HEADER TRANSFERASE 23-APR-13 4KBE
TITLE CRYSTAL STRUCTURE OF PROBABLE SUGAR KINASE PROTEIN FROM RHIZOBIUM ETLI
TITLE 2 CFN 42 COMPLEXED WITH BENZOGUANAMINE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROBABLE SUGAR KINASE PROTEIN;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RHIZOBIUM ETLI;
SOURCE 3 ORGANISM_TAXID: 347834;
SOURCE 4 STRAIN: CFN 42;
SOURCE 5 GENE: RHE_CH00135;
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, NYSGRC, PSI-
KEYWDS 2 BIOLOGY, NEW YORK STRUCTURAL GENOMICS RESEARCH CONSORTIUM,
KEYWDS 3 TRANSFERASE
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 3 06-DEC-23 4KBE 1 REMARK
REVDAT 2 20-SEP-23 4KBE 1 REMARK SEQADV LINK
REVDAT 1 22-MAY-13 4KBE 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 PROBABLE SUGAR KINASE PROTEIN FROM
JRNL TITL 2 RHIZOBIUM ETLI CFN 42 COMPLEXED WITH BENZOGUANAMINE
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 41.22
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 60558
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) : 0.159
REMARK 3 R VALUE (WORKING SET) : 0.157
REMARK 3 FREE R VALUE : 0.215
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 3235
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) : 1.80
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.85
REMARK 3 REFLECTION IN BIN (WORKING SET) : 4375
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.42
REMARK 3 BIN R VALUE (WORKING SET) : 0.1290
REMARK 3 BIN FREE R VALUE SET COUNT : 247
REMARK 3 BIN FREE R VALUE : 0.1900
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5008
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 92
REMARK 3 SOLVENT ATOMS : 555
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 31.47
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.89000
REMARK 3 B22 (A**2) : 0.66000
REMARK 3 B33 (A**2) : -1.56000
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): 0.050
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.026
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.061
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.108
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.975
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.953
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 5305 ; 0.009 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 7203 ; 1.273 ; 1.990
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 700 ; 5.569 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 249 ;37.566 ;23.976
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 817 ;13.647 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 45 ;13.868 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 808 ; 0.084 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4089 ; 0.005 ; 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): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
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): 5305 ; 2.531 ; 3.000
REMARK 3 SPHERICITY; FREE ATOMS (A**2): 170 ;61.712 ; 5.000
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): 5594 ;21.016 ; 5.000
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 -1 A 328
REMARK 3 RESIDUE RANGE : A 401 A 405
REMARK 3 ORIGIN FOR THE GROUP (A): 13.7932 -7.4843 -20.5270
REMARK 3 T TENSOR
REMARK 3 T11: 0.0867 T22: 0.0687
REMARK 3 T33: 0.0023 T12: -0.0013
REMARK 3 T13: -0.0072 T23: 0.0066
REMARK 3 L TENSOR
REMARK 3 L11: 0.4769 L22: 0.2970
REMARK 3 L33: 0.1356 L12: 0.0427
REMARK 3 L13: -0.0111 L23: -0.0599
REMARK 3 S TENSOR
REMARK 3 S11: 0.0076 S12: -0.0078 S13: -0.0070
REMARK 3 S21: 0.0124 S22: 0.0005 S23: 0.0135
REMARK 3 S31: -0.0011 S32: 0.0050 S33: -0.0081
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 -1 B 328
REMARK 3 RESIDUE RANGE : B 401 B 405
REMARK 3 ORIGIN FOR THE GROUP (A): 26.7800 28.9313 -20.3111
REMARK 3 T TENSOR
REMARK 3 T11: 0.0778 T22: 0.0727
REMARK 3 T33: 0.0018 T12: -0.0001
REMARK 3 T13: 0.0094 T23: -0.0012
REMARK 3 L TENSOR
REMARK 3 L11: 0.4704 L22: 0.4386
REMARK 3 L33: 0.1618 L12: 0.0777
REMARK 3 L13: 0.0477 L23: 0.1117
REMARK 3 S TENSOR
REMARK 3 S11: 0.0076 S12: -0.0487 S13: 0.0150
REMARK 3 S21: 0.0091 S22: -0.0042 S23: -0.0007
REMARK 3 S31: 0.0074 S32: -0.0095 S33: -0.0034
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: HYDROGENS HAVE BEEN USED IF PRESENT IN
REMARK 3 THE INPUT
REMARK 4
REMARK 4 4KBE COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 10-MAY-13.
REMARK 100 THE DEPOSITION ID IS D_1000079126.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 28-MAR-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X29A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : NULL
REMARK 200 WAVELENGTH OR RANGE (A) : 1.075
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 63980
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.800
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 : 5.900
REMARK 200 R MERGE (I) : 0.08900
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 7.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.83
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : 5.90
REMARK 200 R MERGE FOR SHELL (I) : 0.59100
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: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 4E3A
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 43.90
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.19
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M AMMONIUM ACETATE, 0.1M
REMARK 280 BIS:TRIS:HCL, PH 6.5, 25% PEG3350, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 40.53600
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 46.25650
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 45.42800
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 46.25650
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 40.53600
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 45.42800
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 5010 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 24700 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 15.0 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 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 -23
REMARK 465 HIS A -22
REMARK 465 HIS A -21
REMARK 465 HIS A -20
REMARK 465 HIS A -19
REMARK 465 HIS A -18
REMARK 465 HIS A -17
REMARK 465 SER A -16
REMARK 465 SER A -15
REMARK 465 GLY A -14
REMARK 465 VAL A -13
REMARK 465 ASP A -12
REMARK 465 LEU A -11
REMARK 465 GLY A -10
REMARK 465 THR A -9
REMARK 465 GLU A -8
REMARK 465 ASN A -7
REMARK 465 LEU A -6
REMARK 465 TYR A -5
REMARK 465 PHE A -4
REMARK 465 GLN A -3
REMARK 465 SER A -2
REMARK 465 MSE B -23
REMARK 465 HIS B -22
REMARK 465 HIS B -21
REMARK 465 HIS B -20
REMARK 465 HIS B -19
REMARK 465 HIS B -18
REMARK 465 HIS B -17
REMARK 465 SER B -16
REMARK 465 SER B -15
REMARK 465 GLY B -14
REMARK 465 VAL B -13
REMARK 465 ASP B -12
REMARK 465 LEU B -11
REMARK 465 GLY B -10
REMARK 465 THR B -9
REMARK 465 GLU B -8
REMARK 465 ASN B -7
REMARK 465 LEU B -6
REMARK 465 TYR B -5
REMARK 465 PHE B -4
REMARK 465 GLN B -3
REMARK 465 SER B -2
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 O HOH A 633 O HOH A 668 1.94
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 SER A 186 -50.27 71.99
REMARK 500 ASP A 187 140.32 -175.00
REMARK 500 SER A 245 -121.66 48.18
REMARK 500 ASP A 270 115.91 -160.82
REMARK 500 SER B 186 -56.08 69.43
REMARK 500 MSE B 244 36.52 -141.28
REMARK 500 SER B 245 -124.04 56.93
REMARK 500 GLU B 267 136.43 -177.48
REMARK 500 ASP B 270 115.31 -166.64
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K A 406 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 270 O
REMARK 620 2 ASP A 270 OD2 81.7
REMARK 620 3 THR A 272 O 92.9 101.6
REMARK 620 4 VAL A 306 O 85.7 152.4 103.5
REMARK 620 5 GLN A 309 O 85.2 79.1 177.9 75.5
REMARK 620 6 GLY A 311 O 172.7 91.7 91.5 98.9 90.5
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K B 406 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 270 O
REMARK 620 2 ASP B 270 OD2 79.8
REMARK 620 3 THR B 272 O 89.0 99.8
REMARK 620 4 VAL B 306 O 84.3 150.5 104.6
REMARK 620 5 GLN B 309 O 85.7 79.9 174.7 74.3
REMARK 620 6 GLY B 311 O 173.7 94.7 89.1 101.9 96.2
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADN A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BZE A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS A 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS A 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS A 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K A 406
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADN B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BZE B 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS B 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS B 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS B 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K B 406
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4E3A RELATED DB: PDB
REMARK 900 RELATED ID: NYSGRC-014306 RELATED DB: TARGETTRACK
REMARK 900 RELATED ID: 4KAD RELATED DB: PDB
REMARK 900 RELATED ID: 4KAH RELATED DB: PDB
REMARK 900 RELATED ID: 4KAL RELATED DB: PDB
REMARK 900 RELATED ID: 4KAN RELATED DB: PDB
DBREF 4KBE A -1 328 UNP Q2KDX6 Q2KDX6_RHIEC 1 330
DBREF 4KBE B -1 328 UNP Q2KDX6 Q2KDX6_RHIEC 1 330
SEQADV 4KBE MSE A -23 UNP Q2KDX6 EXPRESSION TAG
SEQADV 4KBE HIS A -22 UNP Q2KDX6 EXPRESSION TAG
SEQADV 4KBE HIS A -21 UNP Q2KDX6 EXPRESSION TAG
SEQADV 4KBE HIS A -20 UNP Q2KDX6 EXPRESSION TAG
SEQADV 4KBE HIS A -19 UNP Q2KDX6 EXPRESSION TAG
SEQADV 4KBE HIS A -18 UNP Q2KDX6 EXPRESSION TAG
SEQADV 4KBE HIS A -17 UNP Q2KDX6 EXPRESSION TAG
SEQADV 4KBE SER A -16 UNP Q2KDX6 EXPRESSION TAG
SEQADV 4KBE SER A -15 UNP Q2KDX6 EXPRESSION TAG
SEQADV 4KBE GLY A -14 UNP Q2KDX6 EXPRESSION TAG
SEQADV 4KBE VAL A -13 UNP Q2KDX6 EXPRESSION TAG
SEQADV 4KBE ASP A -12 UNP Q2KDX6 EXPRESSION TAG
SEQADV 4KBE LEU A -11 UNP Q2KDX6 EXPRESSION TAG
SEQADV 4KBE GLY A -10 UNP Q2KDX6 EXPRESSION TAG
SEQADV 4KBE THR A -9 UNP Q2KDX6 EXPRESSION TAG
SEQADV 4KBE GLU A -8 UNP Q2KDX6 EXPRESSION TAG
SEQADV 4KBE ASN A -7 UNP Q2KDX6 EXPRESSION TAG
SEQADV 4KBE LEU A -6 UNP Q2KDX6 EXPRESSION TAG
SEQADV 4KBE TYR A -5 UNP Q2KDX6 EXPRESSION TAG
SEQADV 4KBE PHE A -4 UNP Q2KDX6 EXPRESSION TAG
SEQADV 4KBE GLN A -3 UNP Q2KDX6 EXPRESSION TAG
SEQADV 4KBE SER A -2 UNP Q2KDX6 EXPRESSION TAG
SEQADV 4KBE MSE B -23 UNP Q2KDX6 EXPRESSION TAG
SEQADV 4KBE HIS B -22 UNP Q2KDX6 EXPRESSION TAG
SEQADV 4KBE HIS B -21 UNP Q2KDX6 EXPRESSION TAG
SEQADV 4KBE HIS B -20 UNP Q2KDX6 EXPRESSION TAG
SEQADV 4KBE HIS B -19 UNP Q2KDX6 EXPRESSION TAG
SEQADV 4KBE HIS B -18 UNP Q2KDX6 EXPRESSION TAG
SEQADV 4KBE HIS B -17 UNP Q2KDX6 EXPRESSION TAG
SEQADV 4KBE SER B -16 UNP Q2KDX6 EXPRESSION TAG
SEQADV 4KBE SER B -15 UNP Q2KDX6 EXPRESSION TAG
SEQADV 4KBE GLY B -14 UNP Q2KDX6 EXPRESSION TAG
SEQADV 4KBE VAL B -13 UNP Q2KDX6 EXPRESSION TAG
SEQADV 4KBE ASP B -12 UNP Q2KDX6 EXPRESSION TAG
SEQADV 4KBE LEU B -11 UNP Q2KDX6 EXPRESSION TAG
SEQADV 4KBE GLY B -10 UNP Q2KDX6 EXPRESSION TAG
SEQADV 4KBE THR B -9 UNP Q2KDX6 EXPRESSION TAG
SEQADV 4KBE GLU B -8 UNP Q2KDX6 EXPRESSION TAG
SEQADV 4KBE ASN B -7 UNP Q2KDX6 EXPRESSION TAG
SEQADV 4KBE LEU B -6 UNP Q2KDX6 EXPRESSION TAG
SEQADV 4KBE TYR B -5 UNP Q2KDX6 EXPRESSION TAG
SEQADV 4KBE PHE B -4 UNP Q2KDX6 EXPRESSION TAG
SEQADV 4KBE GLN B -3 UNP Q2KDX6 EXPRESSION TAG
SEQADV 4KBE SER B -2 UNP Q2KDX6 EXPRESSION TAG
SEQRES 1 A 352 MSE HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU
SEQRES 2 A 352 GLY THR GLU ASN LEU TYR PHE GLN SER MSE THR ARG PHE
SEQRES 3 A 352 ASP VAL LEU THR VAL GLY ASN ALA ILE VAL ASP ILE ILE
SEQRES 4 A 352 SER ARG CYS ASN ASP GLN PHE LEU ILE ASP ASN GLN ILE
SEQRES 5 A 352 THR LYS ALA ALA MSE ASN LEU ILE ASP ALA GLU ARG ALA
SEQRES 6 A 352 GLU LEU LEU TYR SER ARG MSE GLY PRO ALA LEU GLU ALA
SEQRES 7 A 352 SER GLY GLY SER ALA GLY ASN THR ALA ALA GLY VAL ALA
SEQRES 8 A 352 ASN LEU GLY GLY LYS ALA ALA TYR PHE GLY ASN VAL ALA
SEQRES 9 A 352 ALA ASP GLN LEU GLY ASP ILE PHE THR HIS ASP ILE ARG
SEQRES 10 A 352 ALA GLN GLY VAL HIS TYR GLN THR LYS PRO LYS GLY ALA
SEQRES 11 A 352 PHE PRO PRO THR ALA ARG SER MSE ILE PHE VAL THR GLU
SEQRES 12 A 352 ASP GLY GLU ARG SER MSE ASN THR TYR LEU GLY ALA CYS
SEQRES 13 A 352 VAL GLU LEU GLY PRO GLU ASP VAL GLU ALA ASP VAL VAL
SEQRES 14 A 352 ALA ASP ALA LYS VAL THR TYR PHE GLU GLY TYR LEU TRP
SEQRES 15 A 352 ASP PRO PRO ARG ALA LYS GLU ALA ILE LEU ASP CYS ALA
SEQRES 16 A 352 ARG ILE ALA HIS GLN HIS GLY ARG GLU MSE SER MSE THR
SEQRES 17 A 352 LEU SER ASP SER PHE CYS VAL ASP ARG TYR ARG GLY GLU
SEQRES 18 A 352 PHE LEU ASP LEU MSE ARG SER GLY LYS VAL ASP ILE VAL
SEQRES 19 A 352 PHE ALA ASN ARG GLN GLU ALA LEU SER LEU TYR GLN THR
SEQRES 20 A 352 ASP ASP PHE GLU GLU ALA LEU ASN ARG ILE ALA ALA ASP
SEQRES 21 A 352 CYS LYS ILE ALA ALA VAL THR MSE SER GLU ASN GLY ALA
SEQRES 22 A 352 VAL ILE LEU LYS GLY ARG GLU ARG TYR TYR VAL ASN ALA
SEQRES 23 A 352 ILE ARG ILE ARG GLU VAL VAL ASP THR THR GLY ALA GLY
SEQRES 24 A 352 ASP LEU PHE ALA SER GLY PHE LEU TYR GLY TYR THR GLN
SEQRES 25 A 352 GLY ARG SER LEU GLU ASP CYS GLY LYS LEU GLY CYS LEU
SEQRES 26 A 352 ALA ALA GLY ILE VAL ILE GLN GLN ILE GLY PRO ARG PRO
SEQRES 27 A 352 MSE THR SER LEU SER GLU ALA ALA LYS GLN ALA GLY LEU
SEQRES 28 A 352 ILE
SEQRES 1 B 352 MSE HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU
SEQRES 2 B 352 GLY THR GLU ASN LEU TYR PHE GLN SER MSE THR ARG PHE
SEQRES 3 B 352 ASP VAL LEU THR VAL GLY ASN ALA ILE VAL ASP ILE ILE
SEQRES 4 B 352 SER ARG CYS ASN ASP GLN PHE LEU ILE ASP ASN GLN ILE
SEQRES 5 B 352 THR LYS ALA ALA MSE ASN LEU ILE ASP ALA GLU ARG ALA
SEQRES 6 B 352 GLU LEU LEU TYR SER ARG MSE GLY PRO ALA LEU GLU ALA
SEQRES 7 B 352 SER GLY GLY SER ALA GLY ASN THR ALA ALA GLY VAL ALA
SEQRES 8 B 352 ASN LEU GLY GLY LYS ALA ALA TYR PHE GLY ASN VAL ALA
SEQRES 9 B 352 ALA ASP GLN LEU GLY ASP ILE PHE THR HIS ASP ILE ARG
SEQRES 10 B 352 ALA GLN GLY VAL HIS TYR GLN THR LYS PRO LYS GLY ALA
SEQRES 11 B 352 PHE PRO PRO THR ALA ARG SER MSE ILE PHE VAL THR GLU
SEQRES 12 B 352 ASP GLY GLU ARG SER MSE ASN THR TYR LEU GLY ALA CYS
SEQRES 13 B 352 VAL GLU LEU GLY PRO GLU ASP VAL GLU ALA ASP VAL VAL
SEQRES 14 B 352 ALA ASP ALA LYS VAL THR TYR PHE GLU GLY TYR LEU TRP
SEQRES 15 B 352 ASP PRO PRO ARG ALA LYS GLU ALA ILE LEU ASP CYS ALA
SEQRES 16 B 352 ARG ILE ALA HIS GLN HIS GLY ARG GLU MSE SER MSE THR
SEQRES 17 B 352 LEU SER ASP SER PHE CYS VAL ASP ARG TYR ARG GLY GLU
SEQRES 18 B 352 PHE LEU ASP LEU MSE ARG SER GLY LYS VAL ASP ILE VAL
SEQRES 19 B 352 PHE ALA ASN ARG GLN GLU ALA LEU SER LEU TYR GLN THR
SEQRES 20 B 352 ASP ASP PHE GLU GLU ALA LEU ASN ARG ILE ALA ALA ASP
SEQRES 21 B 352 CYS LYS ILE ALA ALA VAL THR MSE SER GLU ASN GLY ALA
SEQRES 22 B 352 VAL ILE LEU LYS GLY ARG GLU ARG TYR TYR VAL ASN ALA
SEQRES 23 B 352 ILE ARG ILE ARG GLU VAL VAL ASP THR THR GLY ALA GLY
SEQRES 24 B 352 ASP LEU PHE ALA SER GLY PHE LEU TYR GLY TYR THR GLN
SEQRES 25 B 352 GLY ARG SER LEU GLU ASP CYS GLY LYS LEU GLY CYS LEU
SEQRES 26 B 352 ALA ALA GLY ILE VAL ILE GLN GLN ILE GLY PRO ARG PRO
SEQRES 27 B 352 MSE THR SER LEU SER GLU ALA ALA LYS GLN ALA GLY LEU
SEQRES 28 B 352 ILE
MODRES 4KBE MSE A -1 MET SELENOMETHIONINE
MODRES 4KBE MSE A 33 MET SELENOMETHIONINE
MODRES 4KBE MSE A 48 MET SELENOMETHIONINE
MODRES 4KBE MSE A 114 MET SELENOMETHIONINE
MODRES 4KBE MSE A 125 MET SELENOMETHIONINE
MODRES 4KBE MSE A 181 MET SELENOMETHIONINE
MODRES 4KBE MSE A 183 MET SELENOMETHIONINE
MODRES 4KBE MSE A 202 MET SELENOMETHIONINE
MODRES 4KBE MSE A 244 MET SELENOMETHIONINE
MODRES 4KBE MSE A 315 MET SELENOMETHIONINE
MODRES 4KBE MSE B -1 MET SELENOMETHIONINE
MODRES 4KBE MSE B 33 MET SELENOMETHIONINE
MODRES 4KBE MSE B 48 MET SELENOMETHIONINE
MODRES 4KBE MSE B 114 MET SELENOMETHIONINE
MODRES 4KBE MSE B 125 MET SELENOMETHIONINE
MODRES 4KBE MSE B 181 MET SELENOMETHIONINE
MODRES 4KBE MSE B 183 MET SELENOMETHIONINE
MODRES 4KBE MSE B 202 MET SELENOMETHIONINE
MODRES 4KBE MSE B 244 MET SELENOMETHIONINE
MODRES 4KBE MSE B 315 MET SELENOMETHIONINE
HET MSE A -1 8
HET MSE A 33 8
HET MSE A 48 8
HET MSE A 114 8
HET MSE A 125 8
HET MSE A 181 8
HET MSE A 183 8
HET MSE A 202 8
HET MSE A 244 8
HET MSE A 315 8
HET MSE B -1 8
HET MSE B 33 8
HET MSE B 48 8
HET MSE B 114 8
HET MSE B 125 8
HET MSE B 181 8
HET MSE B 183 8
HET MSE B 202 8
HET MSE B 244 8
HET MSE B 315 8
HET ADN A 401 19
HET BZE A 402 14
HET DMS A 403 4
HET DMS A 404 4
HET DMS A 405 4
HET K A 406 1
HET ADN B 401 19
HET BZE B 402 14
HET DMS B 403 4
HET DMS B 404 4
HET DMS B 405 4
HET K B 406 1
HETNAM MSE SELENOMETHIONINE
HETNAM ADN ADENOSINE
HETNAM BZE 6-PHENYL-1,3,5-TRIAZINE-2,4-DIAMINE
HETNAM DMS DIMETHYL SULFOXIDE
HETNAM K POTASSIUM ION
HETSYN BZE BENZOGUANAMINE
FORMUL 1 MSE 20(C5 H11 N O2 SE)
FORMUL 3 ADN 2(C10 H13 N5 O4)
FORMUL 4 BZE 2(C9 H9 N5)
FORMUL 5 DMS 6(C2 H6 O S)
FORMUL 8 K 2(K 1+)
FORMUL 15 HOH *555(H2 O)
HELIX 1 1 ASN A 19 ASN A 26 1 8
HELIX 2 2 ASP A 37 MSE A 48 1 12
HELIX 3 3 GLY A 57 GLY A 70 1 14
HELIX 4 4 ASP A 82 GLN A 95 1 14
HELIX 5 5 LEU A 129 LEU A 135 5 7
HELIX 6 6 GLY A 136 VAL A 140 5 5
HELIX 7 7 GLU A 141 ASP A 147 1 7
HELIX 8 8 TYR A 156 ASP A 159 5 4
HELIX 9 9 ARG A 162 HIS A 177 1 16
HELIX 10 10 ASP A 187 SER A 204 1 18
HELIX 11 11 ARG A 214 TYR A 221 1 8
HELIX 12 12 ASP A 225 CYS A 237 1 13
HELIX 13 13 SER A 245 ASN A 247 5 3
HELIX 14 14 GLY A 273 GLN A 288 1 16
HELIX 15 15 SER A 291 ILE A 307 1 17
HELIX 16 16 SER A 317 ALA A 325 1 9
HELIX 17 17 ASN B 19 ASN B 26 1 8
HELIX 18 18 ASP B 37 MSE B 48 1 12
HELIX 19 19 GLY B 57 GLY B 70 1 14
HELIX 20 20 ASP B 82 GLN B 95 1 14
HELIX 21 21 LEU B 129 LEU B 135 5 7
HELIX 22 22 GLY B 136 VAL B 140 5 5
HELIX 23 23 GLU B 141 ASP B 147 1 7
HELIX 24 24 TYR B 156 ASP B 159 5 4
HELIX 25 25 ARG B 162 HIS B 177 1 16
HELIX 26 26 ASP B 187 SER B 204 1 18
HELIX 27 27 ARG B 214 GLN B 222 1 9
HELIX 28 28 ASP B 225 CYS B 237 1 13
HELIX 29 29 SER B 245 ASN B 247 5 3
HELIX 30 30 GLY B 273 GLN B 288 1 16
HELIX 31 31 SER B 291 ILE B 307 1 17
HELIX 32 32 SER B 317 ALA B 325 1 9
SHEET 1 A 9 HIS A 98 TYR A 99 0
SHEET 2 A 9 ALA A 73 PHE A 76 1 N ALA A 73 O HIS A 98
SHEET 3 A 9 PHE A 2 VAL A 7 1 N THR A 6 O ALA A 74
SHEET 4 A 9 ALA A 148 GLU A 154 1 O TYR A 152 N LEU A 5
SHEET 5 A 9 GLU A 180 THR A 184 1 O SER A 182 N THR A 151
SHEET 6 A 9 ILE A 209 ASN A 213 1 O PHE A 211 N MSE A 183
SHEET 7 A 9 ILE A 239 THR A 243 1 O ALA A 241 N VAL A 210
SHEET 8 A 9 ALA A 249 LYS A 253 -1 O LEU A 252 N ALA A 240
SHEET 9 A 9 GLU A 256 VAL A 260 -1 O VAL A 260 N ALA A 249
SHEET 1 B 5 MSE A 33 LEU A 35 0
SHEET 2 B 5 ARG A 123 TYR A 128 1 O MSE A 125 N ASN A 34
SHEET 3 B 5 ALA A 111 VAL A 117 -1 N MSE A 114 O ASN A 126
SHEET 4 B 5 ILE A 11 ARG A 17 1 N ILE A 14 O ILE A 115
SHEET 5 B 5 LEU A 52 SER A 55 -1 O ALA A 54 N ASP A 13
SHEET 1 C 9 HIS B 98 TYR B 99 0
SHEET 2 C 9 ALA B 73 PHE B 76 1 N TYR B 75 O HIS B 98
SHEET 3 C 9 PHE B 2 VAL B 7 1 N THR B 6 O ALA B 74
SHEET 4 C 9 ALA B 148 GLU B 154 1 O TYR B 152 N LEU B 5
SHEET 5 C 9 GLU B 180 THR B 184 1 O SER B 182 N THR B 151
SHEET 6 C 9 ILE B 209 ASN B 213 1 O PHE B 211 N MSE B 183
SHEET 7 C 9 ILE B 239 THR B 243 1 O ALA B 241 N VAL B 210
SHEET 8 C 9 ALA B 249 LYS B 253 -1 O LEU B 252 N ALA B 240
SHEET 9 C 9 GLU B 256 VAL B 260 -1 O TYR B 258 N ILE B 251
SHEET 1 D 5 MSE B 33 LEU B 35 0
SHEET 2 D 5 ARG B 123 TYR B 128 1 O MSE B 125 N ASN B 34
SHEET 3 D 5 ALA B 111 VAL B 117 -1 N MSE B 114 O ASN B 126
SHEET 4 D 5 ILE B 11 ARG B 17 1 N ILE B 14 O ILE B 115
SHEET 5 D 5 LEU B 52 SER B 55 -1 O LEU B 52 N ILE B 15
LINK C MSE A -1 N THR A 0 1555 1555 1.33
LINK C ALA A 32 N MSE A 33 1555 1555 1.33
LINK C MSE A 33 N ASN A 34 1555 1555 1.33
LINK C ARG A 47 N MSE A 48 1555 1555 1.32
LINK C MSE A 48 N GLY A 49 1555 1555 1.33
LINK C SER A 113 N MSE A 114 1555 1555 1.33
LINK C MSE A 114 N ILE A 115 1555 1555 1.32
LINK C SER A 124 N MSE A 125 1555 1555 1.33
LINK C MSE A 125 N ASN A 126 1555 1555 1.34
LINK C GLU A 180 N MSE A 181 1555 1555 1.33
LINK C MSE A 181 N SER A 182 1555 1555 1.33
LINK C SER A 182 N MSE A 183 1555 1555 1.33
LINK C MSE A 183 N THR A 184 1555 1555 1.32
LINK C LEU A 201 N MSE A 202 1555 1555 1.33
LINK C MSE A 202 N ARG A 203 1555 1555 1.33
LINK C THR A 243 N MSE A 244 1555 1555 1.33
LINK C MSE A 244 N SER A 245 1555 1555 1.33
LINK C PRO A 314 N MSE A 315 1555 1555 1.33
LINK C MSE A 315 N THR A 316 1555 1555 1.33
LINK C MSE B -1 N THR B 0 1555 1555 1.33
LINK C ALA B 32 N MSE B 33 1555 1555 1.33
LINK C MSE B 33 N ASN B 34 1555 1555 1.34
LINK C ARG B 47 N MSE B 48 1555 1555 1.33
LINK C MSE B 48 N GLY B 49 1555 1555 1.32
LINK C SER B 113 N MSE B 114 1555 1555 1.33
LINK C MSE B 114 N ILE B 115 1555 1555 1.32
LINK C SER B 124 N MSE B 125 1555 1555 1.33
LINK C MSE B 125 N ASN B 126 1555 1555 1.33
LINK C GLU B 180 N MSE B 181 1555 1555 1.33
LINK C MSE B 181 N SER B 182 1555 1555 1.32
LINK C SER B 182 N MSE B 183 1555 1555 1.33
LINK C MSE B 183 N THR B 184 1555 1555 1.33
LINK C LEU B 201 N MSE B 202 1555 1555 1.33
LINK C MSE B 202 N ARG B 203 1555 1555 1.33
LINK C THR B 243 N MSE B 244 1555 1555 1.33
LINK C MSE B 244 N SER B 245 1555 1555 1.34
LINK C PRO B 314 N MSE B 315 1555 1555 1.33
LINK C MSE B 315 N THR B 316 1555 1555 1.33
LINK O ASP A 270 K K A 406 1555 1555 2.80
LINK OD2 ASP A 270 K K A 406 1555 1555 3.49
LINK O THR A 272 K K A 406 1555 1555 2.80
LINK O VAL A 306 K K A 406 1555 1555 2.69
LINK O GLN A 309 K K A 406 1555 1555 2.80
LINK O GLY A 311 K K A 406 1555 1555 2.75
LINK O ASP B 270 K K B 406 1555 1555 2.82
LINK OD2 ASP B 270 K K B 406 1555 1555 3.43
LINK O THR B 272 K K B 406 1555 1555 2.96
LINK O VAL B 306 K K B 406 1555 1555 2.78
LINK O GLN B 309 K K B 406 1555 1555 2.75
LINK O GLY B 311 K K B 406 1555 1555 2.69
CISPEP 1 PHE A 107 PRO A 108 0 0.48
CISPEP 2 PHE B 107 PRO B 108 0 -4.32
SITE 1 AC1 18 ASN A 9 ILE A 11 ASP A 13 MSE A 33
SITE 2 AC1 18 GLY A 56 GLY A 57 SER A 58 ASN A 61
SITE 3 AC1 18 MSE A 125 THR A 127 GLU A 154 TYR A 156
SITE 4 AC1 18 GLY A 273 ASP A 276 PRO A 312 HOH A 504
SITE 5 AC1 18 HOH A 514 HOH A 539
SITE 1 AC2 10 ILE A 15 SER A 16 ARG A 17 PRO A 50
SITE 2 AC2 10 LEU A 52 HOH A 608 HOH A 677 GLN B 95
SITE 3 AC2 10 PRO B 314 MSE B 315
SITE 1 AC3 5 ILE A 14 ALA A 41 TYR A 45 ARG A 112
SITE 2 AC3 5 DMS A 404
SITE 1 AC4 3 ALA A 38 ARG A 112 DMS A 403
SITE 1 AC5 8 GLN A 309 ILE A 310 GLY A 311 PRO A 312
SITE 2 AC5 8 ARG A 313 MSE A 315 HOH A 521 HOH B 604
SITE 1 AC6 5 ASP A 270 THR A 272 VAL A 306 GLN A 309
SITE 2 AC6 5 GLY A 311
SITE 1 AC7 18 ASN B 9 ILE B 11 ASP B 13 MSE B 33
SITE 2 AC7 18 GLY B 56 GLY B 57 SER B 58 ASN B 61
SITE 3 AC7 18 MSE B 125 THR B 127 GLU B 154 TYR B 156
SITE 4 AC7 18 GLY B 273 ASP B 276 PRO B 312 HOH B 510
SITE 5 AC7 18 HOH B 524 HOH B 542
SITE 1 AC8 10 GLN A 95 PRO A 314 MSE A 315 ILE B 15
SITE 2 AC8 10 SER B 16 ARG B 17 PRO B 50 LEU B 52
SITE 3 AC8 10 HOH B 604 HOH B 771
SITE 1 AC9 4 GLU B 42 ARG B 112 DMS B 404 HOH B 685
SITE 1 BC1 5 ILE B 14 ALA B 41 TYR B 45 ARG B 112
SITE 2 BC1 5 DMS B 403
SITE 1 BC2 8 HOH A 608 GLN B 309 ILE B 310 GLY B 311
SITE 2 BC2 8 PRO B 312 ARG B 313 MSE B 315 HOH B 525
SITE 1 BC3 5 ASP B 270 THR B 272 VAL B 306 GLN B 309
SITE 2 BC3 5 GLY B 311
CRYST1 81.072 90.856 92.513 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 0.012335 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011006 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010809 0.00000
HETATM 1 N MSE A -1 35.126 -24.691 -21.252 1.00 52.01 N
ANISOU 1 N MSE A -1 5703 7103 6954 1087 -76 -3 N
HETATM 2 CA MSE A -1 34.975 -23.203 -21.239 1.00 59.86 C
ANISOU 2 CA MSE A -1 7302 7439 8000 1522 -778 511 C
HETATM 3 C MSE A -1 34.309 -22.754 -22.512 1.00 56.71 C
ANISOU 3 C MSE A -1 7193 6570 7782 1273 -53 1331 C
HETATM 4 O MSE A -1 34.642 -23.220 -23.607 1.00 54.08 O
ANISOU 4 O MSE A -1 7182 6044 7322 829 -178 1657 O
HETATM 5 CB MSE A -1 36.304 -22.466 -21.033 1.00 68.83 C
ANISOU 5 CB MSE A -1 7858 9255 9038 601 -321 308 C
HETATM 6 CG MSE A -1 37.472 -23.041 -21.830 1.00 76.35 C
ANISOU 6 CG MSE A -1 9463 10803 8741 1422 870 1107 C
HETATM 7 SE MSE A -1 38.933 -21.721 -21.948 1.00 79.27 SE
ANISOU 7 SE MSE A -1 9707 13232 7179 1150 2033 2528 SE
HETATM 8 CE MSE A -1 39.647 -22.316 -23.683 1.00 68.98 C
ANISOU 8 CE MSE A -1 8889 7260 10060 3224 5282 5088 C
(ATOM LINES ARE NOT SHOWN.)
END