53732708 MET 69 MODIFIED RESIDUE
SEQADV 2B61 GLU A 129 GB 53732708 ASP 129 SEE REMARK 999
SEQADV 2B61 ILE A 133 GB 53732708 VAL 133 SEE REMARK 999
SEQADV 2B61 MSE A 147 GB 53732708 MET 147 MODIFIED RESIDUE
SEQADV 2B61 MSE A 160 GB 53732708 MET 160 MODIFIED RESIDUE
SEQADV 2B61 MSE A 183 GB 53732708 MET 183 MODIFIED RESIDUE
SEQADV 2B61 MSE A 213 GB 53732708 MET 213 MODIFIED RESIDUE
SEQADV 2B61 MSE A 216 GB 53732708 MET 216 MODIFIED RESIDUE
SEQADV 2B61 MSE A 275 GB 53732708 MET 275 MODIFIED RESIDUE
SEQADV 2B61 GLU A 283 GB 53732708 ASP 283 SEE REMARK 999
SEQRES 1 A 377 GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY LEU
SEQRES 2 A 377 VAL PRO ARG GLY SER HIS MET SER VAL GLN ASN VAL VAL
SEQRES 3 A 377 LEU PHE ASP THR GLN PRO LEU THR LEU MSE LEU GLY GLY
SEQRES 4 A 377 LYS LEU SER TYR ILE ASN VAL ALA TYR GLN THR TYR GLY
SEQRES 5 A 377 THR LEU ASN ASP GLU LYS ASN ASN ALA VAL LEU ILE CYS
SEQRES 6 A 377 HIS ALA LEU THR GLY ASP ALA GLU PRO TYR PHE ASP ASP
SEQRES 7 A 377 GLY ARG ASP GLY TRP TRP GLN ASN PHE MSE GLY ALA GLY
SEQRES 8 A 377 LEU ALA LEU ASP THR ASP ARG TYR PHE PHE ILE SER SER
SEQRES 9 A 377 ASN VAL LEU GLY GLY CYS LYS GLY THR THR GLY PRO SER
SEQRES 10 A 377 SER ILE ASN PRO GLN THR GLY LYS PRO TYR GLY SER GLN
SEQRES 11 A 377 PHE PRO ASN ILE VAL VAL GLN ASP ILE VAL LYS VAL GLN
SEQRES 12 A 377 LYS ALA LEU LEU GLU HIS LEU GLY ILE SER HIS LEU LYS
SEQRES 13 A 377 ALA ILE ILE GLY GLY SER PHE GLY GLY MSE GLN ALA ASN
SEQRES 14 A 377 GLN TRP ALA ILE ASP TYR PRO ASP PHE MSE ASP ASN ILE
SEQRES 15 A 377 VAL ASN LEU CYS SER SER ILE TYR PHE SER ALA GLU ALA
SEQRES 16 A 377 ILE GLY PHE ASN HIS VAL MSE ARG GLN ALA VAL ILE ASN
SEQRES 17 A 377 ASP PRO ASN PHE ASN GLY GLY ASP TYR TYR GLU GLY THR
SEQRES 18 A 377 PRO PRO ASP GLN GLY LEU SER ILE ALA ARG MSE LEU GLY
SEQRES 19 A 377 MSE LEU THR TYR ARG THR ASP LEU GLN LEU ALA LYS ALA
SEQRES 20 A 377 PHE GLY ARG ALA THR LYS SER ASP GLY SER PHE TRP GLY
SEQRES 21 A 377 ASP TYR PHE GLN VAL GLU SER TYR LEU SER TYR GLN GLY
SEQRES 22 A 377 LYS LYS PHE LEU GLU ARG PHE ASP ALA ASN SER TYR LEU
SEQRES 23 A 377 HIS LEU LEU ARG ALA LEU ASP MSE TYR ASP PRO SER LEU
SEQRES 24 A 377 GLY TYR GLU ASN VAL LYS GLU ALA LEU SER ARG ILE LYS
SEQRES 25 A 377 ALA ARG TYR THR LEU VAL SER VAL THR THR ASP GLN LEU
SEQRES 26 A 377 PHE LYS PRO ILE ASP LEU TYR LYS SER LYS GLN LEU LEU
SEQRES 27 A 377 GLU GLN SER GLY VAL ASP LEU HIS PHE TYR GLU PHE PRO
SEQRES 28 A 377 SER ASP TYR GLY HIS ASP ALA PHE LEU VAL ASP TYR ASP
SEQRES 29 A 377 GLN PHE GLU LYS ARG ILE ARG ASP GLY LEU ALA GLY ASN
MODRES 2B61 MSE A 17 MET SELENOMETHIONINE
MODRES 2B61 MSE A 69 MET SELENOMETHIONINE
MODRES 2B61 MSE A 147 MET SELENOMETHIONINE
MODRES 2B61 MSE A 160 MET SELENOMETHIONINE
MODRES 2B61 MSE A 183 MET SELENOMETHIONINE
MODRES 2B61 MSE A 213 MET SELENOMETHIONINE
MODRES 2B61 MSE A 216 MET SELENOMETHIONINE
MODRES 2B61 MSE A 275 MET SELENOMETHIONINE
HET MSE A 17 8
HET MSE A 69 8
HET MSE A 147 8
HET MSE A 160 8
HET MSE A 183 8
HET MSE A 213 8
HET MSE A 216 8
HET MSE A 275 8
HETNAM MSE SELENOMETHIONINE
FORMUL 1 MSE 8(C5 H11 N1 O2 SE1)
FORMUL 2 HOH *425(H2 O1)
HELIX 1 1 TRP A 65 ASN A 67 5 3
HELIX 2 2 TYR A 108 PHE A 112 5 5
HELIX 3 3 VAL A 116 LEU A 131 1 16
HELIX 4 4 SER A 143 TYR A 156 1 14
HELIX 5 5 SER A 173 ASN A 189 1 17
HELIX 6 6 PHE A 193 ASP A 197 5 5
HELIX 7 7 PRO A 204 ARG A 220 1 17
HELIX 8 8 THR A 221 PHE A 229 1 9
HELIX 9 9 PHE A 244 GLU A 259 1 16
HELIX 10 10 ASP A 262 TYR A 276 1 15
HELIX 11 11 ASN A 284 SER A 290 1 7
HELIX 12 12 LYS A 308 SER A 322 1 15
HELIX 13 13 TYR A 335 HIS A 337 5 3
HELIX 14 14 ASP A 338 ASP A 343 1 6
HELIX 15 15 ASP A 343 GLY A 357 1 15
SHEET 1 A 8 GLN A 4 LEU A 8 0
SHEET 2 A 8 ILE A 25 TYR A 32 -1 O ILE A 25 N LEU A 8
SHEET 3 A 8 PHE A 81 SER A 85 -1 O SER A 84 N GLN A 30
SHEET 4 A 8 ALA A 42 CYS A 46 1 N ILE A 45 O ILE A 83
SHEET 5 A 8 LEU A 136 GLY A 142 1 O ILE A 140 N LEU A 44
SHEET 6 A 8 MSE A 160 LEU A 166 1 O VAL A 164 N ILE A 139
SHEET 7 A 8 ARG A 295 VAL A 301 1 O THR A 297 N ILE A 163
SHEET 8 A 8 ASP A 325 PHE A 331 1 O TYR A 329 N SER A 300
SHEET 1 B 2 LEU A 14 THR A 15 0
SHEET 2 B 2 LYS A 21 LEU A 22 -1 O LEU A 22 N LEU A 14
SHEET 1 C 2 MSE A 69 GLY A 70 0
SHEET 2 C 2 LEU A 75 ASP A 76 1 O LEU A 75 N GLY A 70
CRYST1 85.264 85.264 120.263 90.00 90.00 120.00 P 31 2 1 6
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 0.011730 0.006770 0.000000 0.00000
SCALE2 0.000000 0.013540 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008310 0.00000
TER 2848 ASN A 358
MASTER 298 0 8 15 12 0 0 6 3272 1 64 29
END
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