HEADER TRANSFERASE 07-SEP-10 3ORM
TITLE MYCOBACTERIUM TUBERCULOSIS PKNB KINASE DOMAIN D76A MUTANT
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SERINE/THREONINE PROTEIN KINASE;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: KINASE DOMAIN (UNP RESIDUES 1 TO 308);
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM TUBERCULOSIS;
SOURCE 3 ORGANISM_TAXID: 419947;
SOURCE 4 STRAIN: H37RV;
SOURCE 5 GENE: MRA_0016, PKNB, PKNB (RV0014C);
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21+;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET28B
KEYWDS STRUCTURAL GENOMICS, TB STRUCTURAL GENOMICS CONSORTIUM, TBSGC, KINASE
KEYWDS 2 DOMAIN, SIGNAL TRANSDUCTION, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR N.ECHOLS,T.N.LOMBANA,T.ALBER,TB STRUCTURAL GENOMICS CONSORTIUM
AUTHOR 2 (TBSGC)
REVDAT 3 06-SEP-23 3ORM 1 REMARK SEQADV LINK
REVDAT 2 06-FEB-13 3ORM 1 JRNL REMARK VERSN
REVDAT 1 15-DEC-10 3ORM 0
JRNL AUTH T.N.LOMBANA,N.ECHOLS,M.C.GOOD,N.D.THOMSEN,H.L.NG,
JRNL AUTH 2 A.E.GREENSTEIN,A.M.FALICK,D.S.KING,T.ALBER
JRNL TITL ALLOSTERIC ACTIVATION MECHANISM OF THE MYCOBACTERIUM
JRNL TITL 2 TUBERCULOSIS RECEPTOR SER/THR PROTEIN KINASE, PKNB.
JRNL REF STRUCTURE V. 18 1667 2010
JRNL REFN ISSN 0969-2126
JRNL PMID 21134645
JRNL DOI 10.1016/J.STR.2010.09.019
REMARK 2
REMARK 2 RESOLUTION. 2.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.01
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.200
REMARK 3 COMPLETENESS FOR RANGE (%) : 81.3
REMARK 3 NUMBER OF REFLECTIONS : 9801
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.218
REMARK 3 R VALUE (WORKING SET) : 0.215
REMARK 3 FREE R VALUE : 0.288
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.630
REMARK 3 FREE R VALUE TEST SET COUNT : 700
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 20.0055 - 4.2640 0.96 3433 130 0.2008 0.3022
REMARK 3 2 4.2640 - 3.3898 0.89 3130 168 0.1869 0.2611
REMARK 3 3 3.3898 - 2.9628 0.84 2950 168 0.2196 0.2628
REMARK 3 4 2.9628 - 2.6927 0.71 2519 101 0.2653 0.3253
REMARK 3 5 2.6927 - 2.5000 0.67 2386 133 0.3092 0.3654
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 0.90
REMARK 3 SHRINKAGE RADIUS : 0.77
REMARK 3 K_SOL : 0.37
REMARK 3 B_SOL : 21.98
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.330
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : NULL
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 60.55
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -4.93710
REMARK 3 B22 (A**2) : -0.85400
REMARK 3 B33 (A**2) : 5.79120
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 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.006 2086
REMARK 3 ANGLE : 1.100 2852
REMARK 3 CHIRALITY : 0.053 328
REMARK 3 PLANARITY : 0.005 375
REMARK 3 DIHEDRAL : 18.152 790
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 2
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: ( CHAIN A AND RESID 10:96 )
REMARK 3 ORIGIN FOR THE GROUP (A): -3.6692 22.9337 9.8537
REMARK 3 T TENSOR
REMARK 3 T11: 0.3077 T22: 0.1512
REMARK 3 T33: 0.1400 T12: 0.0199
REMARK 3 T13: -0.0514 T23: 0.0469
REMARK 3 L TENSOR
REMARK 3 L11: 1.2759 L22: 0.6832
REMARK 3 L33: 0.6907 L12: -0.8443
REMARK 3 L13: -0.4863 L23: 0.0668
REMARK 3 S TENSOR
REMARK 3 S11: -0.0530 S12: 0.0158 S13: -0.0130
REMARK 3 S21: -0.4878 S22: 0.0603 S23: 0.2820
REMARK 3 S31: -0.2642 S32: -0.1901 S33: 0.0001
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: ( CHAIN A AND RESID 97:289 )
REMARK 3 ORIGIN FOR THE GROUP (A): 10.1868 4.9315 23.1280
REMARK 3 T TENSOR
REMARK 3 T11: 0.0401 T22: 0.0909
REMARK 3 T33: 0.0816 T12: -0.0762
REMARK 3 T13: -0.0005 T23: 0.0419
REMARK 3 L TENSOR
REMARK 3 L11: 2.4570 L22: 1.8658
REMARK 3 L33: 2.0674 L12: -0.4200
REMARK 3 L13: 0.7029 L23: -0.3843
REMARK 3 S TENSOR
REMARK 3 S11: 0.0645 S12: -0.2362 S13: -0.1065
REMARK 3 S21: -0.1381 S22: 0.1036 S23: -0.1388
REMARK 3 S31: 0.0939 S32: -0.4061 S33: 0.0002
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3ORM COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-SEP-10.
REMARK 100 THE DEPOSITION ID IS D_1000061485.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 19-APR-07
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 : ALS
REMARK 200 BEAMLINE : 8.3.1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.116
REMARK 200 MONOCHROMATOR : Y
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 9801
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.500
REMARK 200 RESOLUTION RANGE LOW (A) : 67.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.0
REMARK 200 DATA REDUNDANCY : 3.000
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.07000
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 17.6800
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.59
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.5
REMARK 200 DATA REDUNDANCY IN SHELL : 2.60
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 0.324
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: PDB ENTRY 1MRU
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 40.85
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.08
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG 3350, 100MM BIS-TRIS PROPANE
REMARK 280 PH 8.5, 200MM NAF, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE
REMARK 280 277K
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 20.22900
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 67.37300
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 25.53800
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 67.37300
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 20.22900
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 25.53800
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 300 REMARK: STRUCTURE IS OF A MONOMERIC MUTANT; THE WILD-TYPE PROTEIN
REMARK 300 FORMS A DIMER.
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 GLY A -2
REMARK 465 SER A -1
REMARK 465 HIS A 0
REMARK 465 MET A 1
REMARK 465 THR A 2
REMARK 465 THR A 3
REMARK 465 PRO A 4
REMARK 465 SER A 5
REMARK 465 HIS A 6
REMARK 465 LEU A 7
REMARK 465 SER A 8
REMARK 465 ASP A 9
REMARK 465 ASP A 165
REMARK 465 SER A 166
REMARK 465 GLY A 167
REMARK 465 ASN A 168
REMARK 465 SER A 169
REMARK 465 VAL A 170
REMARK 465 THR A 171
REMARK 465 GLN A 172
REMARK 465 THR A 173
REMARK 465 ALA A 174
REMARK 465 ALA A 175
REMARK 465 VAL A 176
REMARK 465 ILE A 177
REMARK 465 GLY A 178
REMARK 465 ASP A 290
REMARK 465 ALA A 291
REMARK 465 GLU A 292
REMARK 465 ARG A 293
REMARK 465 THR A 294
REMARK 465 SER A 295
REMARK 465 LEU A 296
REMARK 465 LEU A 297
REMARK 465 SER A 298
REMARK 465 SER A 299
REMARK 465 ALA A 300
REMARK 465 ALA A 301
REMARK 465 GLY A 302
REMARK 465 ASN A 303
REMARK 465 LEU A 304
REMARK 465 SER A 305
REMARK 465 GLY A 306
REMARK 465 PRO A 307
REMARK 465 ARG A 308
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 GLU A 12 CG CD OE1 OE2
REMARK 470 LEU A 13 CG CD1 CD2
REMARK 470 GLU A 15 CG CD OE1 OE2
REMARK 470 GLU A 24 CG CD OE1 OE2
REMARK 470 SER A 51 OG
REMARK 470 ARG A 57 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 161 CG CD NE CZ NH1 NH2
REMARK 470 THR A 289 OG1 CG2
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 317 O HOH A 323 2.13
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 OE1 GLN A 131 OE1 GLU A 260 3555 2.18
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 THR A 77 -150.70 -134.64
REMARK 500 GLU A 81 46.75 -93.36
REMARK 500 THR A 82 159.43 -46.96
REMARK 500 ARG A 137 -14.11 95.31
REMARK 500 ASP A 138 31.69 -144.81
REMARK 500 ALA A 180 3.85 -150.20
REMARK 500 VAL A 229 78.23 -118.23
REMARK 500 ARG A 230 -46.72 164.99
REMARK 500 GLU A 241 -172.04 -66.54
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 MN A 341 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 156 OD2
REMARK 620 2 ASP A 156 OD1 53.1
REMARK 620 3 AGS A 340 O2B 82.3 87.7
REMARK 620 4 AGS A 340 S1G 107.7 156.2 74.6
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AGS A 340
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN A 341
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3ORM RELATED DB: PDB
REMARK 900 RELATED ID: 3ORO RELATED DB: PDB
REMARK 900 RELATED ID: 3ORP RELATED DB: PDB
REMARK 900 RELATED ID: 3ORT RELATED DB: PDB
REMARK 900 RELATED ID: 1MRU RELATED DB: PDB
REMARK 900 WILD-TYPE
REMARK 900 RELATED ID: 1O6Y RELATED DB: PDB
REMARK 900 WILD-TYPE
REMARK 900 RELATED ID: 3ORI RELATED DB: PDB
REMARK 900 L33D MUTANT
REMARK 900 RELATED ID: 3ORK RELATED DB: PDB
REMARK 900 L33D MUTANT
REMARK 900 RELATED ID: 3ORL RELATED DB: PDB
REMARK 900 L33D MUTANT
DBREF 3ORM A 1 308 UNP A5TY84 A5TY84_MYCTA 1 308
SEQADV 3ORM GLY A -2 UNP A5TY84 EXPRESSION TAG
SEQADV 3ORM SER A -1 UNP A5TY84 EXPRESSION TAG
SEQADV 3ORM HIS A 0 UNP A5TY84 EXPRESSION TAG
SEQADV 3ORM ALA A 76 UNP A5TY84 ASP 76 ENGINEERED MUTATION
SEQRES 1 A 311 GLY SER HIS MET THR THR PRO SER HIS LEU SER ASP ARG
SEQRES 2 A 311 TYR GLU LEU GLY GLU ILE LEU GLY PHE GLY GLY MET SER
SEQRES 3 A 311 GLU VAL HIS LEU ALA ARG ASP LEU ARG LEU HIS ARG ASP
SEQRES 4 A 311 VAL ALA VAL LYS VAL LEU ARG ALA ASP LEU ALA ARG ASP
SEQRES 5 A 311 PRO SER PHE TYR LEU ARG PHE ARG ARG GLU ALA GLN ASN
SEQRES 6 A 311 ALA ALA ALA LEU ASN HIS PRO ALA ILE VAL ALA VAL TYR
SEQRES 7 A 311 ALA THR GLY GLU ALA GLU THR PRO ALA GLY PRO LEU PRO
SEQRES 8 A 311 TYR ILE VAL MET GLU TYR VAL ASP GLY VAL THR LEU ARG
SEQRES 9 A 311 ASP ILE VAL HIS THR GLU GLY PRO MET THR PRO LYS ARG
SEQRES 10 A 311 ALA ILE GLU VAL ILE ALA ASP ALA CYS GLN ALA LEU ASN
SEQRES 11 A 311 PHE SER HIS GLN ASN GLY ILE ILE HIS ARG ASP VAL LYS
SEQRES 12 A 311 PRO ALA ASN ILE MET ILE SER ALA THR ASN ALA VAL LYS
SEQRES 13 A 311 VAL MET ASP PHE GLY ILE ALA ARG ALA ILE ALA ASP SER
SEQRES 14 A 311 GLY ASN SER VAL THR GLN THR ALA ALA VAL ILE GLY THR
SEQRES 15 A 311 ALA GLN TYR LEU SER PRO GLU GLN ALA ARG GLY ASP SER
SEQRES 16 A 311 VAL ASP ALA ARG SER ASP VAL TYR SER LEU GLY CYS VAL
SEQRES 17 A 311 LEU TYR GLU VAL LEU THR GLY GLU PRO PRO PHE THR GLY
SEQRES 18 A 311 ASP SER PRO VAL SER VAL ALA TYR GLN HIS VAL ARG GLU
SEQRES 19 A 311 ASP PRO ILE PRO PRO SER ALA ARG HIS GLU GLY LEU SER
SEQRES 20 A 311 ALA ASP LEU ASP ALA VAL VAL LEU LYS ALA LEU ALA LYS
SEQRES 21 A 311 ASN PRO GLU ASN ARG TYR GLN THR ALA ALA GLU MET ARG
SEQRES 22 A 311 ALA ASP LEU VAL ARG VAL HIS ASN GLY GLU PRO PRO GLU
SEQRES 23 A 311 ALA PRO LYS VAL LEU THR ASP ALA GLU ARG THR SER LEU
SEQRES 24 A 311 LEU SER SER ALA ALA GLY ASN LEU SER GLY PRO ARG
HET AGS A 340 31
HET MN A 341 1
HETNAM AGS PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER
HETNAM MN MANGANESE (II) ION
HETSYN AGS ATP-GAMMA-S; ADENOSINE 5'-(3-THIOTRIPHOSPHATE);
HETSYN 2 AGS ADENOSINE 5'-(GAMMA-THIOTRIPHOSPHATE); ADENOSINE-5'-
HETSYN 3 AGS DIPHOSPHATE MONOTHIOPHOSPHATE
FORMUL 2 AGS C10 H16 N5 O12 P3 S
FORMUL 3 MN MN 2+
FORMUL 4 HOH *15(H2 O)
HELIX 1 1 ALA A 44 ALA A 47 5 4
HELIX 2 2 ASP A 49 ALA A 64 1 16
HELIX 3 3 LEU A 100 GLY A 108 1 9
HELIX 4 4 THR A 111 ASN A 132 1 22
HELIX 5 5 LYS A 140 ALA A 142 5 3
HELIX 6 6 SER A 184 ARG A 189 1 6
HELIX 7 7 ASP A 194 GLY A 212 1 19
HELIX 8 8 SER A 220 VAL A 229 1 10
HELIX 9 9 PRO A 235 ARG A 239 5 5
HELIX 10 10 SER A 244 LEU A 255 1 12
HELIX 11 11 ASN A 258 ARG A 262 5 5
HELIX 12 12 THR A 265 ASN A 278 1 14
SHEET 1 A 5 TYR A 11 PHE A 19 0
SHEET 2 A 5 SER A 23 ASP A 30 -1 O LEU A 27 N GLY A 14
SHEET 3 A 5 ARG A 35 LEU A 42 -1 O VAL A 39 N HIS A 26
SHEET 4 A 5 LEU A 87 GLU A 93 -1 O ILE A 90 N LYS A 40
SHEET 5 A 5 VAL A 74 ALA A 76 -1 N TYR A 75 O VAL A 91
SHEET 1 B 5 TYR A 11 PHE A 19 0
SHEET 2 B 5 SER A 23 ASP A 30 -1 O LEU A 27 N GLY A 14
SHEET 3 B 5 ARG A 35 LEU A 42 -1 O VAL A 39 N HIS A 26
SHEET 4 B 5 LEU A 87 GLU A 93 -1 O ILE A 90 N LYS A 40
SHEET 5 B 5 GLU A 79 ALA A 80 -1 N ALA A 80 O LEU A 87
SHEET 1 C 3 GLY A 97 THR A 99 0
SHEET 2 C 3 ILE A 144 SER A 147 -1 O ILE A 146 N VAL A 98
SHEET 3 C 3 VAL A 152 VAL A 154 -1 O LYS A 153 N MET A 145
LINK OD2 ASP A 156 MN MN A 341 1555 1555 2.45
LINK OD1 ASP A 156 MN MN A 341 1555 1555 2.48
LINK O2B AGS A 340 MN MN A 341 1555 1555 2.14
LINK S1G AGS A 340 MN MN A 341 1555 1555 2.60
SITE 1 AC1 17 LEU A 17 GLY A 18 GLY A 20 GLY A 21
SITE 2 AC1 17 MET A 22 SER A 23 VAL A 25 LYS A 40
SITE 3 AC1 17 GLU A 93 VAL A 95 THR A 99 LYS A 140
SITE 4 AC1 17 ASN A 143 MET A 155 ASP A 156 HOH A 309
SITE 5 AC1 17 MN A 341
SITE 1 AC2 2 ASP A 156 AGS A 340
CRYST1 40.458 51.076 134.746 90.00 90.00 90.00 P 21 21 21 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 0.024717 0.000000 0.000000 0.00000
SCALE2 0.000000 0.019579 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007421 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
