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HEADER TRANSFERASE 26-JUN-09 3I1I
TITLE X-RAY CRYSTAL STRUCTURE OF HOMOSERINE O-ACETYLTRANSFERASE
TITLE 2 FROM BACILLUS ANTHRACIS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HOMOSERINE O-ACETYLTRANSFERASE;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BACILLUS ANTHRACIS STR. 'AMES
SOURCE 3 ANCESTOR';
SOURCE 4 ORGANISM_COMMON: ANTHRAX BACTERIUM;
SOURCE 5 ORGANISM_TAXID: 261594;
SOURCE 6 STRAIN: AMES ANCESTOR, A2084;
SOURCE 7 GENE: BAS4629, BA_4983, GBAA4983, GBAA_4983;
SOURCE 8 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 9 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 10 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 11 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 12 EXPRESSION_SYSTEM_PLASMID: PMCSG7
KEYWDS STRUCTURAL GENOMICS, IDP01610, HOMOSERINE, O-
KEYWDS 2 ACETYLTRANSFERASE, BACILLUS ANTHRACIS, TRANSFERASE, CENTER
KEYWDS 3 FOR STRUCTURAL GENOMICS OF INFECTIOUS DISEASES, CSGID
EXPDTA X-RAY DIFFRACTION
AUTHOR J.OSIPIUK,M.ZHOU,S.GRIMSHAW,W.F.ANDERSON,A.JOACHIMIAK
REVDAT 1 07-JUL-09 3I1I 0
JRNL AUTH J.OSIPIUK,M.ZHOU,S.GRIMSHAW,W.F.ANDERSON,
JRNL AUTH 2 A.JOACHIMIAK
JRNL TITL X-RAY CRYSTAL STRUCTURE OF HOMOSERINE
JRNL TITL 2 O-ACETYLTRANSFERASE FROM BACILLUS ANTHRACIS.
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 2.44 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0054
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) : 2.44
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 47.30
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 3 NUMBER OF REFLECTIONS : 50039
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) : 0.163
REMARK 3 R VALUE (WORKING SET) : 0.161
REMARK 3 FREE R VALUE : 0.197
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2539
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.44
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.50
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3385
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 97.72
REMARK 3 BIN R VALUE (WORKING SET) : 0.2190
REMARK 3 BIN FREE R VALUE SET COUNT : 172
REMARK 3 BIN FREE R VALUE : 0.2740
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6060
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 14
REMARK 3 SOLVENT ATOMS : 353
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 49.40
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 28.71
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.25000
REMARK 3 B22 (A**2) : 1.25000
REMARK 3 B33 (A**2) : -1.87000
REMARK 3 B12 (A**2) : 0.62000
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): 0.218
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.180
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.106
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 10.128
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.960
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.943
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 6237 ; 0.017 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 4214 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 8461 ; 1.487 ; 1.947
REMARK 3 BOND ANGLES OTHERS (DEGREES): 10318 ; 0.926 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 775 ; 5.856 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 301 ;34.899 ;24.718
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1105 ;15.980 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 27 ;20.388 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 909 ; 0.089 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 6937 ; 0.006 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 1244 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
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): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
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): 3760 ; 0.741 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1518 ; 0.166 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 6104 ; 1.456 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2477 ; 2.683 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2341 ; 4.098 ; 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 : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 2
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A -2 A 374
REMARK 3 ORIGIN FOR THE GROUP (A): 1.2295 104.3469 19.0727
REMARK 3 T TENSOR
REMARK 3 T11: 0.0803 T22: 0.0129
REMARK 3 T33: 0.0246 T12: 0.0089
REMARK 3 T13: 0.0012 T23: 0.0124
REMARK 3 L TENSOR
REMARK 3 L11: 0.0958 L22: 0.1842
REMARK 3 L33: 1.1417 L12: -0.0452
REMARK 3 L13: -0.3136 L23: 0.0688
REMARK 3 S TENSOR
REMARK 3 S11: -0.0248 S12: 0.0013 S13: -0.0126
REMARK 3 S21: 0.0162 S22: 0.0074 S23: -0.0228
REMARK 3 S31: 0.0788 S32: -0.0377 S33: 0.0174
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B -2 B 374
REMARK 3 ORIGIN FOR THE GROUP (A): -15.1686 92.3205 62.3995
REMARK 3 T TENSOR
REMARK 3 T11: 0.0239 T22: 0.0737
REMARK 3 T33: 0.0332 T12: 0.0093
REMARK 3 T13: 0.0115 T23: 0.0241
REMARK 3 L TENSOR
REMARK 3 L11: 0.2168 L22: 0.3380
REMARK 3 L33: 0.8899 L12: 0.2051
REMARK 3 L13: -0.0591 L23: 0.0678
REMARK 3 S TENSOR
REMARK 3 S11: -0.0240 S12: 0.0716 S13: 0.0339
REMARK 3 S21: -0.0480 S22: 0.0503 S23: 0.0578
REMARK 3 S31: -0.0508 S32: -0.2223 S33: -0.0264
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: 1. HYDROGENS HAVE BEEN ADDED IN THE
REMARK 3 RIDING POSITIONS. 2. U VALUES: RESIDUAL ONLY.
REMARK 4
REMARK 4 3I1I COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 29-JUN-09.
REMARK 100 THE RCSB ID CODE IS RCSB053845.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 30-MAR-09
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 19-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9792
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-3000
REMARK 200 DATA SCALING SOFTWARE : HKL-3000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 50355
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.440
REMARK 200 RESOLUTION RANGE LOW (A) : 47.300
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 12.300
REMARK 200 R MERGE (I) : 0.13400
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 28.0030
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.44
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.48
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.4
REMARK 200 DATA REDUNDANCY IN SHELL : 8.00
REMARK 200 R MERGE FOR SHELL (I) : 0.79100
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.810
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: SHELXD, MLPHARE, DM, SOLVE/RESOLVE, HKL-3000
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 66.75
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.70
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M TRIS BUFFER, 1 M AMMONIUM
REMARK 280 PHOSPHATE, PH 8.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE
REMARK 280 289K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+5/6
REMARK 290 6555 X-Y,X,Z+1/6
REMARK 290 7555 Y,X,-Z+1/3
REMARK 290 8555 X-Y,-Y,-Z
REMARK 290 9555 -X,-X+Y,-Z+2/3
REMARK 290 10555 -Y,-X,-Z+5/6
REMARK 290 11555 -X+Y,Y,-Z+1/2
REMARK 290 12555 X,X-Y,-Z+1/6
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 98.38967
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 196.77933
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 147.58450
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 245.97417
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 49.19483
REMARK 290 SMTRY1 7 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 7 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 98.38967
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 9 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 9 0.000000 0.000000 -1.000000 196.77933
REMARK 290 SMTRY1 10 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 10 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 245.97417
REMARK 290 SMTRY1 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 11 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 147.58450
REMARK 290 SMTRY1 12 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 12 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 49.19483
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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 300 REMARK: AUTHORS STATE THAT THE ASSEMBLY OF THE BIOLOGICAL UNIT
REMARK 300 THAT IS SHOWN IN REMARK 350 IS PUTATIVE.
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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 5690 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 28120 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -25.9 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
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 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 213.42503
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 5660 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 28360 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -26.9 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, 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 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 147.58450
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 -2
REMARK 465 ASN A -1
REMARK 465 ALA A 0
REMARK 465 VAL A 374
REMARK 465 SER B -2
REMARK 465 ASN B -1
REMARK 465 ALA B 0
REMARK 465 PHE B 373
REMARK 465 VAL B 374
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 DISTANCE
REMARK 500 ND1 HIS A 167 O HOH A 533 2.17
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 LEU A 285 CA - CB - CG ANGL. DEV. = 13.9 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
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 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 ALA A 50 -158.77 -88.56
REMARK 500 SER A 152 -123.21 60.61
REMARK 500 ILE A 176 56.13 38.07
REMARK 500 LYS A 207 45.70 -101.16
REMARK 500 ASP A 288 97.41 -167.64
REMARK 500 GLN B 95 59.84 -92.89
REMARK 500 SER B 152 -117.53 55.72
REMARK 500 LYS B 207 58.99 -105.37
REMARK 500 GLU B 244 126.20 -26.52
REMARK 500 ASP B 288 97.79 -163.27
REMARK 500 SER B 344 139.31 -172.21
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH B 503 DISTANCE = 5.71 ANGSTROMS
REMARK 525 HOH B 553 DISTANCE = 5.56 ANGSTROMS
REMARK 525 HOH B 554 DISTANCE = 6.95 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 501
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A 503
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 504
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 B 502
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: IDP01610 RELATED DB: TARGETDB
DBREF 3I1I A 1 374 UNP Q81KL4 Q81KL4_BACAN 1 374
DBREF 3I1I B 1 374 UNP Q81KL4 Q81KL4_BACAN 1 374
SEQADV 3I1I SER A -2 UNP Q81KL4 EXPRESSION TAG
SEQADV 3I1I ASN A -1 UNP Q81KL4 EXPRESSION TAG
SEQADV 3I1I ALA A 0 UNP Q81KL4 EXPRESSION TAG
SEQADV 3I1I SER B -2 UNP Q81KL4 EXPRESSION TAG
SEQADV 3I1I ASN B -1 UNP Q81KL4 EXPRESSION TAG
SEQADV 3I1I ALA B 0 UNP Q81KL4 EXPRESSION TAG
SEQRES 1 A 377 SER ASN ALA MSE GLN ILE VAL LYS LYS GLU LYS PHE ILE
SEQRES 2 A 377 LEU LYS GLU TYR THR PHE GLU ASN GLY ARG THR ILE PRO
SEQRES 3 A 377 VAL GLN MSE GLY TYR GLU THR TYR GLY THR LEU ASN ARG
SEQRES 4 A 377 GLU ARG SER ASN VAL ILE LEU ILE CYS HIS TYR PHE SER
SEQRES 5 A 377 ALA THR SER HIS ALA ALA GLY LYS TYR THR ALA HIS ASP
SEQRES 6 A 377 GLU GLU SER GLY TRP TRP ASP GLY LEU ILE GLY PRO GLY
SEQRES 7 A 377 LYS ALA ILE ASP THR ASN GLN TYR PHE VAL ILE CYS THR
SEQRES 8 A 377 ASP ASN LEU CYS ASN VAL GLN VAL LYS ASN PRO HIS VAL
SEQRES 9 A 377 ILE THR THR GLY PRO LYS SER ILE ASN PRO LYS THR GLY
SEQRES 10 A 377 ASP GLU TYR ALA MSE ASP PHE PRO VAL PHE THR PHE LEU
SEQRES 11 A 377 ASP VAL ALA ARG MSE GLN CYS GLU LEU ILE LYS ASP MSE
SEQRES 12 A 377 GLY ILE ALA ARG LEU HIS ALA VAL MSE GLY PRO SER ALA
SEQRES 13 A 377 GLY GLY MSE ILE ALA GLN GLN TRP ALA VAL HIS TYR PRO
SEQRES 14 A 377 HIS MSE VAL GLU ARG MSE ILE GLY VAL ILE THR ASN PRO
SEQRES 15 A 377 GLN ASN PRO ILE ILE THR SER VAL ASN VAL ALA GLN ASN
SEQRES 16 A 377 ALA ILE GLU ALA ILE ARG LEU ASP PRO SER TRP LYS GLY
SEQRES 17 A 377 GLY LYS TYR GLY GLU GLU GLN PRO MSE LYS GLY LEU GLN
SEQRES 18 A 377 LEU ALA ASN ARG MSE MSE PHE MSE ASN ALA PHE ASP GLU
SEQRES 19 A 377 HIS PHE TYR GLU THR THR TYR PRO ARG ASN SER ILE GLU
SEQRES 20 A 377 VAL GLU PRO TYR GLU LYS VAL SER SER LEU THR SER PHE
SEQRES 21 A 377 GLU LYS GLU ILE ASN LYS LEU THR TYR ARG SER ILE GLU
SEQRES 22 A 377 LEU VAL ASP ALA ASN SER TRP MSE TYR THR ALA LYS ALA
SEQRES 23 A 377 VAL LEU LEU HIS ASP ILE ALA HIS GLY PHE SER SER LEU
SEQRES 24 A 377 GLU GLU ALA LEU SER ASN VAL GLU ALA ASN VAL LEU MSE
SEQRES 25 A 377 ILE PRO CYS LYS GLN ASP LEU LEU GLN PRO SER ARG TYR
SEQRES 26 A 377 ASN TYR LYS MSE VAL ASP LEU LEU GLN LYS GLN GLY LYS
SEQRES 27 A 377 TYR ALA GLU VAL TYR GLU ILE GLU SER ILE ASN GLY HIS
SEQRES 28 A 377 MSE ALA GLY VAL PHE ASP ILE HIS LEU PHE GLU LYS LYS
SEQRES 29 A 377 VAL TYR GLU PHE LEU ASN ARG LYS VAL SER SER PHE VAL
SEQRES 1 B 377 SER ASN ALA MSE GLN ILE VAL LYS LYS GLU LYS PHE ILE
SEQRES 2 B 377 LEU LYS GLU TYR THR PHE GLU ASN GLY ARG THR ILE PRO
SEQRES 3 B 377 VAL GLN MSE GLY TYR GLU THR TYR GLY THR LEU ASN ARG
SEQRES 4 B 377 GLU ARG SER ASN VAL ILE LEU ILE CYS HIS TYR PHE SER
SEQRES 5 B 377 ALA THR SER HIS ALA ALA GLY LYS TYR THR ALA HIS ASP
SEQRES 6 B 377 GLU GLU SER GLY TRP TRP ASP GLY LEU ILE GLY PRO GLY
SEQRES 7 B 377 LYS ALA ILE ASP THR ASN GLN TYR PHE VAL ILE CYS THR
SEQRES 8 B 377 ASP ASN LEU CYS ASN VAL GLN VAL LYS ASN PRO HIS VAL
SEQRES 9 B 377 ILE THR THR GLY PRO LYS SER ILE ASN PRO LYS THR GLY
SEQRES 10 B 377 ASP GLU TYR ALA MSE ASP PHE PRO VAL PHE THR PHE LEU
SEQRES 11 B 377 ASP VAL ALA ARG MSE GLN CYS GLU LEU ILE LYS ASP MSE
SEQRES 12 B 377 GLY ILE ALA ARG LEU HIS ALA VAL MSE GLY PRO SER ALA
SEQRES 13 B 377 GLY GLY MSE ILE ALA GLN GLN TRP ALA VAL HIS TYR PRO
SEQRES 14 B 377 HIS MSE VAL GLU ARG MSE ILE GLY VAL ILE THR ASN PRO
SEQRES 15 B 377 GLN ASN PRO ILE ILE THR SER VAL ASN VAL ALA GLN ASN
SEQRES 16 B 377 ALA ILE GLU ALA ILE ARG LEU ASP PRO SER TRP LYS GLY
SEQRES 17 B 377 GLY LYS TYR GLY GLU GLU GLN PRO MSE LYS GLY LEU GLN
SEQRES 18 B 377 LEU ALA ASN ARG MSE MSE PHE MSE ASN ALA PHE ASP GLU
SEQRES 19 B 377 HIS PHE TYR GLU THR THR TYR PRO ARG ASN SER ILE GLU
SEQRES 20 B 377 VAL GLU PRO TYR GLU LYS VAL SER SER LEU THR SER PHE
SEQRES 21 B 377 GLU LYS GLU ILE ASN LYS LEU THR TYR ARG SER ILE GLU
SEQRES 22 B 377 LEU VAL ASP ALA ASN SER TRP MSE TYR THR ALA LYS ALA
SEQRES 23 B 377 VAL LEU LEU HIS ASP ILE ALA HIS GLY PHE SER SER LEU
SEQRES 24 B 377 GLU GLU ALA LEU SER ASN VAL GLU ALA ASN VAL LEU MSE
SEQRES 25 B 377 ILE PRO CYS LYS GLN ASP LEU LEU GLN PRO SER ARG TYR
SEQRES 26 B 377 ASN TYR LYS MSE VAL ASP LEU LEU GLN LYS GLN GLY LYS
SEQRES 27 B 377 TYR ALA GLU VAL TYR GLU ILE GLU SER ILE ASN GLY HIS
SEQRES 28 B 377 MSE ALA GLY VAL PHE ASP ILE HIS LEU PHE GLU LYS LYS
SEQRES 29 B 377 VAL TYR GLU PHE LEU ASN ARG LYS VAL SER SER PHE VAL
MODRES 3I1I MSE A 1 MET SELENOMETHIONINE
MODRES 3I1I MSE A 26 MET SELENOMETHIONINE
MODRES 3I1I MSE A 119 MET SELENOMETHIONINE
MODRES 3I1I MSE A 132 MET SELENOMETHIONINE
MODRES 3I1I MSE A 140 MET SELENOMETHIONINE
MODRES 3I1I MSE A 149 MET SELENOMETHIONINE
MODRES 3I1I MSE A 156 MET SELENOMETHIONINE
MODRES 3I1I MSE A 168 MET SELENOMETHIONINE
MODRES 3I1I MSE A 172 MET SELENOMETHIONINE
MODRES 3I1I MSE A 214 MET SELENOMETHIONINE
MODRES 3I1I MSE A 223 MET SELENOMETHIONINE
MODRES 3I1I MSE A 224 MET SELENOMETHIONINE
MODRES 3I1I MSE A 226 MET SELENOMETHIONINE
MODRES 3I1I MSE A 278 MET SELENOMETHIONINE
MODRES 3I1I MSE A 309 MET SELENOMETHIONINE
MODRES 3I1I MSE A 326 MET SELENOMETHIONINE
MODRES 3I1I MSE A 349 MET SELENOMETHIONINE
MODRES 3I1I MSE B 1 MET SELENOMETHIONINE
MODRES 3I1I MSE B 26 MET SELENOMETHIONINE
MODRES 3I1I MSE B 119 MET SELENOMETHIONINE
MODRES 3I1I MSE B 132 MET SELENOMETHIONINE
MODRES 3I1I MSE B 140 MET SELENOMETHIONINE
MODRES 3I1I MSE B 149 MET SELENOMETHIONINE
MODRES 3I1I MSE B 156 MET SELENOMETHIONINE
MODRES 3I1I MSE B 168 MET SELENOMETHIONINE
MODRES 3I1I MSE B 172 MET SELENOMETHIONINE
MODRES 3I1I MSE B 214 MET SELENOMETHIONINE
MODRES 3I1I MSE B 223 MET SELENOMETHIONINE
MODRES 3I1I MSE B 224 MET SELENOMETHIONINE
MODRES 3I1I MSE B 226 MET SELENOMETHIONINE
MODRES 3I1I MSE B 278 MET SELENOMETHIONINE
MODRES 3I1I MSE B 309 MET SELENOMETHIONINE
MODRES 3I1I MSE B 326 MET SELENOMETHIONINE
MODRES 3I1I MSE B 349 MET SELENOMETHIONINE
HET MSE A 1 8
HET MSE A 26 8
HET MSE A 119 8
HET MSE A 132 8
HET MSE A 140 8
HET MSE A 149 8
HET MSE A 156 8
HET MSE A 168 8
HET MSE A 172 8
HET MSE A 214 8
HET MSE A 223 8
HET MSE A 224 13
HET MSE A 226 8
HET MSE A 278 8
HET MSE A 309 8
HET MSE A 326 8
HET MSE A 349 8
HET MSE B 1 8
HET MSE B 26 8
HET MSE B 119 8
HET MSE B 132 8
HET MSE B 140 8
HET MSE B 149 8
HET MSE B 156 8
HET MSE B 168 8
HET MSE B 172 8
HET MSE B 214 8
HET MSE B 223 8
HET MSE B 224 13
HET MSE B 226 8
HET MSE B 278 8
HET MSE B 309 8
HET MSE B 326 8
HET MSE B 349 8
HET PO4 A 501 5
HET ACT A 503 4
HET GOL A 504 6
HET PO4 B 502 5
HETNAM MSE SELENOMETHIONINE
HETNAM PO4 PHOSPHATE ION
HETNAM ACT ACETATE ION
HETNAM GOL GLYCEROL
FORMUL 1 MSE 34(C5 H11 N O2 SE)
FORMUL 3 PO4 2(O4 P 3-)
FORMUL 4 ACT C2 H3 O2 1-
FORMUL 5 GOL C3 H8 O3
FORMUL 7 HOH *347(H2 O)
HELIX 1 1 TYR A 117 PHE A 121 5 5
HELIX 2 2 THR A 125 MSE A 140 1 16
HELIX 3 3 SER A 152 TYR A 165 1 14
HELIX 4 4 PRO A 182 VAL A 189 1 8
HELIX 5 5 ALA A 190 ASP A 200 1 11
HELIX 6 6 PRO A 201 LYS A 207 5 7
HELIX 7 7 PRO A 213 MSE A 226 1 14
HELIX 8 8 ASP A 230 TYR A 238 1 9
HELIX 9 9 VAL A 245 GLU A 249 5 5
HELIX 10 10 THR A 255 SER A 268 1 14
HELIX 11 11 ASP A 273 HIS A 287 1 15
HELIX 12 12 SER A 295 ASN A 302 1 8
HELIX 13 13 SER A 320 GLN A 333 1 14
HELIX 14 14 ASN A 346 HIS A 348 5 3
HELIX 15 15 MSE A 349 ASP A 354 1 6
HELIX 16 16 ILE A 355 LEU A 357 5 3
HELIX 17 17 PHE A 358 ARG A 368 1 11
HELIX 18 18 TYR B 117 PHE B 121 5 5
HELIX 19 19 THR B 125 MSE B 140 1 16
HELIX 20 20 SER B 152 TYR B 165 1 14
HELIX 21 21 PRO B 166 VAL B 169 5 4
HELIX 22 22 PRO B 182 VAL B 189 1 8
HELIX 23 23 VAL B 189 ASP B 200 1 12
HELIX 24 24 PRO B 201 LYS B 207 5 7
HELIX 25 25 PRO B 213 MSE B 226 1 14
HELIX 26 26 ASP B 230 TYR B 238 1 9
HELIX 27 27 VAL B 245 GLU B 249 5 5
HELIX 28 28 THR B 255 SER B 268 1 14
HELIX 29 29 ASP B 273 HIS B 287 1 15
HELIX 30 30 SER B 295 ASN B 302 1 8
HELIX 31 31 SER B 320 GLN B 333 1 14
HELIX 32 32 ASN B 346 HIS B 348 5 3
HELIX 33 33 MSE B 349 ASP B 354 1 6
HELIX 34 34 ILE B 355 LEU B 357 5 3
HELIX 35 35 PHE B 358 ARG B 368 1 11
SHEET 1 A 8 GLU A 7 THR A 15 0
SHEET 2 A 8 THR A 21 TYR A 31 -1 O TYR A 28 N GLU A 7
SHEET 3 A 8 PHE A 84 THR A 88 -1 O VAL A 85 N TYR A 31
SHEET 4 A 8 VAL A 41 CYS A 45 1 N ILE A 44 O ILE A 86
SHEET 5 A 8 ALA A 147 PRO A 151 1 O MSE A 149 N CYS A 45
SHEET 6 A 8 ARG A 171 VAL A 175 1 O VAL A 175 N GLY A 150
SHEET 7 A 8 ASN A 306 ILE A 310 1 O ILE A 310 N GLY A 174
SHEET 8 A 8 ALA A 337 VAL A 339 1 O GLU A 338 N MSE A 309
SHEET 1 B 2 ILE A 72 GLY A 73 0
SHEET 2 B 2 ILE A 78 ASP A 79 1 O ILE A 78 N GLY A 73
SHEET 1 C 8 GLU B 7 THR B 15 0
SHEET 2 C 8 THR B 21 TYR B 31 -1 O TYR B 28 N GLU B 7
SHEET 3 C 8 PHE B 84 THR B 88 -1 O VAL B 85 N TYR B 31
SHEET 4 C 8 VAL B 41 ILE B 44 1 N ILE B 44 O ILE B 86
SHEET 5 C 8 ALA B 147 PRO B 151 1 O MSE B 149 N LEU B 43
SHEET 6 C 8 ARG B 171 VAL B 175 1 O ARG B 171 N VAL B 148
SHEET 7 C 8 ASN B 306 ILE B 310 1 O ASN B 306 N MSE B 172
SHEET 8 C 8 ALA B 337 VAL B 339 1 O GLU B 338 N MSE B 309
SHEET 1 D 2 ILE B 72 GLY B 73 0
SHEET 2 D 2 ILE B 78 ASP B 79 1 O ILE B 78 N GLY B 73
LINK C MSE A 1 N GLN A 2 1555 1555 1.33
LINK C GLN A 25 N MSE A 26 1555 1555 1.33
LINK C MSE A 26 N GLY A 27 1555 1555 1.32
LINK C ALA A 118 N MSE A 119 1555 1555 1.33
LINK C MSE A 119 N ASP A 120 1555 1555 1.33
LINK C ARG A 131 N MSE A 132 1555 1555 1.33
LINK C MSE A 132 N GLN A 133 1555 1555 1.33
LINK C ASP A 139 N MSE A 140 1555 1555 1.33
LINK C MSE A 140 N GLY A 141 1555 1555 1.33
LINK C VAL A 148 N MSE A 149 1555 1555 1.31
LINK C MSE A 149 N GLY A 150 1555 1555 1.32
LINK C GLY A 155 N MSE A 156 1555 1555 1.32
LINK C MSE A 156 N ILE A 157 1555 1555 1.34
LINK C HIS A 167 N MSE A 168 1555 1555 1.33
LINK C MSE A 168 N VAL A 169 1555 1555 1.33
LINK C ARG A 171 N MSE A 172 1555 1555 1.32
LINK C MSE A 172 N ILE A 173 1555 1555 1.33
LINK C PRO A 213 N MSE A 214 1555 1555 1.32
LINK C MSE A 214 N LYS A 215 1555 1555 1.33
LINK C ARG A 222 N MSE A 223 1555 1555 1.32
LINK C MSE A 223 N MSE A 224 1555 1555 1.32
LINK C MSE A 224 N PHE A 225 1555 1555 1.33
LINK C PHE A 225 N MSE A 226 1555 1555 1.33
LINK C MSE A 226 N ASN A 227 1555 1555 1.33
LINK C TRP A 277 N MSE A 278 1555 1555 1.33
LINK C MSE A 278 N TYR A 279 1555 1555 1.34
LINK C LEU A 308 N MSE A 309 1555 1555 1.33
LINK C MSE A 309 N ILE A 310 1555 1555 1.34
LINK C LYS A 325 N MSE A 326 1555 1555 1.32
LINK C MSE A 326 N VAL A 327 1555 1555 1.33
LINK C HIS A 348 N MSE A 349 1555 1555 1.33
LINK C MSE A 349 N ALA A 350 1555 1555 1.33
LINK C MSE B 1 N GLN B 2 1555 1555 1.33
LINK C GLN B 25 N MSE B 26 1555 1555 1.32
LINK C MSE B 26 N GLY B 27 1555 1555 1.33
LINK C ALA B 118 N MSE B 119 1555 1555 1.33
LINK C MSE B 119 N ASP B 120 1555 1555 1.32
LINK C ARG B 131 N MSE B 132 1555 1555 1.32
LINK C MSE B 132 N GLN B 133 1555 1555 1.32
LINK C ASP B 139 N MSE B 140 1555 1555 1.33
LINK C MSE B 140 N GLY B 141 1555 1555 1.33
LINK C VAL B 148 N MSE B 149 1555 1555 1.32
LINK C MSE B 149 N GLY B 150 1555 1555 1.32
LINK C GLY B 155 N MSE B 156 1555 1555 1.32
LINK C MSE B 156 N ILE B 157 1555 1555 1.33
LINK C HIS B 167 N MSE B 168 1555 1555 1.33
LINK C MSE B 168 N VAL B 169 1555 1555 1.33
LINK C ARG B 171 N MSE B 172 1555 1555 1.31
LINK C MSE B 172 N ILE B 173 1555 1555 1.34
LINK C PRO B 213 N MSE B 214 1555 1555 1.34
LINK C MSE B 214 N LYS B 215 1555 1555 1.33
LINK C ARG B 222 N MSE B 223 1555 1555 1.34
LINK C MSE B 223 N MSE B 224 1555 1555 1.33
LINK C MSE B 224 N PHE B 225 1555 1555 1.33
LINK C PHE B 225 N MSE B 226 1555 1555 1.33
LINK C MSE B 226 N ASN B 227 1555 1555 1.32
LINK C TRP B 277 N MSE B 278 1555 1555 1.33
LINK C MSE B 278 N TYR B 279 1555 1555 1.34
LINK C LEU B 308 N MSE B 309 1555 1555 1.33
LINK C MSE B 309 N ILE B 310 1555 1555 1.35
LINK C LYS B 325 N MSE B 326 1555 1555 1.32
LINK C MSE B 326 N VAL B 327 1555 1555 1.33
LINK C HIS B 348 N MSE B 349 1555 1555 1.33
LINK C MSE B 349 N ALA B 350 1555 1555 1.34
SITE 1 AC1 5 ASP A 230 GLU A 231 HIS A 232 ARG A 321
SITE 2 AC1 5 HOH A 393
SITE 1 AC2 3 THR A 104 HOH A 421 HOH A 513
SITE 1 AC3 3 ARG A 131 HIS A 164 GLU B 210
SITE 1 AC4 4 ASP B 230 GLU B 231 ARG B 321 HOH B 396
CRYST1 123.221 123.221 295.169 90.00 90.00 120.00 P 61 2 2 24
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 0.008115 0.004685 0.000000 0.00000
SCALE2 0.000000 0.009371 0.000000 0.00000
SCALE3 0.000000 0.000000 0.003388 0.00000
TER 3057 PHE A 373
TER 6062 SER B 372
MASTER 428 0 38 35 20 0 5 6 6427 2 364 58
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