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HEADER HYDROLASE 09-JUL-10 3NWO
TITLE CRYSTAL STRUCTURE OF PROLINE IMINOPEPTIDASE MYCOBACTERIUM SMEGMATIS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROLINE IMINOPEPTIDASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: PIP;
COMPND 5 EC: 3.4.11.5;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM SMEGMATIS;
SOURCE 3 ORGANISM_TAXID: 246196;
SOURCE 4 STRAIN: ATCC 700084 / MC(2)155;
SOURCE 5 GENE: MSMEG_2681;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: AVA0421
KEYWDS STRUCTURAL GENOMICS, SEATTLE STRUCTURAL GENOMICS CENTER FOR
KEYWDS 2 INFECTIOUS DISEASE, SSGCID, PROLINE IMINOPEPTIDASE, MYCOBACTERIUM
KEYWDS 3 SMEGMATIS, MYCOBACTERIUM, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR SEATTLE STRUCTURAL GENOMICS CENTER FOR INFECTIOUS DISEASE (SSGCID)
REVDAT 1 04-AUG-10 3NWO 0
JRNL AUTH T.L.ARAKAKI,A.GARDBERG,B.L.STAKER,J.ABENDROTH
JRNL TITL CRYSTAL STRUCTURE OF PROLINE IMINOPEPTIDASE MYCOBACTERIUM
JRNL TITL 2 SMEGMATIS
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0109
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) : 1.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 37.94
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 3 NUMBER OF REFLECTIONS : 21658
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) : 0.138
REMARK 3 R VALUE (WORKING SET) : 0.136
REMARK 3 FREE R VALUE : 0.173
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1104
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) : 1.90
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.95
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1478
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 97.55
REMARK 3 BIN R VALUE (WORKING SET) : 0.1990
REMARK 3 BIN FREE R VALUE SET COUNT : 75
REMARK 3 BIN FREE R VALUE : 0.2610
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2304
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 17
REMARK 3 SOLVENT ATOMS : 333
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 17.99
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 10.29
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.23000
REMARK 3 B22 (A**2) : -0.17000
REMARK 3 B33 (A**2) : -0.04000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.17000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.122
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.082
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.283
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.965
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.943
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2443 ; 0.015 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): 1598 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3353 ; 1.412 ; 1.928
REMARK 3 BOND ANGLES OTHERS (DEGREES): 3886 ; 0.957 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 312 ; 5.757 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 120 ;28.803 ;23.417
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 345 ;12.861 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 18 ;20.089 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 367 ; 0.089 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2789 ; 0.008 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 503 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 1518 ; 0.668 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 601 ; 0.208 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2463 ; 1.112 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 925 ; 1.904 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 883 ; 2.930 ; 4.500
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 5
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 8 A 32
REMARK 3 ORIGIN FOR THE GROUP (A): 13.9510 51.2930 29.5690
REMARK 3 T TENSOR
REMARK 3 T11: 0.0451 T22: 0.0059
REMARK 3 T33: 0.0193 T12: -0.0006
REMARK 3 T13: -0.0131 T23: -0.0006
REMARK 3 L TENSOR
REMARK 3 L11: 1.0983 L22: 2.8788
REMARK 3 L33: 1.2874 L12: 1.4229
REMARK 3 L13: 0.5960 L23: 1.7701
REMARK 3 S TENSOR
REMARK 3 S11: 0.0773 S12: -0.0478 S13: -0.0518
REMARK 3 S21: 0.1729 S22: -0.1038 S23: -0.0232
REMARK 3 S31: 0.1099 S32: -0.0744 S33: 0.0265
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 : A 33 A 145
REMARK 3 ORIGIN FOR THE GROUP (A): 10.8960 54.5640 17.8720
REMARK 3 T TENSOR
REMARK 3 T11: 0.0308 T22: 0.0268
REMARK 3 T33: 0.0227 T12: -0.0024
REMARK 3 T13: 0.0032 T23: 0.0006
REMARK 3 L TENSOR
REMARK 3 L11: 0.0217 L22: 0.1658
REMARK 3 L33: 0.0689 L12: 0.0185
REMARK 3 L13: -0.0128 L23: 0.0385
REMARK 3 S TENSOR
REMARK 3 S11: 0.0231 S12: 0.0072 S13: 0.0023
REMARK 3 S21: 0.0282 S22: -0.0081 S23: 0.0017
REMARK 3 S31: 0.0030 S32: -0.0220 S33: -0.0149
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 : A 146 A 198
REMARK 3 ORIGIN FOR THE GROUP (A): 27.6160 55.3670 -5.1960
REMARK 3 T TENSOR
REMARK 3 T11: 0.0417 T22: 0.0148
REMARK 3 T33: 0.0299 T12: 0.0010
REMARK 3 T13: 0.0217 T23: 0.0030
REMARK 3 L TENSOR
REMARK 3 L11: 0.3396 L22: 0.3376
REMARK 3 L33: 0.3692 L12: -0.2938
REMARK 3 L13: 0.1010 L23: -0.2294
REMARK 3 S TENSOR
REMARK 3 S11: 0.0110 S12: -0.0175 S13: -0.0150
REMARK 3 S21: -0.0386 S22: 0.0107 S23: -0.0022
REMARK 3 S31: -0.0051 S32: -0.0178 S33: -0.0217
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 : A 199 A 228
REMARK 3 ORIGIN FOR THE GROUP (A): 18.2610 45.9410 5.4100
REMARK 3 T TENSOR
REMARK 3 T11: 0.0396 T22: 0.0329
REMARK 3 T33: 0.0236 T12: 0.0092
REMARK 3 T13: 0.0266 T23: 0.0067
REMARK 3 L TENSOR
REMARK 3 L11: 3.0326 L22: 0.3780
REMARK 3 L33: 0.5053 L12: 0.3710
REMARK 3 L13: 1.0820 L23: -0.0665
REMARK 3 S TENSOR
REMARK 3 S11: -0.0624 S12: 0.1632 S13: 0.0638
REMARK 3 S21: -0.0862 S22: 0.0070 S23: -0.0467
REMARK 3 S31: 0.0269 S32: 0.0672 S33: 0.0555
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 229 A 306
REMARK 3 ORIGIN FOR THE GROUP (A): 13.7030 67.0840 12.2260
REMARK 3 T TENSOR
REMARK 3 T11: 0.0255 T22: 0.0059
REMARK 3 T33: 0.0174 T12: 0.0067
REMARK 3 T13: 0.0113 T23: -0.0005
REMARK 3 L TENSOR
REMARK 3 L11: 0.4398 L22: 0.1988
REMARK 3 L33: 0.5991 L12: -0.1061
REMARK 3 L13: -0.0448 L23: 0.1250
REMARK 3 S TENSOR
REMARK 3 S11: 0.0344 S12: 0.0032 S13: 0.0400
REMARK 3 S21: -0.0224 S22: -0.0196 S23: -0.0127
REMARK 3 S31: -0.0435 S32: -0.0167 S33: -0.0148
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS. U VALUES: WITH TLS ADDED
REMARK 4
REMARK 4 3NWO COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-JUL-10.
REMARK 100 THE RCSB ID CODE IS RCSB060372.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 14-MAY-10
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU MICROMAX-007 HF
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : NULL
REMARK 200 WAVELENGTH OR RANGE (A) : 1.54
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RIGAKU SATURN 944+
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 24228
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.800
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 94.8
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.11700
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 12.8700
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) : 1.85
REMARK 200 COMPLETENESS FOR SHELL (%) : 55.8
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.52700
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.200
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: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 40.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.10
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG 3350, 0.2 M SODIUM CITRATE,
REMARK 280 0.1 M TRIS PROPANE, PH 8.5, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
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 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 35.96500
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 34.96000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 35.96500
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 34.96000
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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 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 MET A -20
REMARK 465 ALA A -19
REMARK 465 HIS A -18
REMARK 465 HIS A -17
REMARK 465 HIS A -16
REMARK 465 HIS A -15
REMARK 465 HIS A -14
REMARK 465 HIS A -13
REMARK 465 MET A -12
REMARK 465 GLY A -11
REMARK 465 THR A -10
REMARK 465 LEU A -9
REMARK 465 GLU A -8
REMARK 465 ALA A -7
REMARK 465 ASN A -6
REMARK 465 THR A -5
REMARK 465 ASN A -4
REMARK 465 GLY A -3
REMARK 465 PRO A -2
REMARK 465 GLY A -1
REMARK 465 SER A 0
REMARK 465 MET A 1
REMARK 465 LEU A 2
REMARK 465 SER A 3
REMARK 465 ARG A 4
REMARK 465 MET A 5
REMARK 465 PRO A 6
REMARK 465 VAL A 7
REMARK 465 ALA A 307
REMARK 465 ARG A 308
REMARK 465 VAL A 309
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 ALA A 46 173.33 70.00
REMARK 500 SER A 113 -118.41 64.62
REMARK 500 SER A 279 -126.07 -136.40
REMARK 500 CYS A 281 58.90 -98.29
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 MG A 310 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A 547 O
REMARK 620 2 HOH A 520 O 96.0
REMARK 620 3 HOH A 511 O 172.1 83.8
REMARK 620 4 HOH A 583 O 91.3 172.1 89.4
REMARK 620 5 HOH A 500 O 86.8 92.6 85.4 90.8
REMARK 620 6 HOH A 515 O 94.7 89.7 93.2 86.8 177.2
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 MG A 310
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 311
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 312
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 313
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: MYSMA.00560.A RELATED DB: TARGETDB
DBREF 3NWO A 1 309 UNP A0QVS8 A0QVS8_MYCS2 1 309
SEQADV 3NWO MET A -20 UNP A0QVS8 EXPRESSION TAG
SEQADV 3NWO ALA A -19 UNP A0QVS8 EXPRESSION TAG
SEQADV 3NWO HIS A -18 UNP A0QVS8 EXPRESSION TAG
SEQADV 3NWO HIS A -17 UNP A0QVS8 EXPRESSION TAG
SEQADV 3NWO HIS A -16 UNP A0QVS8 EXPRESSION TAG
SEQADV 3NWO HIS A -15 UNP A0QVS8 EXPRESSION TAG
SEQADV 3NWO HIS A -14 UNP A0QVS8 EXPRESSION TAG
SEQADV 3NWO HIS A -13 UNP A0QVS8 EXPRESSION TAG
SEQADV 3NWO MET A -12 UNP A0QVS8 EXPRESSION TAG
SEQADV 3NWO GLY A -11 UNP A0QVS8 EXPRESSION TAG
SEQADV 3NWO THR A -10 UNP A0QVS8 EXPRESSION TAG
SEQADV 3NWO LEU A -9 UNP A0QVS8 EXPRESSION TAG
SEQADV 3NWO GLU A -8 UNP A0QVS8 EXPRESSION TAG
SEQADV 3NWO ALA A -7 UNP A0QVS8 EXPRESSION TAG
SEQADV 3NWO ASN A -6 UNP A0QVS8 EXPRESSION TAG
SEQADV 3NWO THR A -5 UNP A0QVS8 EXPRESSION TAG
SEQADV 3NWO ASN A -4 UNP A0QVS8 EXPRESSION TAG
SEQADV 3NWO GLY A -3 UNP A0QVS8 EXPRESSION TAG
SEQADV 3NWO PRO A -2 UNP A0QVS8 EXPRESSION TAG
SEQADV 3NWO GLY A -1 UNP A0QVS8 EXPRESSION TAG
SEQADV 3NWO SER A 0 UNP A0QVS8 EXPRESSION TAG
SEQRES 1 A 330 MET ALA HIS HIS HIS HIS HIS HIS MET GLY THR LEU GLU
SEQRES 2 A 330 ALA ASN THR ASN GLY PRO GLY SER MET LEU SER ARG MET
SEQRES 3 A 330 PRO VAL SER SER ARG THR VAL PRO PHE GLY ASP HIS GLU
SEQRES 4 A 330 THR TRP VAL GLN VAL THR THR PRO GLU ASN ALA GLN PRO
SEQRES 5 A 330 HIS ALA LEU PRO LEU ILE VAL LEU HIS GLY GLY PRO GLY
SEQRES 6 A 330 MET ALA HIS ASN TYR VAL ALA ASN ILE ALA ALA LEU ALA
SEQRES 7 A 330 ASP GLU THR GLY ARG THR VAL ILE HIS TYR ASP GLN VAL
SEQRES 8 A 330 GLY CYS GLY ASN SER THR HIS LEU PRO ASP ALA PRO ALA
SEQRES 9 A 330 ASP PHE TRP THR PRO GLN LEU PHE VAL ASP GLU PHE HIS
SEQRES 10 A 330 ALA VAL CYS THR ALA LEU GLY ILE GLU ARG TYR HIS VAL
SEQRES 11 A 330 LEU GLY GLN SER TRP GLY GLY MET LEU GLY ALA GLU ILE
SEQRES 12 A 330 ALA VAL ARG GLN PRO SER GLY LEU VAL SER LEU ALA ILE
SEQRES 13 A 330 CYS ASN SER PRO ALA SER MET ARG LEU TRP SER GLU ALA
SEQRES 14 A 330 ALA GLY ASP LEU ARG ALA GLN LEU PRO ALA GLU THR ARG
SEQRES 15 A 330 ALA ALA LEU ASP ARG HIS GLU ALA ALA GLY THR ILE THR
SEQRES 16 A 330 HIS PRO ASP TYR LEU GLN ALA ALA ALA GLU PHE TYR ARG
SEQRES 17 A 330 ARG HIS VAL CYS ARG VAL VAL PRO THR PRO GLN ASP PHE
SEQRES 18 A 330 ALA ASP SER VAL ALA GLN MET GLU ALA GLU PRO THR VAL
SEQRES 19 A 330 TYR HIS THR MET ASN GLY PRO ASN GLU PHE HIS VAL VAL
SEQRES 20 A 330 GLY THR LEU GLY ASP TRP SER VAL ILE ASP ARG LEU PRO
SEQRES 21 A 330 ASP VAL THR ALA PRO VAL LEU VAL ILE ALA GLY GLU HIS
SEQRES 22 A 330 ASP GLU ALA THR PRO LYS THR TRP GLN PRO PHE VAL ASP
SEQRES 23 A 330 HIS ILE PRO ASP VAL ARG SER HIS VAL PHE PRO GLY THR
SEQRES 24 A 330 SER HIS CYS THR HIS LEU GLU LYS PRO GLU GLU PHE ARG
SEQRES 25 A 330 ALA VAL VAL ALA GLN PHE LEU HIS GLN HIS ASP LEU ALA
SEQRES 26 A 330 ALA ASP ALA ARG VAL
HET MG A 310 1
HET GOL A 311 6
HET EDO A 312 4
HET GOL A 313 6
HETNAM MG MAGNESIUM ION
HETNAM GOL GLYCEROL
HETNAM EDO 1,2-ETHANEDIOL
HETSYN EDO ETHYLENE GLYCOL
FORMUL 2 MG MG 2+
FORMUL 3 GOL 2(C3 H8 O3)
FORMUL 4 EDO C2 H6 O2
FORMUL 6 HOH *333(H2 O)
HELIX 1 1 HIS A 47 ALA A 54 5 8
HELIX 2 2 ALA A 55 GLY A 61 1 7
HELIX 3 3 PRO A 82 TRP A 86 5 5
HELIX 4 4 THR A 87 GLY A 103 1 17
HELIX 5 5 SER A 113 ARG A 125 1 13
HELIX 6 6 SER A 141 LEU A 156 1 16
HELIX 7 7 PRO A 157 GLY A 171 1 15
HELIX 8 8 HIS A 175 VAL A 190 1 16
HELIX 9 9 PRO A 197 GLU A 210 1 14
HELIX 10 10 PRO A 211 ASN A 218 1 8
HELIX 11 11 GLY A 227 TRP A 232 5 6
HELIX 12 12 VAL A 234 VAL A 241 5 8
HELIX 13 13 THR A 256 ILE A 267 1 12
HELIX 14 14 CYS A 281 LYS A 286 1 6
HELIX 15 15 LYS A 286 ASP A 306 1 21
SHEET 1 A 8 SER A 9 PHE A 14 0
SHEET 2 A 8 HIS A 17 THR A 24 -1 O VAL A 21 N ARG A 10
SHEET 3 A 8 VAL A 64 TYR A 67 -1 O HIS A 66 N GLN A 22
SHEET 4 A 8 LEU A 36 LEU A 39 1 N LEU A 36 O ILE A 65
SHEET 5 A 8 TYR A 107 GLN A 112 1 O LEU A 110 N LEU A 39
SHEET 6 A 8 LEU A 130 CYS A 136 1 O VAL A 131 N TYR A 107
SHEET 7 A 8 VAL A 245 GLY A 250 1 O ILE A 248 N ILE A 135
SHEET 8 A 8 VAL A 270 PHE A 275 1 O ARG A 271 N VAL A 247
LINK MG MG A 310 O HOH A 547 1555 1555 2.04
LINK MG MG A 310 O HOH A 520 1555 1555 2.05
LINK MG MG A 310 O HOH A 511 1555 1555 2.10
LINK MG MG A 310 O HOH A 583 1555 1555 2.16
LINK MG MG A 310 O HOH A 500 1555 1555 2.20
LINK MG MG A 310 O HOH A 515 1555 1555 2.21
CISPEP 1 GLY A 42 PRO A 43 0 -9.94
CISPEP 2 VAL A 194 PRO A 195 0 1.60
SITE 1 AC1 6 HOH A 500 HOH A 511 HOH A 515 HOH A 520
SITE 2 AC1 6 HOH A 547 HOH A 583
SITE 1 AC2 7 GLY A 42 PRO A 43 SER A 113 TRP A 114
SITE 2 AC2 7 ASN A 218 LEU A 229 HOH A 602
SITE 1 AC3 4 MET A 45 TYR A 49 HIS A 280 HOH A 569
SITE 1 AC4 8 ASN A 28 GLN A 30 GLU A 59 THR A 76
SITE 2 AC4 8 HOH A 410 HOH A 419 HOH A 512 HOH A 531
CRYST1 71.930 69.920 55.630 90.00 93.18 90.00 C 1 2 1 4
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 0.013902 0.000000 0.000772 0.00000
SCALE2 0.000000 0.014302 0.000000 0.00000
SCALE3 0.000000 0.000000 0.018004 0.00000
TER 2353 ASP A 306
MASTER 415 0 4 15 8 0 7 6 2654 1 24 26
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