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HEADER HYDROLASE 23-APR-07 2UZ0
TITLE THE CRYSTAL CRYSTAL STRUCTURE OF THE ESTA PROTEIN, A
TITLE 2 VIRULENCE FACTOR ESTA PROTEIN FROM STREPTOCOCCUS PNEUMONIA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TRIBUTYRIN ESTERASE;
COMPND 3 SYNONYM: ESTERASE;
COMPND 4 CHAIN: A, B, C, D;
COMPND 5 FRAGMENT: RESIDUES 2-259;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 3 EXPRESSION_SYSTEM_STRAIN: B834;
SOURCE 4 ORGANISM_SCIENTIFIC: STREPTOCOCCUS PNEUMONIAE;
SOURCE 5 ATCC: BAA-255D
KEYWDS ESTERASE, ALPHA/BETA HYDROLASE, HYDROLASE,
KEYWDS 2 A VIRULENCE FACTOR FOR LUNG INFECTION
EXPDTA X-RAY DIFFRACTION
AUTHOR M.H.KIM,B.S.KANG,K.J.KIM,T.K.OH
REVDAT 1 23-OCT-07 2UZ0 0
JRNL AUTH M.H.KIM,B.S.KANG,S.KIM,K.J.KIM,C.H.LEE,B.C.OH,
JRNL AUTH 2 S.C.PARK,T.K.OH
JRNL TITL THE CRYSTAL STRUCTURE OF THE ESTA PROTEIN, A
JRNL TITL 2 VIRULENCE FACTOR FROM STREPTOCOCCUS PNEUMONIAE.
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.7 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
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) : 1.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NONE
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.65
REMARK 3 NUMBER OF REFLECTIONS : 107413
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) : 0.18421
REMARK 3 R VALUE (WORKING SET) : 0.18270
REMARK 3 FREE R VALUE : 0.21274
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.0
REMARK 3 FREE R VALUE TEST SET COUNT : 5662
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) : 1.702
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.746
REMARK 3 REFLECTION IN BIN (WORKING SET) : 7607
REMARK 3 BIN R VALUE (WORKING SET) : 0.232
REMARK 3 BIN FREE R VALUE SET COUNT : 378
REMARK 3 BIN FREE R VALUE : 0.271
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 7884
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 318
REMARK 3 SOLVENT ATOMS : 563
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 20.251
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.28
REMARK 3 B22 (A**2) : -0.42
REMARK 3 B33 (A**2) : 0.78
REMARK 3 B12 (A**2) : 0.00
REMARK 3 B13 (A**2) : 0.55
REMARK 3 B23 (A**2) : 0.00
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.110
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.105
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.067
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.949
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.957
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 (A): 8401 ; 0.011 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED (DEGREES): 11390 ; 1.307 ; 1.943
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1006 ; 6.113 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 391 ;31.784 ;23.990
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1364 ;14.103 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 32 ;20.207 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1188 ; 0.091 ; 0.200
REMARK 3 GENERAL PLANES REFINED (A): 6405 ; 0.005 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED (A): 4269 ; 0.318 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED (A): 5664 ; 0.328 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED (A): 602 ; 0.104 ; 0.200
REMARK 3 SYMMETRY VDW REFINED (A): 36 ; 0.167 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED (A): 16 ; 0.161 ; 0.200
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED (A**2): 5118 ; 1.110 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE REFINED (A**2): 7981 ; 1.111 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED (A**2): 3924 ; 2.083 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED (A**2): 3401 ; 2.896 ; 4.500
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 4
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 -4 A 257
REMARK 3 ORIGIN FOR THE GROUP (A): 31.5520 0.1450 44.6390
REMARK 3 T TENSOR
REMARK 3 T11: -0.0580 T22: -0.0526
REMARK 3 T33: 0.0248 T12: 0.0033
REMARK 3 T13: 0.0117 T23: 0.0058
REMARK 3 L TENSOR
REMARK 3 L11: 0.7928 L22: 0.4305
REMARK 3 L33: 0.3158 L12: -0.0324
REMARK 3 L13: 0.0329 L23: 0.0270
REMARK 3 S TENSOR
REMARK 3 S11: -0.0024 S12: 0.0039 S13: -0.0461
REMARK 3 S21: 0.0004 S22: -0.0003 S23: -0.0407
REMARK 3 S31: 0.0237 S32: 0.0013 S33: 0.0027
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 -4 B 257
REMARK 3 ORIGIN FOR THE GROUP (A): -2.6970 5.7370 40.2130
REMARK 3 T TENSOR
REMARK 3 T11: -0.0651 T22: -0.0448
REMARK 3 T33: 0.0310 T12: -0.0027
REMARK 3 T13: 0.0068 T23: 0.0008
REMARK 3 L TENSOR
REMARK 3 L11: 0.8877 L22: 0.2579
REMARK 3 L33: 0.3666 L12: 0.0903
REMARK 3 L13: -0.1923 L23: -0.0265
REMARK 3 S TENSOR
REMARK 3 S11: -0.0014 S12: 0.0612 S13: -0.0660
REMARK 3 S21: -0.0013 S22: -0.0085 S23: 0.0459
REMARK 3 S31: -0.0127 S32: 0.0002 S33: 0.0100
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C -4 C 253
REMARK 3 ORIGIN FOR THE GROUP (A): 26.7910 20.5190 14.0280
REMARK 3 T TENSOR
REMARK 3 T11: -0.0287 T22: 0.0000
REMARK 3 T33: -0.0519 T12: 0.0025
REMARK 3 T13: 0.0230 T23: 0.0202
REMARK 3 L TENSOR
REMARK 3 L11: 0.6578 L22: 0.5797
REMARK 3 L33: 0.8875 L12: 0.1670
REMARK 3 L13: -0.0453 L23: 0.0481
REMARK 3 S TENSOR
REMARK 3 S11: 0.0023 S12: 0.1182 S13: 0.0170
REMARK 3 S21: -0.1141 S22: -0.0051 S23: -0.0079
REMARK 3 S31: -0.0754 S32: 0.0513 S33: 0.0028
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D -4 D 257
REMARK 3 ORIGIN FOR THE GROUP (A): 10.6200 -10.3970 10.3370
REMARK 3 T TENSOR
REMARK 3 T11: -0.0493 T22: 0.0017
REMARK 3 T33: 0.0302 T12: -0.0040
REMARK 3 T13: -0.0181 T23: -0.1199
REMARK 3 L TENSOR
REMARK 3 L11: 1.1255 L22: 0.5264
REMARK 3 L33: 1.0113 L12: 0.0132
REMARK 3 L13: 0.0740 L23: 0.0340
REMARK 3 S TENSOR
REMARK 3 S11: 0.0349 S12: 0.2256 S13: -0.2615
REMARK 3 S21: -0.1059 S22: -0.0519 S23: 0.0940
REMARK 3 S31: 0.1423 S32: -0.0605 S33: 0.0170
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 ADDED IN THE
REMARK 3 RIDING POSITIONS.
REMARK 4
REMARK 4 2UZ0 COMPLIES WITH FORMAT V. 3.1, 01-AUG-2007
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY EBI ON 23-APR-2007.
REMARK 100 THE EBI ID CODE IS EBI-32331.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 08-JUL-2005
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PAL/PLS BEAMLINE 4A
REMARK 200 BEAMLINE : 4A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0000
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL2000
REMARK 200 DATA SCALING SOFTWARE : HKL2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 113097
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.70
REMARK 200 RESOLUTION RANGE LOW (A) : 40.00
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.0
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 3.8
REMARK 200 R MERGE (I) : 0.08
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 15.70
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.76
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.1
REMARK 200 DATA REDUNDANCY IN SHELL : 3.6
REMARK 200 R MERGE FOR SHELL (I) : 0.45
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.40
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: STARTING MODEL FOR MR WAS A PARTIALLY REFINED MODEL
REMARK 200 OF THE SEMET CRYSTAL AT A 1.9A.
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 42
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.12
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 10% (V/V) PEG 6000,8% (V/V)
REMARK 280 ETHYLENE GLYCOL,4% (V/V) 2-METHYL-2,4-PENTANEDIOL,10 MM
REMARK 280 CYSTEINE,0.1 M TRIS-HCL PH 7.0
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 36.06400
REMARK 290 SMTRY3 2 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 PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK ALSO PROVIDES INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 GENERATING THE BIOMOLECULE
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PQS
REMARK 350 AVERAGE BURIED SURFACE AREA: 3232.4 ANGSTROM**2
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D
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 ALA A 25
REMARK 465 ASN A 26
REMARK 465 ARG A 27
REMARK 465 VAL A 28
REMARK 465 GLU A 29
REMARK 465 GLU A 30
REMARK 465 PRO A 31
REMARK 465 GLU A 32
REMARK 465 CYS A 33
REMARK 465 THR A 258
REMARK 465 ALA B 25
REMARK 465 ASN B 26
REMARK 465 ARG B 27
REMARK 465 VAL B 28
REMARK 465 GLU B 29
REMARK 465 GLU B 30
REMARK 465 PRO B 31
REMARK 465 GLU B 32
REMARK 465 CYS B 33
REMARK 465 GLU B 34
REMARK 465 THR B 258
REMARK 465 ALA C 25
REMARK 465 ASN C 26
REMARK 465 ARG C 27
REMARK 465 VAL C 28
REMARK 465 GLU C 29
REMARK 465 GLU C 30
REMARK 465 PRO C 31
REMARK 465 GLU C 32
REMARK 465 CYS C 33
REMARK 465 GLU C 254
REMARK 465 GLU C 255
REMARK 465 ARG C 256
REMARK 465 LEU C 257
REMARK 465 THR C 258
REMARK 465 ALA D 25
REMARK 465 ASN D 26
REMARK 465 ARG D 27
REMARK 465 VAL D 28
REMARK 465 GLU D 29
REMARK 465 GLU D 30
REMARK 465 PRO D 31
REMARK 465 GLU D 32
REMARK 465 CYS D 33
REMARK 465 PHE D 151
REMARK 465 SER D 152
REMARK 465 PRO D 153
REMARK 465 GLU D 154
REMARK 465 SER D 155
REMARK 465 GLN D 156
REMARK 465 ASN D 157
REMARK 465 LEU D 158
REMARK 465 THR D 258
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 VAL A 18 CG1 CG2
REMARK 470 VAL B 18 CG1 CG2
REMARK 470 ARG B 172 CG CD NE CZ NH1 NH2
REMARK 470 VAL C 18 CG1 CG2
REMARK 470 VAL D 18 CG1 CG2
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER;
REMARK 480 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 480 I=INSERTION CODE):
REMARK 480 M RES CSSEQI ATOMS
REMARK 480 LYS A 252 CD CE NZ
REMARK 480 LYS B 252 CG CD CE NZ
REMARK 480 GLU B 255 CG CD OE1 OE2
REMARK 480 LYS C 101 CD CE NZ
REMARK 480 ARG C 172 CG CD NE CZ NH1 NH2
REMARK 480 LYS C 191 CE NZ
REMARK 480 ARG D 172 CB CG CD NE CZ NH1 NH2
REMARK 480 LYS D 193 CD CE NZ
REMARK 480 ASP D 250 CG OD1 OD2
REMARK 480 LYS D 252 CG CD CE NZ
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCELIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 LYS A 252 CB - CG - CD ANGL. DEV. = 19.0 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 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 MSE A -2 -13.16 77.74
REMARK 500 SER A 46 -9.61 77.84
REMARK 500 SER A 120 -114.38 50.76
REMARK 500 MSE B -2 -12.34 80.29
REMARK 500 SER B 46 -4.29 78.40
REMARK 500 SER B 120 -114.56 50.66
REMARK 500 MSE C -2 -13.44 82.30
REMARK 500 SER C 46 -7.11 78.18
REMARK 500 ASN C 57 34.32 -92.56
REMARK 500 SER C 120 -119.15 52.16
REMARK 500 MSE D -2 -11.27 78.05
REMARK 500 SER D 46 -8.41 77.21
REMARK 500 ASN D 57 34.60 -88.67
REMARK 500 SER D 120 -116.79 58.81
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 LYS C 252 LEU C 253 0 140.63
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 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 CA A1258 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 LEU C 53 O
REMARK 620 2 HOH A2039 O 82.6
REMARK 620 3 HOH A2043 O 94.1 88.0
REMARK 620 4 HOH C2038 O 91.5 168.4 82.5
REMARK 620 5 HOH C2043 O 86.3 96.6 175.4 92.9
REMARK 620 6 LEU A 53 O 162.3 79.7 85.8 106.0 95.3
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B1258 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 LEU D 53 O
REMARK 620 2 LEU B 53 O 163.0
REMARK 620 3 HOH B2038 O 83.0 80.0
REMARK 620 4 HOH B2040 O 95.9 84.8 93.4
REMARK 620 5 HOH B2035 O 98.9 98.0 177.5 84.8
REMARK 620 6 HOH D2036 O 87.1 94.4 94.0 172.3 87.7
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 SITE_DESCRIPTION: CA BINDING SITE FOR CHAIN A
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 SITE_DESCRIPTION: CA BINDING SITE FOR CHAIN B
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 SITE_DESCRIPTION: GOL BINDING SITE FOR CHAIN A
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 SITE_DESCRIPTION: GOL BINDING SITE FOR CHAIN A
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 SITE_DESCRIPTION: GOL BINDING SITE FOR CHAIN C
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 SITE_DESCRIPTION: GOL BINDING SITE FOR CHAIN D
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 SITE_DESCRIPTION: GOL BINDING SITE FOR CHAIN C
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 SITE_DESCRIPTION: GOL BINDING SITE FOR CHAIN D
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 SITE_DESCRIPTION: EDO BINDING SITE FOR CHAIN C
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 SITE_DESCRIPTION: EDO BINDING SITE FOR CHAIN A
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 SITE_DESCRIPTION: EDO BINDING SITE FOR CHAIN C
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 SITE_DESCRIPTION: EDO BINDING SITE FOR CHAIN B
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2CFN RELATED DB: PDB
REMARK 900 THE CRYSTAL STRUCTURE OF A VIRULENCE FACTOR
REMARK 900 ESTA FROM STREPTOCOCCUS PNEUMONIAE
DBREF 2UZ0 A -4 0 PDB 2UZ0 2UZ0 -4 0
DBREF 2UZ0 A 1 258 UNP Q97S09 Q97S09_STRPN 2 259
DBREF 2UZ0 B -4 0 PDB 2UZ0 2UZ0 -4 0
DBREF 2UZ0 B 1 258 UNP Q97S09 Q97S09_STRPN 2 259
DBREF 2UZ0 C -4 0 PDB 2UZ0 2UZ0 -4 0
DBREF 2UZ0 C 1 258 UNP Q97S09 Q97S09_STRPN 2 259
DBREF 2UZ0 D -4 0 PDB 2UZ0 2UZ0 -4 0
DBREF 2UZ0 D 1 258 UNP Q97S09 Q97S09_STRPN 2 259
SEQRES 1 A 263 GLY ALA MSE ASP PRO ALA VAL MSE LYS ILE GLU TYR TYR
SEQRES 2 A 263 SER GLN VAL LEU ASP MSE GLU TRP GLY VAL ASN VAL LEU
SEQRES 3 A 263 TYR PRO ASP ALA ASN ARG VAL GLU GLU PRO GLU CYS GLU
SEQRES 4 A 263 ASP ILE PRO VAL LEU TYR LEU LEU HIS GLY MSE SER GLY
SEQRES 5 A 263 ASN HIS ASN SER TRP LEU LYS ARG THR ASN VAL GLU ARG
SEQRES 6 A 263 LEU LEU ARG GLY THR ASN LEU ILE VAL VAL MSE PRO ASN
SEQRES 7 A 263 THR SER ASN GLY TRP TYR THR ASP THR GLN TYR GLY PHE
SEQRES 8 A 263 ASP TYR TYR THR ALA LEU ALA GLU GLU LEU PRO GLN VAL
SEQRES 9 A 263 LEU LYS ARG PHE PHE PRO ASN MSE THR SER LYS ARG GLU
SEQRES 10 A 263 LYS THR PHE ILE ALA GLY LEU SER MSE GLY GLY TYR GLY
SEQRES 11 A 263 CYS PHE LYS LEU ALA LEU THR THR ASN ARG PHE SER HIS
SEQRES 12 A 263 ALA ALA SER PHE SER GLY ALA LEU SER PHE GLN ASN PHE
SEQRES 13 A 263 SER PRO GLU SER GLN ASN LEU GLY SER PRO ALA TYR TRP
SEQRES 14 A 263 ARG GLY VAL PHE GLY GLU ILE ARG ASP TRP THR THR SER
SEQRES 15 A 263 PRO TYR SER LEU GLU SER LEU ALA LYS LYS SER ASP LYS
SEQRES 16 A 263 LYS THR LYS LEU TRP ALA TRP CYS GLY GLU GLN ASP PHE
SEQRES 17 A 263 LEU TYR GLU ALA ASN ASN LEU ALA VAL LYS ASN LEU LYS
SEQRES 18 A 263 LYS LEU GLY PHE ASP VAL THR TYR SER HIS SER ALA GLY
SEQRES 19 A 263 THR HIS GLU TRP TYR TYR TRP GLU LYS GLN LEU GLU VAL
SEQRES 20 A 263 PHE LEU THR THR LEU PRO ILE ASP PHE LYS LEU GLU GLU
SEQRES 21 A 263 ARG LEU THR
SEQRES 1 B 263 GLY ALA MSE ASP PRO ALA VAL MSE LYS ILE GLU TYR TYR
SEQRES 2 B 263 SER GLN VAL LEU ASP MSE GLU TRP GLY VAL ASN VAL LEU
SEQRES 3 B 263 TYR PRO ASP ALA ASN ARG VAL GLU GLU PRO GLU CYS GLU
SEQRES 4 B 263 ASP ILE PRO VAL LEU TYR LEU LEU HIS GLY MSE SER GLY
SEQRES 5 B 263 ASN HIS ASN SER TRP LEU LYS ARG THR ASN VAL GLU ARG
SEQRES 6 B 263 LEU LEU ARG GLY THR ASN LEU ILE VAL VAL MSE PRO ASN
SEQRES 7 B 263 THR SER ASN GLY TRP TYR THR ASP THR GLN TYR GLY PHE
SEQRES 8 B 263 ASP TYR TYR THR ALA LEU ALA GLU GLU LEU PRO GLN VAL
SEQRES 9 B 263 LEU LYS ARG PHE PHE PRO ASN MSE THR SER LYS ARG GLU
SEQRES 10 B 263 LYS THR PHE ILE ALA GLY LEU SER MSE GLY GLY TYR GLY
SEQRES 11 B 263 CYS PHE LYS LEU ALA LEU THR THR ASN ARG PHE SER HIS
SEQRES 12 B 263 ALA ALA SER PHE SER GLY ALA LEU SER PHE GLN ASN PHE
SEQRES 13 B 263 SER PRO GLU SER GLN ASN LEU GLY SER PRO ALA TYR TRP
SEQRES 14 B 263 ARG GLY VAL PHE GLY GLU ILE ARG ASP TRP THR THR SER
SEQRES 15 B 263 PRO TYR SER LEU GLU SER LEU ALA LYS LYS SER ASP LYS
SEQRES 16 B 263 LYS THR LYS LEU TRP ALA TRP CYS GLY GLU GLN ASP PHE
SEQRES 17 B 263 LEU TYR GLU ALA ASN ASN LEU ALA VAL LYS ASN LEU LYS
SEQRES 18 B 263 LYS LEU GLY PHE ASP VAL THR TYR SER HIS SER ALA GLY
SEQRES 19 B 263 THR HIS GLU TRP TYR TYR TRP GLU LYS GLN LEU GLU VAL
SEQRES 20 B 263 PHE LEU THR THR LEU PRO ILE ASP PHE LYS LEU GLU GLU
SEQRES 21 B 263 ARG LEU THR
SEQRES 1 C 263 GLY ALA MSE ASP PRO ALA VAL MSE LYS ILE GLU TYR TYR
SEQRES 2 C 263 SER GLN VAL LEU ASP MSE GLU TRP GLY VAL ASN VAL LEU
SEQRES 3 C 263 TYR PRO ASP ALA ASN ARG VAL GLU GLU PRO GLU CYS GLU
SEQRES 4 C 263 ASP ILE PRO VAL LEU TYR LEU LEU HIS GLY MSE SER GLY
SEQRES 5 C 263 ASN HIS ASN SER TRP LEU LYS ARG THR ASN VAL GLU ARG
SEQRES 6 C 263 LEU LEU ARG GLY THR ASN LEU ILE VAL VAL MSE PRO ASN
SEQRES 7 C 263 THR SER ASN GLY TRP TYR THR ASP THR GLN TYR GLY PHE
SEQRES 8 C 263 ASP TYR TYR THR ALA LEU ALA GLU GLU LEU PRO GLN VAL
SEQRES 9 C 263 LEU LYS ARG PHE PHE PRO ASN MSE THR SER LYS ARG GLU
SEQRES 10 C 263 LYS THR PHE ILE ALA GLY LEU SER MSE GLY GLY TYR GLY
SEQRES 11 C 263 CYS PHE LYS LEU ALA LEU THR THR ASN ARG PHE SER HIS
SEQRES 12 C 263 ALA ALA SER PHE SER GLY ALA LEU SER PHE GLN ASN PHE
SEQRES 13 C 263 SER PRO GLU SER GLN ASN LEU GLY SER PRO ALA TYR TRP
SEQRES 14 C 263 ARG GLY VAL PHE GLY GLU ILE ARG ASP TRP THR THR SER
SEQRES 15 C 263 PRO TYR SER LEU GLU SER LEU ALA LYS LYS SER ASP LYS
SEQRES 16 C 263 LYS THR LYS LEU TRP ALA TRP CYS GLY GLU GLN ASP PHE
SEQRES 17 C 263 LEU TYR GLU ALA ASN ASN LEU ALA VAL LYS ASN LEU LYS
SEQRES 18 C 263 LYS LEU GLY PHE ASP VAL THR TYR SER HIS SER ALA GLY
SEQRES 19 C 263 THR HIS GLU TRP TYR TYR TRP GLU LYS GLN LEU GLU VAL
SEQRES 20 C 263 PHE LEU THR THR LEU PRO ILE ASP PHE LYS LEU GLU GLU
SEQRES 21 C 263 ARG LEU THR
SEQRES 1 D 263 GLY ALA MSE ASP PRO ALA VAL MSE LYS ILE GLU TYR TYR
SEQRES 2 D 263 SER GLN VAL LEU ASP MSE GLU TRP GLY VAL ASN VAL LEU
SEQRES 3 D 263 TYR PRO ASP ALA ASN ARG VAL GLU GLU PRO GLU CYS GLU
SEQRES 4 D 263 ASP ILE PRO VAL LEU TYR LEU LEU HIS GLY MSE SER GLY
SEQRES 5 D 263 ASN HIS ASN SER TRP LEU LYS ARG THR ASN VAL GLU ARG
SEQRES 6 D 263 LEU LEU ARG GLY THR ASN LEU ILE VAL VAL MSE PRO ASN
SEQRES 7 D 263 THR SER ASN GLY TRP TYR THR ASP THR GLN TYR GLY PHE
SEQRES 8 D 263 ASP TYR TYR THR ALA LEU ALA GLU GLU LEU PRO GLN VAL
SEQRES 9 D 263 LEU LYS ARG PHE PHE PRO ASN MSE THR SER LYS ARG GLU
SEQRES 10 D 263 LYS THR PHE ILE ALA GLY LEU SER MSE GLY GLY TYR GLY
SEQRES 11 D 263 CYS PHE LYS LEU ALA LEU THR THR ASN ARG PHE SER HIS
SEQRES 12 D 263 ALA ALA SER PHE SER GLY ALA LEU SER PHE GLN ASN PHE
SEQRES 13 D 263 SER PRO GLU SER GLN ASN LEU GLY SER PRO ALA TYR TRP
SEQRES 14 D 263 ARG GLY VAL PHE GLY GLU ILE ARG ASP TRP THR THR SER
SEQRES 15 D 263 PRO TYR SER LEU GLU SER LEU ALA LYS LYS SER ASP LYS
SEQRES 16 D 263 LYS THR LYS LEU TRP ALA TRP CYS GLY GLU GLN ASP PHE
SEQRES 17 D 263 LEU TYR GLU ALA ASN ASN LEU ALA VAL LYS ASN LEU LYS
SEQRES 18 D 263 LYS LEU GLY PHE ASP VAL THR TYR SER HIS SER ALA GLY
SEQRES 19 D 263 THR HIS GLU TRP TYR TYR TRP GLU LYS GLN LEU GLU VAL
SEQRES 20 D 263 PHE LEU THR THR LEU PRO ILE ASP PHE LYS LEU GLU GLU
SEQRES 21 D 263 ARG LEU THR
MODRES 2UZ0 MSE A -2 MET SELENOMETHIONINE
MODRES 2UZ0 MSE A 3 MET SELENOMETHIONINE
MODRES 2UZ0 MSE A 14 MET SELENOMETHIONINE
MODRES 2UZ0 MSE A 45 MET SELENOMETHIONINE
MODRES 2UZ0 MSE A 71 MET SELENOMETHIONINE
MODRES 2UZ0 MSE A 107 MET SELENOMETHIONINE
MODRES 2UZ0 MSE A 121 MET SELENOMETHIONINE
MODRES 2UZ0 MSE B -2 MET SELENOMETHIONINE
MODRES 2UZ0 MSE B 3 MET SELENOMETHIONINE
MODRES 2UZ0 MSE B 14 MET SELENOMETHIONINE
MODRES 2UZ0 MSE B 45 MET SELENOMETHIONINE
MODRES 2UZ0 MSE B 71 MET SELENOMETHIONINE
MODRES 2UZ0 MSE B 107 MET SELENOMETHIONINE
MODRES 2UZ0 MSE B 121 MET SELENOMETHIONINE
MODRES 2UZ0 MSE C -2 MET SELENOMETHIONINE
MODRES 2UZ0 MSE C 3 MET SELENOMETHIONINE
MODRES 2UZ0 MSE C 14 MET SELENOMETHIONINE
MODRES 2UZ0 MSE C 45 MET SELENOMETHIONINE
MODRES 2UZ0 MSE C 71 MET SELENOMETHIONINE
MODRES 2UZ0 MSE C 107 MET SELENOMETHIONINE
MODRES 2UZ0 MSE C 121 MET SELENOMETHIONINE
MODRES 2UZ0 MSE D -2 MET SELENOMETHIONINE
MODRES 2UZ0 MSE D 3 MET SELENOMETHIONINE
MODRES 2UZ0 MSE D 14 MET SELENOMETHIONINE
MODRES 2UZ0 MSE D 45 MET SELENOMETHIONINE
MODRES 2UZ0 MSE D 71 MET SELENOMETHIONINE
MODRES 2UZ0 MSE D 107 MET SELENOMETHIONINE
MODRES 2UZ0 MSE D 121 MET SELENOMETHIONINE
HET MSE A -2 8
HET MSE A 3 13
HET MSE A 14 13
HET MSE A 45 8
HET MSE A 71 8
HET MSE A 107 8
HET MSE A 121 8
HET MSE B -2 8
HET MSE B 3 13
HET MSE B 14 13
HET MSE B 45 8
HET MSE B 71 8
HET MSE B 107 8
HET MSE B 121 8
HET MSE C -2 8
HET MSE C 3 13
HET MSE C 14 13
HET MSE C 45 8
HET MSE C 71 8
HET MSE C 107 8
HET MSE C 121 8
HET MSE D -2 8
HET MSE D 3 13
HET MSE D 14 13
HET MSE D 45 8
HET MSE D 71 8
HET MSE D 107 8
HET MSE D 121 8
HET CA A1258 1
HET CA B1258 1
HET GOL A1259 6
HET GOL A1260 6
HET GOL C1254 6
HET GOL D1258 6
HET GOL C1255 6
HET GOL D1259 6
HET EDO C1256 4
HET EDO A1261 4
HET EDO C1257 4
HET EDO B1259 4
HETNAM EDO 1,2-ETHANEDIOL
HETSYN EDO ETHYLENE GLYCOL
HETNAM CA CALCIUM ION
HETNAM GOL GLYCEROL
HETNAM MSE SELENOMETHIONINE
FORMUL 5 EDO 4(C2 H6 O2)
FORMUL 6 CA 2(CA 2+)
FORMUL 7 GOL 6(C3 H8 O3)
FORMUL 8 MSE 28(C5 H11 N O2 SE)
FORMUL 9 HOH *563(H2 O1)
HELIX 1 1 ASN A 50 THR A 56 1 7
HELIX 2 2 ASN A 57 LEU A 62 1 6
HELIX 3 3 ASP A 87 GLU A 94 1 8
HELIX 4 4 GLU A 94 PHE A 104 1 11
HELIX 5 5 LYS A 110 GLU A 112 5 3
HELIX 6 6 SER A 120 ASN A 134 1 15
HELIX 7 7 SER A 152 GLN A 156 5 5
HELIX 8 8 SER A 160 GLY A 169 1 10
HELIX 9 9 SER A 180 ALA A 185 1 6
HELIX 10 10 LYS A 186 SER A 188 5 3
HELIX 11 11 LEU A 204 LEU A 218 1 15
HELIX 12 12 GLU A 232 LEU A 247 1 16
HELIX 13 13 ASN B 50 THR B 56 1 7
HELIX 14 14 ASN B 57 LEU B 62 1 6
HELIX 15 15 ASP B 87 GLU B 94 1 8
HELIX 16 16 GLU B 94 PHE B 104 1 11
HELIX 17 17 LYS B 110 GLU B 112 5 3
HELIX 18 18 SER B 120 ASN B 134 1 15
HELIX 19 19 SER B 152 ASN B 157 5 6
HELIX 20 20 SER B 160 GLY B 169 1 10
HELIX 21 21 SER B 180 ALA B 185 1 6
HELIX 22 22 LYS B 186 SER B 188 5 3
HELIX 23 23 LEU B 204 LEU B 218 1 15
HELIX 24 24 GLU B 232 THR B 245 1 14
HELIX 25 25 ASN C 50 THR C 56 1 7
HELIX 26 26 ASN C 57 LEU C 62 1 6
HELIX 27 27 ASP C 87 GLU C 94 1 8
HELIX 28 28 GLU C 94 PHE C 104 1 11
HELIX 29 29 LYS C 110 GLU C 112 5 3
HELIX 30 30 SER C 120 ASN C 134 1 15
HELIX 31 31 SER C 152 ASN C 157 5 6
HELIX 32 32 SER C 160 GLY C 169 1 10
HELIX 33 33 SER C 180 ALA C 185 1 6
HELIX 34 34 LYS C 186 SER C 188 5 3
HELIX 35 35 LEU C 204 LEU C 218 1 15
HELIX 36 36 GLU C 232 THR C 246 1 15
HELIX 37 37 ASN D 50 THR D 56 1 7
HELIX 38 38 ASN D 57 LEU D 62 1 6
HELIX 39 39 ASP D 87 GLU D 94 1 8
HELIX 40 40 GLU D 94 PHE D 104 1 11
HELIX 41 41 LYS D 110 GLU D 112 5 3
HELIX 42 42 SER D 120 ASN D 134 1 15
HELIX 43 43 SER D 160 GLY D 169 1 10
HELIX 44 44 SER D 180 ALA D 185 1 6
HELIX 45 45 LYS D 186 SER D 188 5 3
HELIX 46 46 LEU D 204 LEU D 218 1 15
HELIX 47 47 GLU D 232 THR D 245 1 14
SHEET 1 AA16 ASP A 221 SER A 227 0
SHEET 2 AA16 LYS A 193 GLY A 199 1 O LEU A 194 N THR A 223
SHEET 3 AA16 HIS A 138 PHE A 142 1 O ALA A 139 N TRP A 195
SHEET 4 AA16 THR A 114 LEU A 119 1 O ILE A 116 N ALA A 140
SHEET 5 AA16 VAL A 38 LEU A 42 1 O VAL A 38 N PHE A 115
SHEET 6 AA16 ILE A 68 MSE A 71 1 O ILE A 68 N LEU A 39
SHEET 7 AA16 MSE A 14 TYR A 22 -1 O ASN A 19 N MSE A 71
SHEET 8 AA16 ALA A 1 SER A 9 -1 O ALA A 1 N TYR A 22
SHEET 9 AA16 ALA D 1 SER D 9 -1 O VAL D 2 N GLU A 6
SHEET 10 AA16 MSE D 14 TYR D 22 -1 O MSE D 14 N SER D 9
SHEET 11 AA16 ILE D 68 MSE D 71 -1 O VAL D 69 N LEU D 21
SHEET 12 AA16 VAL D 38 LEU D 42 1 O LEU D 39 N VAL D 70
SHEET 13 AA16 THR D 114 LEU D 119 1 O PHE D 115 N TYR D 40
SHEET 14 AA16 HIS D 138 PHE D 142 1 O HIS D 138 N ILE D 116
SHEET 15 AA16 LYS D 193 GLY D 199 1 O LYS D 193 N ALA D 139
SHEET 16 AA16 VAL D 222 SER D 227 1 O THR D 223 N ALA D 196
SHEET 1 BA16 VAL B 222 SER B 227 0
SHEET 2 BA16 LYS B 193 GLY B 199 1 O LEU B 194 N THR B 223
SHEET 3 BA16 HIS B 138 PHE B 142 1 O ALA B 139 N TRP B 195
SHEET 4 BA16 THR B 114 LEU B 119 1 O ILE B 116 N ALA B 140
SHEET 5 BA16 VAL B 38 LEU B 42 1 O VAL B 38 N PHE B 115
SHEET 6 BA16 ILE B 68 MSE B 71 1 O ILE B 68 N LEU B 39
SHEET 7 BA16 MSE B 14 TYR B 22 -1 O ASN B 19 N MSE B 71
SHEET 8 BA16 ALA B 1 SER B 9 -1 O ALA B 1 N TYR B 22
SHEET 9 BA16 ALA C 1 SER C 9 -1 O VAL C 2 N GLU B 6
SHEET 10 BA16 MSE C 14 TYR C 22 -1 O MSE C 14 N SER C 9
SHEET 11 BA16 ILE C 68 MSE C 71 -1 O VAL C 69 N LEU C 21
SHEET 12 BA16 VAL C 38 LEU C 42 1 O LEU C 39 N VAL C 70
SHEET 13 BA16 THR C 114 LEU C 119 1 O PHE C 115 N TYR C 40
SHEET 14 BA16 HIS C 138 PHE C 142 1 O HIS C 138 N ILE C 116
SHEET 15 BA16 LYS C 193 GLY C 199 1 O LYS C 193 N ALA C 139
SHEET 16 BA16 VAL C 222 SER C 227 1 O THR C 223 N ALA C 196
LINK C ALA A -3 N MSE A -2 1555 1555 1.33
LINK C MSE A -2 N ASP A -1 1555 1555 1.33
LINK C VAL A 2 N MSE A 3 1555 1555 1.33
LINK C MSE A 3 N LYS A 4 1555 1555 1.33
LINK C ASP A 13 N MSE A 14 1555 1555 1.33
LINK C MSE A 14 N GLU A 15 1555 1555 1.33
LINK C GLY A 44 N MSE A 45 1555 1555 1.32
LINK C MSE A 45 N SER A 46 1555 1555 1.33
LINK C VAL A 70 N MSE A 71 1555 1555 1.33
LINK C MSE A 71 N PRO A 72 1555 1555 1.35
LINK C ASN A 106 N MSE A 107 1555 1555 1.33
LINK C MSE A 107 N THR A 108 1555 1555 1.33
LINK C SER A 120 N MSE A 121 1555 1555 1.34
LINK C MSE A 121 N GLY A 122 1555 1555 1.33
LINK CA CA A1258 O LEU C 53 1555 1555 2.32
LINK CA CA A1258 O HOH A2039 1555 1555 2.32
LINK CA CA A1258 O HOH C2043 1555 1555 2.33
LINK CA CA A1258 O LEU A 53 1555 1555 2.32
LINK CA CA A1258 O HOH A2043 1555 1555 2.39
LINK CA CA A1258 O HOH C2038 1555 1555 2.29
LINK C ALA B -3 N MSE B -2 1555 1555 1.33
LINK C MSE B -2 N ASP B -1 1555 1555 1.33
LINK C VAL B 2 N MSE B 3 1555 1555 1.34
LINK C MSE B 3 N LYS B 4 1555 1555 1.33
LINK C ASP B 13 N MSE B 14 1555 1555 1.33
LINK C MSE B 14 N GLU B 15 1555 1555 1.33
LINK C GLY B 44 N MSE B 45 1555 1555 1.33
LINK C MSE B 45 N SER B 46 1555 1555 1.34
LINK C VAL B 70 N MSE B 71 1555 1555 1.33
LINK C MSE B 71 N PRO B 72 1555 1555 1.35
LINK C ASN B 106 N MSE B 107 1555 1555 1.33
LINK C MSE B 107 N THR B 108 1555 1555 1.33
LINK C SER B 120 N MSE B 121 1555 1555 1.34
LINK C MSE B 121 N GLY B 122 1555 1555 1.33
LINK CA CA B1258 O HOH B2040 1555 1555 2.41
LINK CA CA B1258 O HOH B2038 1555 1555 2.33
LINK CA CA B1258 O LEU B 53 1555 1555 2.30
LINK CA CA B1258 O LEU D 53 1555 1555 2.30
LINK CA CA B1258 O HOH D2036 1555 1555 2.40
LINK CA CA B1258 O HOH B2035 1555 1555 2.34
LINK C MSE C -2 N ASP C -1 1555 1555 1.33
LINK C ALA C -3 N MSE C -2 1555 1555 1.33
LINK C VAL C 2 N MSE C 3 1555 1555 1.33
LINK C MSE C 3 N LYS C 4 1555 1555 1.33
LINK C ASP C 13 N MSE C 14 1555 1555 1.33
LINK C MSE C 14 N GLU C 15 1555 1555 1.33
LINK C GLY C 44 N MSE C 45 1555 1555 1.33
LINK C MSE C 45 N SER C 46 1555 1555 1.34
LINK C VAL C 70 N MSE C 71 1555 1555 1.33
LINK C MSE C 71 N PRO C 72 1555 1555 1.34
LINK C ASN C 106 N MSE C 107 1555 1555 1.33
LINK C MSE C 107 N THR C 108 1555 1555 1.33
LINK C SER C 120 N MSE C 121 1555 1555 1.34
LINK C MSE C 121 N GLY C 122 1555 1555 1.33
LINK C MSE D -2 N ASP D -1 1555 1555 1.33
LINK C ALA D -3 N MSE D -2 1555 1555 1.33
LINK C VAL D 2 N MSE D 3 1555 1555 1.32
LINK C MSE D 3 N LYS D 4 1555 1555 1.33
LINK C ASP D 13 N MSE D 14 1555 1555 1.33
LINK C MSE D 14 N GLU D 15 1555 1555 1.33
LINK C GLY D 44 N MSE D 45 1555 1555 1.33
LINK C MSE D 45 N SER D 46 1555 1555 1.34
LINK C VAL D 70 N MSE D 71 1555 1555 1.33
LINK C MSE D 71 N PRO D 72 1555 1555 1.34
LINK C ASN D 106 N MSE D 107 1555 1555 1.33
LINK C MSE D 107 N THR D 108 1555 1555 1.33
LINK C SER D 120 N MSE D 121 1555 1555 1.33
LINK C MSE D 121 N GLY D 122 1555 1555 1.33
SITE 1 AC1 6 LEU A 53 HOH A2039 HOH A2043 LEU C 53
SITE 2 AC1 6 HOH C2038 HOH C2043
SITE 1 AC2 6 LEU B 53 HOH B2035 HOH B2038 HOH B2040
SITE 2 AC2 6 LEU D 53 HOH D2036
SITE 1 AC3 6 GLY A 44 SER A 46 SER A 120 HIS A 231
SITE 2 AC3 6 TRP A 236 HOH A2027
SITE 1 AC4 9 LEU A 12 ASP A 13 GLY A 85 PHE A 86
SITE 2 AC4 9 HOH A2010 HOH A2153 ASN B 76 GLY B 159
SITE 3 AC4 9 TYR B 163
SITE 1 AC5 8 LEU C 12 GLY C 85 PHE C 86 HOH C2015
SITE 2 AC5 8 HOH C2063 ASN D 76 GLY D 159 TYR D 163
SITE 1 AC6 8 ASN C 76 GLY C 159 TYR C 163 LEU D 12
SITE 2 AC6 8 GLY D 85 PHE D 86 HOH D2016 HOH D2017
SITE 1 AC7 6 GLY C 44 LEU C 119 SER C 120 HIS C 231
SITE 2 AC7 6 HOH C2080 HOH C2139
SITE 1 AC8 6 GLY D 44 LEU D 119 SER D 120 HIS D 231
SITE 2 AC8 6 HOH D2063 HOH D2091
SITE 1 AC9 8 TRP C 16 ASN C 73 SER C 75 HOH C2019
SITE 2 AC9 8 HOH C2140 TRP D 16 ASN D 73 SER D 75
SITE 1 BC1 8 TRP A 16 ASN A 73 SER A 75 HOH A2154
SITE 2 BC1 8 TRP B 16 ASN B 73 SER B 75 HOH B2009
SITE 1 BC2 7 SER C 109 LYS C 110 ARG C 111 THR C 114
SITE 2 BC2 7 ARG C 135 HOH C2079 HOH C2141
SITE 1 BC3 5 ASN A 76 TYR A 163 LEU B 12 GLY B 85
SITE 2 BC3 5 PHE B 86
CRYST1 71.695 72.128 101.827 90.00 94.31 90.00 P 1 21 1 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 0.013948 0.000000 0.001051 0.00000
SCALE2 0.000000 0.013864 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009848 0.00000
TER 2067 LEU A 257
TER 4119 LEU B 257
TER 6149 LEU C 253
TER 8152 LEU D 257
MASTER 513 0 40 47 32 0 25 6 8765 4 385 84
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