HEADER TRANSFERASE 19-AUG-12 4GO7
TITLE THE REGULATORY SUBUNIT OF ASPARTATE KINASE IN COMPLEX WITH THREONINE
TITLE 2 FROM MYCOBACTERIUM TUBERCULOSIS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ASPARTOKINASE;
COMPND 3 CHAIN: X;
COMPND 4 FRAGMENT: REGULATORY SUBUNIT (UNP RESIDUES 250-421);
COMPND 5 SYNONYM: ASPARTATE KINASE, ASK;
COMPND 6 EC: 2.7.2.4;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM TUBERCULOSIS;
SOURCE 3 ORGANISM_TAXID: 1773;
SOURCE 4 GENE: ASK, RV3709C, MT3812, MTV025.057C;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR Q.YANG,X.LI
REVDAT 3 28-FEB-24 4GO7 1 REMARK SEQADV
REVDAT 2 17-JUL-19 4GO7 1 REMARK
REVDAT 1 05-SEP-12 4GO7 0
JRNL AUTH Q.YANG,K.YU,L.YAN,Y.LI,C.CHEN,X.LI
JRNL TITL STRUCTURAL VIEW OF THE REGULATORY SUBUNIT OF ASPARTATE
JRNL TITL 2 KINASE FROM MYCOBACTERIUM TUBERCULOSIS.
JRNL REF PROTEIN CELL V. 2 745 2011
JRNL REFN ISSN 1674-800X
JRNL PMID 21976064
JRNL DOI 10.1007/S13238-011-1094-2
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0102
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) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 56.79
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 3 NUMBER OF REFLECTIONS : 16661
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) : 0.221
REMARK 3 R VALUE (WORKING SET) : 0.219
REMARK 3 FREE R VALUE : 0.264
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 887
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.05
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1204
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 97.89
REMARK 3 BIN R VALUE (WORKING SET) : 0.2990
REMARK 3 BIN FREE R VALUE SET COUNT : 50
REMARK 3 BIN FREE R VALUE : 0.4010
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1231
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 8
REMARK 3 SOLVENT ATOMS : 43
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 45.06
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.29000
REMARK 3 B22 (A**2) : 1.29000
REMARK 3 B33 (A**2) : -2.58000
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): 0.149
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.150
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.122
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.370
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.950
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.929
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1252 ; 0.026 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 1695 ; 2.074 ; 1.969
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 161 ; 6.863 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 50 ;37.956 ;24.600
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 210 ;17.634 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 7 ;23.125 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 210 ; 0.181 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 912 ; 0.013 ; 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): 819 ; 1.551 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1317 ; 2.543 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 433 ; 3.348 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 378 ; 5.369 ; 4.500
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 : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : 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
REMARK 4
REMARK 4 4GO7 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 24-AUG-12.
REMARK 100 THE DEPOSITION ID IS D_1000074430.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 12-JUN-11
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PHOTON FACTORY
REMARK 200 BEAMLINE : BL-17A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : NULL
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9800
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 : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 17555
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
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 (%) : NULL
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.03
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.7
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 60.38
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.10
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.8M AMMONIUM PHOSPHATE, PH 8.5, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 290K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 41
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 3555 -Y,X+1/2,Z+1/4
REMARK 290 4555 Y+1/2,-X,Z+3/4
REMARK 290 5555 X+1/2,Y+1/2,Z+1/2
REMARK 290 6555 -X,-Y,Z
REMARK 290 7555 -Y+1/2,X,Z+3/4
REMARK 290 8555 Y,-X+1/2,Z+1/4
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 31.18550
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 31.18550
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 68.64450
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 31.18550
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 34.32225
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 31.18550
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 102.96675
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 31.18550
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 31.18550
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 68.64450
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 7 0.000000 -1.000000 0.000000 31.18550
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 1.000000 102.96675
REMARK 290 SMTRY1 8 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 31.18550
REMARK 290 SMTRY3 8 0.000000 0.000000 1.000000 34.32225
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: 4170 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 13490 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -16.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: X
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 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 X -19
REMARK 465 GLY X -18
REMARK 465 HIS X -14
REMARK 465 HIS X -13
REMARK 465 HIS X -12
REMARK 465 HIS X -11
REMARK 465 HIS X -10
REMARK 465 SER X -9
REMARK 465 SER X -8
REMARK 465 GLY X -7
REMARK 465 LEU X -6
REMARK 465 VAL X -5
REMARK 465 PRO X -4
REMARK 465 ARG X -3
REMARK 465 GLY X -2
REMARK 465 ASN X -1
REMARK 465 HIS X 0
REMARK 465 VAL X 54
REMARK 465 GLU X 55
REMARK 465 GLY X 159
REMARK 465 GLY X 160
REMARK 465 ASP X 161
REMARK 465 GLU X 162
REMARK 465 GLY X 169
REMARK 465 THR X 170
REMARK 465 GLY X 171
REMARK 465 ARG X 172
REMARK 465 LEU X 173
REMARK 465 GLU X 174
REMARK 465 HIS X 175
REMARK 465 HIS X 176
REMARK 465 HIS X 177
REMARK 465 HIS X 178
REMARK 465 HIS X 179
REMARK 465 HIS X 180
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 OE1 GLU X 144 O HOH X 319 2.09
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 VAL X 51 CB VAL X 51 CG2 0.128
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ARG X 141 NE - CZ - NH2 ANGL. DEV. = -3.9 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 ASP X 45 -95.72 -96.27
REMARK 500 VAL X 51 140.20 -35.94
REMARK 500 SER X 107 29.57 47.21
REMARK 500 HIS X 108 62.87 -119.80
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE THR X 201
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4GO5 RELATED DB: PDB
DBREF 4GO7 X 1 172 UNP P0A4Z8 AK_MYCTU 250 421
SEQADV 4GO7 MET X -19 UNP P0A4Z8 EXPRESSION TAG
SEQADV 4GO7 GLY X -18 UNP P0A4Z8 EXPRESSION TAG
SEQADV 4GO7 SER X -17 UNP P0A4Z8 EXPRESSION TAG
SEQADV 4GO7 ILE X -16 UNP P0A4Z8 EXPRESSION TAG
SEQADV 4GO7 HIS X -15 UNP P0A4Z8 EXPRESSION TAG
SEQADV 4GO7 HIS X -14 UNP P0A4Z8 EXPRESSION TAG
SEQADV 4GO7 HIS X -13 UNP P0A4Z8 EXPRESSION TAG
SEQADV 4GO7 HIS X -12 UNP P0A4Z8 EXPRESSION TAG
SEQADV 4GO7 HIS X -11 UNP P0A4Z8 EXPRESSION TAG
SEQADV 4GO7 HIS X -10 UNP P0A4Z8 EXPRESSION TAG
SEQADV 4GO7 SER X -9 UNP P0A4Z8 EXPRESSION TAG
SEQADV 4GO7 SER X -8 UNP P0A4Z8 EXPRESSION TAG
SEQADV 4GO7 GLY X -7 UNP P0A4Z8 EXPRESSION TAG
SEQADV 4GO7 LEU X -6 UNP P0A4Z8 EXPRESSION TAG
SEQADV 4GO7 VAL X -5 UNP P0A4Z8 EXPRESSION TAG
SEQADV 4GO7 PRO X -4 UNP P0A4Z8 EXPRESSION TAG
SEQADV 4GO7 ARG X -3 UNP P0A4Z8 EXPRESSION TAG
SEQADV 4GO7 GLY X -2 UNP P0A4Z8 EXPRESSION TAG
SEQADV 4GO7 ASN X -1 UNP P0A4Z8 EXPRESSION TAG
SEQADV 4GO7 HIS X 0 UNP P0A4Z8 EXPRESSION TAG
SEQADV 4GO7 LEU X 173 UNP P0A4Z8 EXPRESSION TAG
SEQADV 4GO7 GLU X 174 UNP P0A4Z8 EXPRESSION TAG
SEQADV 4GO7 HIS X 175 UNP P0A4Z8 EXPRESSION TAG
SEQADV 4GO7 HIS X 176 UNP P0A4Z8 EXPRESSION TAG
SEQADV 4GO7 HIS X 177 UNP P0A4Z8 EXPRESSION TAG
SEQADV 4GO7 HIS X 178 UNP P0A4Z8 EXPRESSION TAG
SEQADV 4GO7 HIS X 179 UNP P0A4Z8 EXPRESSION TAG
SEQADV 4GO7 HIS X 180 UNP P0A4Z8 EXPRESSION TAG
SEQRES 1 X 200 MET GLY SER ILE HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 X 200 LEU VAL PRO ARG GLY ASN HIS MET GLU ASP PRO ILE LEU
SEQRES 3 X 200 THR GLY VAL ALA HIS ASP ARG SER GLU ALA LYS VAL THR
SEQRES 4 X 200 ILE VAL GLY LEU PRO ASP ILE PRO GLY TYR ALA ALA LYS
SEQRES 5 X 200 VAL PHE ARG ALA VAL ALA ASP ALA ASP VAL ASN ILE ASP
SEQRES 6 X 200 MET VAL LEU GLN ASN VAL SER LYS VAL GLU ASP GLY LYS
SEQRES 7 X 200 THR ASP ILE THR PHE THR CYS SER ARG ASP VAL GLY PRO
SEQRES 8 X 200 ALA ALA VAL GLU LYS LEU ASP SER LEU ARG ASN GLU ILE
SEQRES 9 X 200 GLY PHE SER GLN LEU LEU TYR ASP ASP HIS ILE GLY LYS
SEQRES 10 X 200 VAL SER LEU ILE GLY ALA GLY MET ARG SER HIS PRO GLY
SEQRES 11 X 200 VAL THR ALA THR PHE CYS GLU ALA LEU ALA ALA VAL GLY
SEQRES 12 X 200 VAL ASN ILE GLU LEU ILE SER THR SER GLU ILE ARG ILE
SEQRES 13 X 200 SER VAL LEU CYS ARG ASP THR GLU LEU ASP LYS ALA VAL
SEQRES 14 X 200 VAL ALA LEU HIS GLU ALA PHE GLY LEU GLY GLY ASP GLU
SEQRES 15 X 200 GLU ALA THR VAL TYR ALA GLY THR GLY ARG LEU GLU HIS
SEQRES 16 X 200 HIS HIS HIS HIS HIS
HET THR X 201 8
HETNAM THR THREONINE
FORMUL 2 THR C4 H9 N O3
FORMUL 3 HOH *43(H2 O)
HELIX 1 1 GLY X 28 ALA X 40 1 13
HELIX 2 2 VAL X 69 SER X 79 1 11
HELIX 3 3 LEU X 80 GLY X 85 1 6
HELIX 4 4 HIS X 108 VAL X 122 1 15
HELIX 5 5 GLU X 144 GLY X 157 1 14
SHEET 1 A 5 LEU X 128 THR X 131 0
SHEET 2 A 5 ARG X 135 ARG X 141 -1 O SER X 137 N SER X 130
SHEET 3 A 5 ILE X 95 ALA X 103 -1 N GLY X 96 O CYS X 140
SHEET 4 A 5 ILE X 5 ASP X 12 -1 N GLY X 8 O ILE X 101
SHEET 5 A 5 THR X 165 VAL X 166 -1 O THR X 165 N LEU X 6
SHEET 1 B 4 VAL X 47 LEU X 48 0
SHEET 2 B 4 LYS X 58 SER X 66 -1 O THR X 62 N LEU X 48
SHEET 3 B 4 GLU X 15 PRO X 24 -1 N LEU X 23 O THR X 59
SHEET 4 B 4 GLN X 88 ASP X 92 -1 O LEU X 90 N THR X 19
SITE 1 AC1 12 ASP X 25 ILE X 26 PRO X 27 GLY X 28
SITE 2 AC1 12 TYR X 29 ALA X 30 GLN X 49 THR X 59
SITE 3 AC1 12 ASN X 125 ILE X 126 HOH X 304 HOH X 338
CRYST1 62.371 62.371 137.289 90.00 90.00 90.00 I 41 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 0.016033 0.000000 0.000000 0.00000
SCALE2 0.000000 0.016033 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007284 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
