HEADER OXIDOREDUCTASE 03-AUG-13 4M1Q
TITLE CRYSTAL STRUCTURE OF L-LACTATE DEHYDROGENASE FROM BACILLUS
TITLE 2 SELENITIREDUCENS MLS10, NYSGRC TARGET 029814.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: L-LACTATE DEHYDROGENASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: L-LDH;
COMPND 5 EC: 1.1.1.27;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BACILLUS SELENITIREDUCENS;
SOURCE 3 ORGANISM_TAXID: 439292;
SOURCE 4 STRAIN: MLS10;
SOURCE 5 GENE: LDH, BSEL_2311;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)CODON+RIL;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: BC-PSGX3(BC)
KEYWDS STRUCTURAL GENOMICS, PROTEIN STRUCTURE INITIATIVE, L-LACTATE
KEYWDS 2 DEHYDROGENASE, NYSGRC, PSI-BIOLOGY, NEW YORK STRUCTURAL GENOMICS
KEYWDS 3 RESEARCH CONSORTIUM, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR V.N.MALASHKEVICH,R.BHOSLE,R.TORO,B.HILLERICH,A.GIZZI,S.GARFORTH,
AUTHOR 2 A.KAR,M.K.CHAN,J.LAFLUER,H.PATEL,B.MATIKAINEN,S.CHAMALA,S.LIM,
AUTHOR 3 A.CELIKGIL,G.VILLEGAS,B.EVANS,J.LOVE,A.FISER,K.KHAFIZOV,R.SEIDEL,
AUTHOR 4 J.B.BONANNO,S.C.ALMO,NEW YORK STRUCTURAL GENOMICS RESEARCH
AUTHOR 5 CONSORTIUM (NYSGRC)
REVDAT 1 21-AUG-13 4M1Q 0
JRNL AUTH V.N.MALASHKEVICH,R.BHOSLE,R.TORO,B.HILLERICH,A.GIZZI,
JRNL AUTH 2 S.GARFORTH,A.KAR,M.K.CHAN,J.LAFLUER,H.PATEL,B.MATIKAINEN,
JRNL AUTH 3 S.CHAMALA,S.LIM,A.CELIKGIL,G.VILLEGAS,B.EVANS,J.LOVE,
JRNL AUTH 4 A.FISER,K.KHAFIZOV,R.SEIDEL,J.B.BONANNO,S.C.ALMO
JRNL TITL CRYSTAL STRUCTURE OF L-LACTATE DEHYDROGENASE FROM BACILLUS
JRNL TITL 2 SELENITIREDUCENS MLS10, NYSGRC TARGET 029814.
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.7.0032
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.39
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 108441
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) : 0.181
REMARK 3 R VALUE (WORKING SET) : 0.180
REMARK 3 FREE R VALUE : 0.196
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 5414
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) : 1.60
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.64
REMARK 3 REFLECTION IN BIN (WORKING SET) : 7505
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.81
REMARK 3 BIN R VALUE (WORKING SET) : 0.2430
REMARK 3 BIN FREE R VALUE SET COUNT : 380
REMARK 3 BIN FREE R VALUE : 0.2700
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4822
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 58
REMARK 3 SOLVENT ATOMS : 613
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 21.91
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 3.85000
REMARK 3 B22 (A**2) : 3.85000
REMARK 3 B33 (A**2) : -7.70000
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 OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.016
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.016
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.034
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.865
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.964
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.959
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 5046 ; 0.008 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 6848 ; 1.311 ; 1.984
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 646 ; 5.435 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 226 ;35.721 ;24.513
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 825 ;13.352 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 30 ;19.546 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 781 ; 0.085 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3756 ; 0.006 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
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): 2509 ; 1.019 ; 2.344
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3138 ; 1.740 ;31.525
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2537 ; 1.807 ; 2.825
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
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 : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 3 A 314
REMARK 3 RESIDUE RANGE : A 401 A 401
REMARK 3 ORIGIN FOR THE GROUP (A): -18.9077 59.2127 15.6076
REMARK 3 T TENSOR
REMARK 3 T11: 0.0476 T22: 0.0058
REMARK 3 T33: 0.0488 T12: -0.0136
REMARK 3 T13: -0.0021 T23: -0.0064
REMARK 3 L TENSOR
REMARK 3 L11: 0.1651 L22: 0.3603
REMARK 3 L33: 0.4542 L12: 0.1411
REMARK 3 L13: -0.0908 L23: 0.0012
REMARK 3 S TENSOR
REMARK 3 S11: -0.0331 S12: 0.0188 S13: 0.0072
REMARK 3 S21: -0.0470 S22: 0.0125 S23: 0.0373
REMARK 3 S31: 0.0498 S32: -0.0303 S33: 0.0206
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 4 B 315
REMARK 3 RESIDUE RANGE : B 401 B 401
REMARK 3 ORIGIN FOR THE GROUP (A): -1.5547 91.0451 24.4158
REMARK 3 T TENSOR
REMARK 3 T11: 0.0578 T22: 0.0089
REMARK 3 T33: 0.0474 T12: -0.0194
REMARK 3 T13: 0.0043 T23: -0.0050
REMARK 3 L TENSOR
REMARK 3 L11: 0.1357 L22: 0.3407
REMARK 3 L33: 0.3932 L12: 0.0480
REMARK 3 L13: 0.0034 L23: 0.0020
REMARK 3 S TENSOR
REMARK 3 S11: -0.0067 S12: -0.0064 S13: 0.0023
REMARK 3 S21: -0.0307 S22: 0.0166 S23: -0.0120
REMARK 3 S31: -0.0837 S32: 0.0464 S33: -0.0098
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: U VALUES : WITH TLS ADDED
REMARK 3 HYDROGENS HAVE BEEN USED IF PRESENT IN THE INPUT
REMARK 4
REMARK 4 4M1Q COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-AUG-13.
REMARK 100 THE RCSB ID CODE IS RCSB081355.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 18-JUL-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.2
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 31-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : NULL
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9791
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RAYONIX MX225HE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 108623
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.600
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 6.800
REMARK 200 R MERGE (I) : 0.10400
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.63
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 7.10
REMARK 200 R MERGE FOR SHELL (I) : 0.93700
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: SHELXS
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 53.69
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.66
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M NA2HPO4/KH2PO4, PH 6.2, 35% MPD,
REMARK 280 VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+1/3
REMARK 290 6555 -X,-X+Y,-Z+2/3
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 140.17867
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 70.08933
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 70.08933
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 140.17867
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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 18120 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 45140 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -198.0 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 141.81686
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 70.08933
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 -21
REMARK 465 HIS A -20
REMARK 465 HIS A -19
REMARK 465 HIS A -18
REMARK 465 HIS A -17
REMARK 465 HIS A -16
REMARK 465 HIS A -15
REMARK 465 SER A -14
REMARK 465 SER A -13
REMARK 465 GLY A -12
REMARK 465 VAL A -11
REMARK 465 ASP A -10
REMARK 465 LEU A -9
REMARK 465 GLY A -8
REMARK 465 THR A -7
REMARK 465 GLU A -6
REMARK 465 ASN A -5
REMARK 465 LEU A -4
REMARK 465 TYR A -3
REMARK 465 PHE A -2
REMARK 465 GLN A -1
REMARK 465 SER A 0
REMARK 465 MSE A 1
REMARK 465 ASN A 2
REMARK 465 ASP A 315
REMARK 465 MSE A 316
REMARK 465 LYS A 317
REMARK 465 MSE B -21
REMARK 465 HIS B -20
REMARK 465 HIS B -19
REMARK 465 HIS B -18
REMARK 465 HIS B -17
REMARK 465 HIS B -16
REMARK 465 HIS B -15
REMARK 465 SER B -14
REMARK 465 SER B -13
REMARK 465 GLY B -12
REMARK 465 VAL B -11
REMARK 465 ASP B -10
REMARK 465 LEU B -9
REMARK 465 GLY B -8
REMARK 465 THR B -7
REMARK 465 GLU B -6
REMARK 465 ASN B -5
REMARK 465 LEU B -4
REMARK 465 TYR B -3
REMARK 465 PHE B -2
REMARK 465 GLN B -1
REMARK 465 SER B 0
REMARK 465 MSE B 1
REMARK 465 ASN B 2
REMARK 465 THR B 3
REMARK 465 GLN B 84
REMARK 465 LYS B 85
REMARK 465 PRO B 86
REMARK 465 MSE B 316
REMARK 465 LYS B 317
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 MSE A 199 CG - SE - CE ANGL. DEV. = -20.4 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 ASN A 51 49.64 -87.55
REMARK 500 PRO A 86 -45.22 -27.22
REMARK 500 ASN A 114 44.56 -144.50
REMARK 500 HIS A 233 -30.68 -160.33
REMARK 500 ASN B 28 64.86 62.76
REMARK 500 ASN B 114 42.91 -143.16
REMARK 500 VAL B 184 77.07 -101.30
REMARK 500 LYS B 203 56.42 -141.51
REMARK 500 HIS B 233 -32.54 -158.09
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 A 765 DISTANCE = 6.21 ANGSTROMS
REMARK 525 HOH A 802 DISTANCE = 8.19 ANGSTROMS
REMARK 525 HOH B 776 DISTANCE = 8.90 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 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MPD A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MPD A 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MPD A 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MPD B 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MPD B 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MPD B 404
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: NYSGRC-029814 RELATED DB: TARGETTRACK
DBREF 4M1Q A 1 317 UNP D6XW60 D6XW60_BACIE 1 317
DBREF 4M1Q B 1 317 UNP D6XW60 D6XW60_BACIE 1 317
SEQADV 4M1Q MSE A -21 UNP D6XW60 EXPRESSION TAG
SEQADV 4M1Q HIS A -20 UNP D6XW60 EXPRESSION TAG
SEQADV 4M1Q HIS A -19 UNP D6XW60 EXPRESSION TAG
SEQADV 4M1Q HIS A -18 UNP D6XW60 EXPRESSION TAG
SEQADV 4M1Q HIS A -17 UNP D6XW60 EXPRESSION TAG
SEQADV 4M1Q HIS A -16 UNP D6XW60 EXPRESSION TAG
SEQADV 4M1Q HIS A -15 UNP D6XW60 EXPRESSION TAG
SEQADV 4M1Q SER A -14 UNP D6XW60 EXPRESSION TAG
SEQADV 4M1Q SER A -13 UNP D6XW60 EXPRESSION TAG
SEQADV 4M1Q GLY A -12 UNP D6XW60 EXPRESSION TAG
SEQADV 4M1Q VAL A -11 UNP D6XW60 EXPRESSION TAG
SEQADV 4M1Q ASP A -10 UNP D6XW60 EXPRESSION TAG
SEQADV 4M1Q LEU A -9 UNP D6XW60 EXPRESSION TAG
SEQADV 4M1Q GLY A -8 UNP D6XW60 EXPRESSION TAG
SEQADV 4M1Q THR A -7 UNP D6XW60 EXPRESSION TAG
SEQADV 4M1Q GLU A -6 UNP D6XW60 EXPRESSION TAG
SEQADV 4M1Q ASN A -5 UNP D6XW60 EXPRESSION TAG
SEQADV 4M1Q LEU A -4 UNP D6XW60 EXPRESSION TAG
SEQADV 4M1Q TYR A -3 UNP D6XW60 EXPRESSION TAG
SEQADV 4M1Q PHE A -2 UNP D6XW60 EXPRESSION TAG
SEQADV 4M1Q GLN A -1 UNP D6XW60 EXPRESSION TAG
SEQADV 4M1Q SER A 0 UNP D6XW60 EXPRESSION TAG
SEQADV 4M1Q MSE B -21 UNP D6XW60 EXPRESSION TAG
SEQADV 4M1Q HIS B -20 UNP D6XW60 EXPRESSION TAG
SEQADV 4M1Q HIS B -19 UNP D6XW60 EXPRESSION TAG
SEQADV 4M1Q HIS B -18 UNP D6XW60 EXPRESSION TAG
SEQADV 4M1Q HIS B -17 UNP D6XW60 EXPRESSION TAG
SEQADV 4M1Q HIS B -16 UNP D6XW60 EXPRESSION TAG
SEQADV 4M1Q HIS B -15 UNP D6XW60 EXPRESSION TAG
SEQADV 4M1Q SER B -14 UNP D6XW60 EXPRESSION TAG
SEQADV 4M1Q SER B -13 UNP D6XW60 EXPRESSION TAG
SEQADV 4M1Q GLY B -12 UNP D6XW60 EXPRESSION TAG
SEQADV 4M1Q VAL B -11 UNP D6XW60 EXPRESSION TAG
SEQADV 4M1Q ASP B -10 UNP D6XW60 EXPRESSION TAG
SEQADV 4M1Q LEU B -9 UNP D6XW60 EXPRESSION TAG
SEQADV 4M1Q GLY B -8 UNP D6XW60 EXPRESSION TAG
SEQADV 4M1Q THR B -7 UNP D6XW60 EXPRESSION TAG
SEQADV 4M1Q GLU B -6 UNP D6XW60 EXPRESSION TAG
SEQADV 4M1Q ASN B -5 UNP D6XW60 EXPRESSION TAG
SEQADV 4M1Q LEU B -4 UNP D6XW60 EXPRESSION TAG
SEQADV 4M1Q TYR B -3 UNP D6XW60 EXPRESSION TAG
SEQADV 4M1Q PHE B -2 UNP D6XW60 EXPRESSION TAG
SEQADV 4M1Q GLN B -1 UNP D6XW60 EXPRESSION TAG
SEQADV 4M1Q SER B 0 UNP D6XW60 EXPRESSION TAG
SEQRES 1 A 339 MSE HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU
SEQRES 2 A 339 GLY THR GLU ASN LEU TYR PHE GLN SER MSE ASN THR LYS
SEQRES 3 A 339 THR SER ARG VAL VAL ILE ILE GLY THR GLY ALA VAL GLY
SEQRES 4 A 339 SER SER TYR ALA PHE SER MSE ILE ASN GLN ASN VAL THR
SEQRES 5 A 339 ASP GLU MSE VAL LEU ILE ASP LEU ASP LYS ARG LYS THR
SEQRES 6 A 339 GLU GLY ASP ALA MSE ASP LEU ASN HIS GLY ILE PRO PHE
SEQRES 7 A 339 GLY ALA PRO THR LYS VAL TRP ALA GLY ASP TYR GLY ASP
SEQRES 8 A 339 CYS LYS SER ALA ASP ILE VAL VAL ILE THR ALA GLY ALA
SEQRES 9 A 339 ALA GLN LYS PRO GLY GLU THR ARG LEU ASP LEU VAL GLU
SEQRES 10 A 339 LYS ASN ALA ASN ILE PHE LYS GLY ILE VAL ASP GLN VAL
SEQRES 11 A 339 MSE GLY SER GLY PHE ASN GLY ILE PHE ILE ILE ALA THR
SEQRES 12 A 339 ASN PRO VAL ASP VAL LEU ALA TYR ALA THR TRP LYS PHE
SEQRES 13 A 339 SER GLY LEU PRO LYS GLU ARG VAL ILE GLY SER GLY THR
SEQRES 14 A 339 ILE LEU ASP THR ALA ARG PHE ARG PHE LEU LEU SER GLU
SEQRES 15 A 339 TYR PHE ASP ILE ASP VAL ARG ASN ILE HIS GLY TYR ILE
SEQRES 16 A 339 MSE GLY GLU HIS GLY ASP THR GLU LEU PRO VAL TRP SER
SEQRES 17 A 339 GLN THR ARG ILE GLY SER GLU PRO ILE SER ARG TYR MSE
SEQRES 18 A 339 ASP LYS TYR LYS PRO ASP GLY SER ASN LYS ASP LEU ASP
SEQRES 19 A 339 GLU ILE PHE VAL ASN VAL ARG ASP ALA ALA TYR HIS ILE
SEQRES 20 A 339 ILE GLU ARG LYS GLY ALA THR HIS TYR ALA ILE ALA MSE
SEQRES 21 A 339 GLY LEU ALA ARG LEU THR LYS ALA ILE LEU ARG ASN GLU
SEQRES 22 A 339 GLN SER ILE LEU THR VAL SER THR LEU MSE GLU GLY GLU
SEQRES 23 A 339 TYR ASP LEU ASP ASP VAL TYR ILE GLY VAL PRO ALA ILE
SEQRES 24 A 339 VAL SER GLN LYS GLY VAL GLU ARG ALA ILE GLU ILE ASP
SEQRES 25 A 339 LEU ASN ASP GLU GLU MSE LYS LYS LEU HIS HIS SER SER
SEQRES 26 A 339 ASN THR LEU LYS ASP VAL MSE LYS PRO ILE PHE ASP MSE
SEQRES 27 A 339 LYS
SEQRES 1 B 339 MSE HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU
SEQRES 2 B 339 GLY THR GLU ASN LEU TYR PHE GLN SER MSE ASN THR LYS
SEQRES 3 B 339 THR SER ARG VAL VAL ILE ILE GLY THR GLY ALA VAL GLY
SEQRES 4 B 339 SER SER TYR ALA PHE SER MSE ILE ASN GLN ASN VAL THR
SEQRES 5 B 339 ASP GLU MSE VAL LEU ILE ASP LEU ASP LYS ARG LYS THR
SEQRES 6 B 339 GLU GLY ASP ALA MSE ASP LEU ASN HIS GLY ILE PRO PHE
SEQRES 7 B 339 GLY ALA PRO THR LYS VAL TRP ALA GLY ASP TYR GLY ASP
SEQRES 8 B 339 CYS LYS SER ALA ASP ILE VAL VAL ILE THR ALA GLY ALA
SEQRES 9 B 339 ALA GLN LYS PRO GLY GLU THR ARG LEU ASP LEU VAL GLU
SEQRES 10 B 339 LYS ASN ALA ASN ILE PHE LYS GLY ILE VAL ASP GLN VAL
SEQRES 11 B 339 MSE GLY SER GLY PHE ASN GLY ILE PHE ILE ILE ALA THR
SEQRES 12 B 339 ASN PRO VAL ASP VAL LEU ALA TYR ALA THR TRP LYS PHE
SEQRES 13 B 339 SER GLY LEU PRO LYS GLU ARG VAL ILE GLY SER GLY THR
SEQRES 14 B 339 ILE LEU ASP THR ALA ARG PHE ARG PHE LEU LEU SER GLU
SEQRES 15 B 339 TYR PHE ASP ILE ASP VAL ARG ASN ILE HIS GLY TYR ILE
SEQRES 16 B 339 MSE GLY GLU HIS GLY ASP THR GLU LEU PRO VAL TRP SER
SEQRES 17 B 339 GLN THR ARG ILE GLY SER GLU PRO ILE SER ARG TYR MSE
SEQRES 18 B 339 ASP LYS TYR LYS PRO ASP GLY SER ASN LYS ASP LEU ASP
SEQRES 19 B 339 GLU ILE PHE VAL ASN VAL ARG ASP ALA ALA TYR HIS ILE
SEQRES 20 B 339 ILE GLU ARG LYS GLY ALA THR HIS TYR ALA ILE ALA MSE
SEQRES 21 B 339 GLY LEU ALA ARG LEU THR LYS ALA ILE LEU ARG ASN GLU
SEQRES 22 B 339 GLN SER ILE LEU THR VAL SER THR LEU MSE GLU GLY GLU
SEQRES 23 B 339 TYR ASP LEU ASP ASP VAL TYR ILE GLY VAL PRO ALA ILE
SEQRES 24 B 339 VAL SER GLN LYS GLY VAL GLU ARG ALA ILE GLU ILE ASP
SEQRES 25 B 339 LEU ASN ASP GLU GLU MSE LYS LYS LEU HIS HIS SER SER
SEQRES 26 B 339 ASN THR LEU LYS ASP VAL MSE LYS PRO ILE PHE ASP MSE
SEQRES 27 B 339 LYS
MODRES 4M1Q MSE A 24 MET SELENOMETHIONINE
MODRES 4M1Q MSE A 33 MET SELENOMETHIONINE
MODRES 4M1Q MSE A 48 MET SELENOMETHIONINE
MODRES 4M1Q MSE A 109 MET SELENOMETHIONINE
MODRES 4M1Q MSE A 174 MET SELENOMETHIONINE
MODRES 4M1Q MSE A 199 MET SELENOMETHIONINE
MODRES 4M1Q MSE A 238 MET SELENOMETHIONINE
MODRES 4M1Q MSE A 261 MET SELENOMETHIONINE
MODRES 4M1Q MSE A 296 MET SELENOMETHIONINE
MODRES 4M1Q MSE A 310 MET SELENOMETHIONINE
MODRES 4M1Q MSE B 24 MET SELENOMETHIONINE
MODRES 4M1Q MSE B 33 MET SELENOMETHIONINE
MODRES 4M1Q MSE B 48 MET SELENOMETHIONINE
MODRES 4M1Q MSE B 109 MET SELENOMETHIONINE
MODRES 4M1Q MSE B 174 MET SELENOMETHIONINE
MODRES 4M1Q MSE B 199 MET SELENOMETHIONINE
MODRES 4M1Q MSE B 238 MET SELENOMETHIONINE
MODRES 4M1Q MSE B 261 MET SELENOMETHIONINE
MODRES 4M1Q MSE B 296 MET SELENOMETHIONINE
MODRES 4M1Q MSE B 310 MET SELENOMETHIONINE
HET MSE A 24 8
HET MSE A 33 8
HET MSE A 48 8
HET MSE A 109 8
HET MSE A 174 8
HET MSE A 199 8
HET MSE A 238 13
HET MSE A 261 8
HET MSE A 296 8
HET MSE A 310 8
HET MSE B 24 8
HET MSE B 33 8
HET MSE B 48 8
HET MSE B 109 8
HET MSE B 174 8
HET MSE B 199 8
HET MSE B 238 13
HET MSE B 261 8
HET MSE B 296 8
HET MSE B 310 8
HET PO4 A 401 5
HET MPD A 402 8
HET MPD A 403 8
HET MPD A 404 8
HET PO4 B 401 5
HET MPD B 402 8
HET MPD B 403 8
HET MPD B 404 8
HETNAM MSE SELENOMETHIONINE
HETNAM PO4 PHOSPHATE ION
HETNAM MPD (4S)-2-METHYL-2,4-PENTANEDIOL
FORMUL 1 MSE 20(C5 H11 N O2 SE)
FORMUL 3 PO4 2(O4 P 3-)
FORMUL 4 MPD 6(C6 H14 O2)
FORMUL 11 HOH *613(H2 O)
HELIX 1 1 GLY A 14 ASN A 28 1 15
HELIX 2 2 ASP A 39 ASN A 51 1 13
HELIX 3 3 GLY A 53 GLY A 57 5 5
HELIX 4 4 ASP A 66 LYS A 71 5 6
HELIX 5 5 THR A 89 SER A 111 1 23
HELIX 6 6 PRO A 123 GLY A 136 1 14
HELIX 7 7 PRO A 138 GLU A 140 5 3
HELIX 8 8 THR A 147 ASP A 163 1 17
HELIX 9 9 ASP A 165 ARG A 167 5 3
HELIX 10 10 TRP A 185 GLN A 187 5 3
HELIX 11 11 ILE A 195 LYS A 203 1 9
HELIX 12 12 SER A 207 ASP A 220 1 14
HELIX 13 13 ASP A 220 GLY A 230 1 11
HELIX 14 14 HIS A 233 ARG A 249 1 17
HELIX 15 15 GLU A 264 ASP A 266 5 3
HELIX 16 16 ASN A 292 LYS A 311 1 20
HELIX 17 17 GLY B 14 ASN B 28 1 15
HELIX 18 18 ASP B 39 ASN B 51 1 13
HELIX 19 19 GLY B 53 GLY B 57 5 5
HELIX 20 20 ASP B 66 LYS B 71 5 6
HELIX 21 21 THR B 89 SER B 111 1 23
HELIX 22 22 PRO B 123 GLY B 136 1 14
HELIX 23 23 PRO B 138 GLU B 140 5 3
HELIX 24 24 THR B 147 ASP B 163 1 17
HELIX 25 25 ASP B 165 ARG B 167 5 3
HELIX 26 26 TRP B 185 GLN B 187 5 3
HELIX 27 27 ILE B 195 LYS B 203 1 9
HELIX 28 28 SER B 207 ASP B 220 1 14
HELIX 29 29 ASP B 220 GLY B 230 1 11
HELIX 30 30 HIS B 233 ARG B 249 1 17
HELIX 31 31 GLU B 264 ASP B 266 5 3
HELIX 32 32 ASN B 292 LYS B 311 1 20
SHEET 1 A 6 LYS A 61 ALA A 64 0
SHEET 2 A 6 GLU A 32 ILE A 36 1 N MSE A 33 O LYS A 61
SHEET 3 A 6 ARG A 7 ILE A 11 1 N ILE A 10 O VAL A 34
SHEET 4 A 6 ILE A 75 ILE A 78 1 O VAL A 77 N VAL A 9
SHEET 5 A 6 ILE A 116 ILE A 119 1 O ILE A 118 N VAL A 76
SHEET 6 A 6 VAL A 142 GLY A 144 1 O ILE A 143 N PHE A 117
SHEET 1 B 3 ILE A 169 HIS A 170 0
SHEET 2 B 3 ARG A 189 ILE A 190 -1 O ARG A 189 N HIS A 170
SHEET 3 B 3 GLU A 193 PRO A 194 -1 O GLU A 193 N ILE A 190
SHEET 1 C 2 ILE A 173 MSE A 174 0
SHEET 2 C 2 LEU A 182 PRO A 183 -1 O LEU A 182 N MSE A 174
SHEET 1 D 3 SER A 253 GLU A 262 0
SHEET 2 D 3 ASP A 268 SER A 279 -1 O VAL A 270 N MSE A 261
SHEET 3 D 3 GLY A 282 ALA A 286 -1 O GLU A 284 N ILE A 277
SHEET 1 E 6 LYS B 61 ALA B 64 0
SHEET 2 E 6 GLU B 32 ILE B 36 1 N MSE B 33 O LYS B 61
SHEET 3 E 6 ARG B 7 ILE B 11 1 N ILE B 10 O VAL B 34
SHEET 4 E 6 ILE B 75 ILE B 78 1 O VAL B 77 N VAL B 9
SHEET 5 E 6 ILE B 116 ILE B 119 1 O ILE B 118 N ILE B 78
SHEET 6 E 6 VAL B 142 GLY B 144 1 O ILE B 143 N PHE B 117
SHEET 1 F 3 ILE B 169 HIS B 170 0
SHEET 2 F 3 ARG B 189 ILE B 190 -1 O ARG B 189 N HIS B 170
SHEET 3 F 3 GLU B 193 PRO B 194 -1 O GLU B 193 N ILE B 190
SHEET 1 G 2 ILE B 173 MSE B 174 0
SHEET 2 G 2 LEU B 182 PRO B 183 -1 O LEU B 182 N MSE B 174
SHEET 1 H 3 SER B 253 GLU B 262 0
SHEET 2 H 3 ASP B 268 SER B 279 -1 O VAL B 270 N MSE B 261
SHEET 3 H 3 GLY B 282 ALA B 286 -1 O GLY B 282 N SER B 279
LINK C SER A 23 N MSE A 24 1555 1555 1.33
LINK C MSE A 24 N ILE A 25 1555 1555 1.32
LINK C GLU A 32 N MSE A 33 1555 1555 1.33
LINK C MSE A 33 N VAL A 34 1555 1555 1.33
LINK C ALA A 47 N MSE A 48 1555 1555 1.33
LINK C MSE A 48 N ASP A 49 1555 1555 1.34
LINK C VAL A 108 N MSE A 109 1555 1555 1.33
LINK C MSE A 109 N GLY A 110 1555 1555 1.33
LINK C ILE A 173 N MSE A 174 1555 1555 1.34
LINK C MSE A 174 N GLY A 175 1555 1555 1.33
LINK C TYR A 198 N MSE A 199 1555 1555 1.31
LINK C MSE A 199 N ASP A 200 1555 1555 1.31
LINK C ALA A 237 N MSE A 238 1555 1555 1.34
LINK C MSE A 238 N GLY A 239 1555 1555 1.32
LINK C LEU A 260 N MSE A 261 1555 1555 1.33
LINK C MSE A 261 N GLU A 262 1555 1555 1.33
LINK C GLU A 295 N MSE A 296 1555 1555 1.33
LINK C MSE A 296 N LYS A 297 1555 1555 1.33
LINK C VAL A 309 N MSE A 310 1555 1555 1.33
LINK C MSE A 310 N LYS A 311 1555 1555 1.34
LINK C SER B 23 N MSE B 24 1555 1555 1.33
LINK C MSE B 24 N ILE B 25 1555 1555 1.33
LINK C GLU B 32 N MSE B 33 1555 1555 1.33
LINK C MSE B 33 N VAL B 34 1555 1555 1.34
LINK C ALA B 47 N MSE B 48 1555 1555 1.34
LINK C MSE B 48 N ASP B 49 1555 1555 1.33
LINK C VAL B 108 N MSE B 109 1555 1555 1.34
LINK C MSE B 109 N GLY B 110 1555 1555 1.33
LINK C ILE B 173 N MSE B 174 1555 1555 1.34
LINK C MSE B 174 N GLY B 175 1555 1555 1.33
LINK C TYR B 198 N MSE B 199 1555 1555 1.33
LINK C MSE B 199 N ASP B 200 1555 1555 1.34
LINK C ALA B 237 N MSE B 238 1555 1555 1.33
LINK C MSE B 238 N GLY B 239 1555 1555 1.34
LINK C LEU B 260 N MSE B 261 1555 1555 1.33
LINK C MSE B 261 N GLU B 262 1555 1555 1.33
LINK C GLU B 295 N MSE B 296 1555 1555 1.33
LINK C MSE B 296 N LYS B 297 1555 1555 1.34
LINK C VAL B 309 N MSE B 310 1555 1555 1.33
LINK C MSE B 310 N LYS B 311 1555 1555 1.33
CISPEP 1 ASN A 122 PRO A 123 0 -1.41
CISPEP 2 ASN B 122 PRO B 123 0 1.03
SITE 1 AC1 11 ARG A 155 HIS A 170 TYR A 172 HOH A 505
SITE 2 AC1 11 HOH A 520 HOH A 539 ASN B 168 HIS B 170
SITE 3 AC1 11 GLY B 191 SER B 192 HOH B 508
SITE 1 AC2 6 MSE A 48 ASN A 51 HIS A 52 HOH A 603
SITE 2 AC2 6 PHE B 156 ASN B 217
SITE 1 AC3 5 ASP A 212 ASP B 266 ASP B 268 HOH B 749
SITE 2 AC3 5 HOH B 750
SITE 1 AC4 8 GLY A 81 ILE A 100 HOH A 536 HOH A 630
SITE 2 AC4 8 HOH A 777 PRO B 312 PHE B 314 HOH B 681
SITE 1 AC5 11 ASN A 168 HIS A 170 GLY A 191 SER A 192
SITE 2 AC5 11 ARG B 155 HIS B 170 TYR B 172 HOH B 506
SITE 3 AC5 11 HOH B 511 HOH B 513 HOH B 589
SITE 1 AC6 6 PHE A 156 ASN A 217 MSE B 48 ASN B 51
SITE 2 AC6 6 HIS B 52 HOH B 565
SITE 1 AC7 6 LEU A 38 ASP A 39 ALA B 98 ASN B 99
SITE 2 AC7 6 LYS B 102 HOH B 777
SITE 1 AC8 5 TRP B 185 ASN B 208 ASP B 212 HOH B 595
SITE 2 AC8 5 HOH B 675
CRYST1 81.878 81.878 210.268 90.00 90.00 120.00 P 32 2 1 12
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 0.012213 0.007051 0.000000 0.00000
SCALE2 0.000000 0.014103 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004756 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
