HEADER HYDROLASE 02-SEP-15 5DJH
TITLE STRUCTURE OF M. TUBERCULOSIS CYSQ, A PAP PHOSPHATASE WITH AMP, PO4,
TITLE 2 AND 3MG BOUND
CAVEAT 5DJH RESIDUES A SER 117 AND A PRO 122 ARE LINKED (INTERVENING
CAVEAT 2 5DJH RESIDUES SNGQ ARE OMITTED).
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 3'-PHOSPHOADENOSINE 5'-PHOSPHATE PHOSPHATASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: CYSQ, PAP PHOSPHATASE, 3'(2'),5'-BISPHOSPHATE NUCLEOTIDASE,
COMPND 5 5-BISPHOSPHONUCLEOSIDE 3'(2')-PHOSPHOHYDROLASE, D-FRUCTOSE-1,6-
COMPND 6 BISPHOSPHATE 1-PHOSPHOHYDROLASE, DPNPASE, FRUCTOSE-1,6-
COMPND 7 BISPHOSPHATASE, FBPASE, INOSITOL-1-MONOPHOSPHATASE,IMPASE, INOSITOL-
COMPND 8 1-PHOSPHATASE;
COMPND 9 EC: 3.1.3.7, 3.1.3.11, 3.1.3.25;
COMPND 10 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM TUBERCULOSIS;
SOURCE 3 ORGANISM_TAXID: 1773;
SOURCE 4 GENE: CYSQ, MT2189;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET28B
KEYWDS CYSQ, PAP PHOSPHATASE, AMP, MAGNESIUM, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.J.FISHER,A.I.ERICKSON
REVDAT 4 27-SEP-23 5DJH 1 LINK
REVDAT 3 22-NOV-17 5DJH 1 JRNL REMARK
REVDAT 2 02-DEC-15 5DJH 1 JRNL
REVDAT 1 11-NOV-15 5DJH 0
JRNL AUTH A.I.ERICKSON,R.D.SARSAM,A.J.FISHER
JRNL TITL CRYSTAL STRUCTURES OF MYCOBACTERIUM TUBERCULOSIS CYSQ, WITH
JRNL TITL 2 SUBSTRATE AND PRODUCTS BOUND.
JRNL REF BIOCHEMISTRY V. 54 6830 2015
JRNL REFN ISSN 0006-2960
JRNL PMID 26512869
JRNL DOI 10.1021/ACS.BIOCHEM.5B01000
REMARK 2
REMARK 2 RESOLUTION. 1.45 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.9_1692
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) : 1.45
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 38.17
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.090
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.4
REMARK 3 NUMBER OF REFLECTIONS : 42861
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.150
REMARK 3 R VALUE (WORKING SET) : 0.149
REMARK 3 FREE R VALUE : 0.169
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.930
REMARK 3 FREE R VALUE TEST SET COUNT : 2111
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 38.1817 - 4.4050 0.95 2637 143 0.1466 0.1548
REMARK 3 2 4.4050 - 3.4971 0.97 2700 134 0.1177 0.1467
REMARK 3 3 3.4971 - 3.0553 0.96 2668 151 0.1388 0.1496
REMARK 3 4 3.0553 - 2.7760 0.97 2655 170 0.1461 0.1640
REMARK 3 5 2.7760 - 2.5771 0.97 2680 162 0.1515 0.1679
REMARK 3 6 2.5771 - 2.4252 0.98 2684 154 0.1540 0.1800
REMARK 3 7 2.4252 - 2.3037 0.97 2724 152 0.1430 0.1770
REMARK 3 8 2.3037 - 2.2035 0.98 2702 144 0.1430 0.1422
REMARK 3 9 2.2035 - 2.1186 0.98 2748 145 0.1402 0.1625
REMARK 3 10 2.1186 - 2.0455 0.98 2739 121 0.1337 0.1639
REMARK 3 11 2.0455 - 1.9816 0.98 2718 155 0.1460 0.1580
REMARK 3 12 1.9816 - 1.9249 0.98 2706 139 0.1453 0.1478
REMARK 3 13 1.9249 - 1.8743 0.98 2698 150 0.1475 0.1572
REMARK 3 14 1.8743 - 1.8285 0.98 2798 129 0.1481 0.1549
REMARK 3 15 1.8285 - 1.7870 0.98 2689 152 0.1490 0.1784
REMARK 3 16 1.7870 - 1.7489 0.98 2721 140 0.1494 0.1826
REMARK 3 17 1.7489 - 1.7140 0.98 2731 111 0.1541 0.1586
REMARK 3 18 1.7140 - 1.6816 0.98 2766 122 0.1563 0.1863
REMARK 3 19 1.6816 - 1.6516 0.97 2716 110 0.1550 0.1653
REMARK 3 20 1.6516 - 1.6236 0.98 2672 151 0.1661 0.2385
REMARK 3 21 1.6236 - 1.5974 0.98 2770 154 0.1614 0.1875
REMARK 3 22 1.5974 - 1.5728 0.97 2676 134 0.1760 0.2216
REMARK 3 23 1.5728 - 1.5497 0.97 2720 143 0.1781 0.2152
REMARK 3 24 1.5497 - 1.5279 0.97 2704 132 0.1929 0.2247
REMARK 3 25 1.5279 - 1.5072 0.97 2673 129 0.1885 0.2398
REMARK 3 26 1.5072 - 1.4876 0.97 2751 133 0.2143 0.2408
REMARK 3 27 1.4876 - 1.4690 0.97 2686 143 0.2244 0.2605
REMARK 3 28 1.4690 - 1.4513 0.96 2623 126 0.2389 0.2586
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.130
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 15.740
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
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 2042
REMARK 3 ANGLE : 1.173 2804
REMARK 3 CHIRALITY : 0.079 318
REMARK 3 PLANARITY : 0.006 364
REMARK 3 DIHEDRAL : 11.750 747
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 5
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: (CHAIN A AND RESID -16:17)
REMARK 3 ORIGIN FOR THE GROUP (A): -14.1471 28.1759 19.8449
REMARK 3 T TENSOR
REMARK 3 T11: 0.1461 T22: 0.3956
REMARK 3 T33: 0.2789 T12: -0.0606
REMARK 3 T13: 0.0221 T23: 0.0988
REMARK 3 L TENSOR
REMARK 3 L11: 0.4720 L22: 0.5712
REMARK 3 L33: 0.0332 L12: 0.3515
REMARK 3 L13: -0.1156 L23: -0.1272
REMARK 3 S TENSOR
REMARK 3 S11: 0.0938 S12: -0.5736 S13: -0.0273
REMARK 3 S21: 0.2473 S22: 0.0596 S23: 0.5227
REMARK 3 S31: 0.1773 S32: -0.5967 S33: 0.0183
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: (CHAIN A AND RESID 18:123)
REMARK 3 ORIGIN FOR THE GROUP (A): 7.9226 33.0536 21.5984
REMARK 3 T TENSOR
REMARK 3 T11: 0.0654 T22: 0.0825
REMARK 3 T33: 0.0669 T12: -0.0053
REMARK 3 T13: -0.0010 T23: 0.0021
REMARK 3 L TENSOR
REMARK 3 L11: 1.1090 L22: 1.8966
REMARK 3 L33: 0.7665 L12: 0.2818
REMARK 3 L13: 0.3356 L23: 0.0686
REMARK 3 S TENSOR
REMARK 3 S11: 0.0040 S12: -0.0767 S13: -0.0193
REMARK 3 S21: 0.0399 S22: 0.0378 S23: -0.0738
REMARK 3 S31: 0.0349 S32: -0.0227 S33: -0.0475
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: (CHAIN A AND RESID 124:164)
REMARK 3 ORIGIN FOR THE GROUP (A): 4.2539 37.8422 5.9860
REMARK 3 T TENSOR
REMARK 3 T11: 0.1071 T22: 0.1113
REMARK 3 T33: 0.0827 T12: -0.0135
REMARK 3 T13: -0.0207 T23: 0.0123
REMARK 3 L TENSOR
REMARK 3 L11: 1.6084 L22: 0.9617
REMARK 3 L33: 0.9660 L12: 0.2234
REMARK 3 L13: -0.8091 L23: -0.5963
REMARK 3 S TENSOR
REMARK 3 S11: -0.0352 S12: 0.1445 S13: 0.0060
REMARK 3 S21: -0.0848 S22: 0.0583 S23: 0.0027
REMARK 3 S31: 0.0233 S32: -0.1110 S33: -0.0443
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: (CHAIN A AND RESID 165:249)
REMARK 3 ORIGIN FOR THE GROUP (A): 12.9542 30.9982 3.1375
REMARK 3 T TENSOR
REMARK 3 T11: 0.1367 T22: 0.1105
REMARK 3 T33: 0.1072 T12: 0.0094
REMARK 3 T13: 0.0136 T23: -0.0006
REMARK 3 L TENSOR
REMARK 3 L11: 0.2141 L22: 0.6200
REMARK 3 L33: 1.4682 L12: 0.3077
REMARK 3 L13: -0.4054 L23: -0.6152
REMARK 3 S TENSOR
REMARK 3 S11: -0.0105 S12: 0.0235 S13: -0.0465
REMARK 3 S21: -0.1371 S22: -0.0354 S23: -0.0628
REMARK 3 S31: 0.1324 S32: 0.0924 S33: 0.0393
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: (CHAIN A AND RESID 250:267)
REMARK 3 ORIGIN FOR THE GROUP (A): 13.6470 28.4347 -9.2652
REMARK 3 T TENSOR
REMARK 3 T11: 0.3616 T22: 0.1663
REMARK 3 T33: 0.1156 T12: -0.0078
REMARK 3 T13: 0.0570 T23: 0.0066
REMARK 3 L TENSOR
REMARK 3 L11: 8.2874 L22: 3.9574
REMARK 3 L33: 5.2623 L12: -1.1707
REMARK 3 L13: -3.8999 L23: 2.9595
REMARK 3 S TENSOR
REMARK 3 S11: -0.1406 S12: 0.0834 S13: -0.0953
REMARK 3 S21: -0.3798 S22: 0.0539 S23: -0.0980
REMARK 3 S31: 0.4116 S32: 0.0994 S33: 0.0708
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 5DJH COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-SEP-15.
REMARK 100 THE DEPOSITION ID IS D_1000212618.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 28-MAY-14
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRL
REMARK 200 BEAMLINE : BL7-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.12709
REMARK 200 MONOCHROMATOR : SIDE SCATTERING I-BEAM BENT
REMARK 200 SINGLE CRYSTAL, ASYMMETRIC CUT
REMARK 200 4.9650 DEGREES
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : XSCALE JULY 4, 2012, XDS
REMARK 200 NOVEMBER 11, 2013
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 42861
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.451
REMARK 200 RESOLUTION RANGE LOW (A) : 38.168
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.2
REMARK 200 DATA REDUNDANCY : 3.530
REMARK 200 R MERGE (I) : 0.03300
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 23.8700
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.45
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.49
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.2
REMARK 200 DATA REDUNDANCY IN SHELL : 3.48
REMARK 200 R MERGE FOR SHELL (I) : 0.38700
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.470
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: PDB ENTRY 5DJF
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 36.73
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.94
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M MAGNESIUM ACETATE, 0.1 M BIS
REMARK 280 -TRIS-HCL, 35% PEG550 MME, PH 6.5, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 298.15K
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 20.31800
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 50.59900
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 29.07000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 50.59900
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 20.31800
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 29.07000
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 TOTAL BURIED SURFACE AREA: 1280 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 11460 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -40.0 KCAL/MOL
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 -21
REMARK 465 GLY A -20
REMARK 465 SER A -19
REMARK 465 SER A -18
REMARK 465 HIS A -17
REMARK 465 SER A -10
REMARK 465 SER A -9
REMARK 465 GLY A -8
REMARK 465 LEU A -7
REMARK 465 VAL A -6
REMARK 465 PRO A -5
REMARK 465 ARG A -4
REMARK 465 GLY A -3
REMARK 465 SER A -2
REMARK 465 HIS A -1
REMARK 465 MET A 0
REMARK 465 VAL A 1
REMARK 465 VAL A 2
REMARK 465 SER A 3
REMARK 465 PRO A 4
REMARK 465 ALA A 5
REMARK 465 ALA A 6
REMARK 465 PRO A 7
REMARK 465 ASP A 8
REMARK 465 LEU A 9
REMARK 465 THR A 10
REMARK 465 SER A 118
REMARK 465 ASN A 119
REMARK 465 GLY A 120
REMARK 465 GLN A 121
REMARK 465 GLY A 147
REMARK 465 ALA A 148
REMARK 465 ALA A 149
REMARK 465 PRO A 150
REMARK 465 ALA A 151
REMARK 465 GLY A 152
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 470 O HOH A 627 2.12
REMARK 500 O ARG A 116 O HOH A 401 2.17
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 A 12 74.74 59.75
REMARK 500 SER A 117 -45.37 166.76
REMARK 500 SER A 186 132.62 78.59
REMARK 500 SER A 186 136.09 73.54
REMARK 500 GLN A 208 173.60 177.69
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 301 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 73 OE1
REMARK 620 2 ASP A 91 OD1 91.7
REMARK 620 3 LEU A 93 O 169.8 86.1
REMARK 620 4 PO4 A 305 O2 96.5 96.8 93.7
REMARK 620 5 PO4 A 305 O3 97.6 162.6 87.1 67.6
REMARK 620 6 HOH A 439 O 86.0 99.8 84.6 163.1 95.5
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 303 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 73 OE2
REMARK 620 2 PO4 A 305 O4 103.7
REMARK 620 3 HOH A 414 O 89.3 93.0
REMARK 620 4 HOH A 466 O 91.4 89.7 177.0
REMARK 620 5 HOH A 493 O 86.6 169.4 89.5 87.6
REMARK 620 6 HOH A 497 O 165.8 90.2 87.1 91.5 79.7
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 302 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 91 OD2
REMARK 620 2 ASP A 94 OD1 95.2
REMARK 620 3 ASP A 212 OD1 92.3 90.9
REMARK 620 4 AMP A 304 O3' 172.8 91.8 89.6
REMARK 620 5 PO4 A 305 O2 91.0 99.3 169.0 85.9
REMARK 620 6 HOH A 442 O 98.2 163.0 78.2 75.3 91.0
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 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue AMP A 304
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 A 305
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5DJF RELATED DB: PDB
REMARK 900 RELATED ID: 5DJJ RELATED DB: PDB
REMARK 900 RELATED ID: 5DJI RELATED DB: PDB
REMARK 900 RELATED ID: 5DJG RELATED DB: PDB
REMARK 900 RELATED ID: 5DJK RELATED DB: PDB
DBREF 5DJH A 2 267 UNP P9WKJ0 CYSQ_MYCTO 2 267
SEQADV 5DJH MET A -21 UNP P9WKJ0 EXPRESSION TAG
SEQADV 5DJH GLY A -20 UNP P9WKJ0 EXPRESSION TAG
SEQADV 5DJH SER A -19 UNP P9WKJ0 EXPRESSION TAG
SEQADV 5DJH SER A -18 UNP P9WKJ0 EXPRESSION TAG
SEQADV 5DJH HIS A -17 UNP P9WKJ0 EXPRESSION TAG
SEQADV 5DJH HIS A -16 UNP P9WKJ0 EXPRESSION TAG
SEQADV 5DJH HIS A -15 UNP P9WKJ0 EXPRESSION TAG
SEQADV 5DJH HIS A -14 UNP P9WKJ0 EXPRESSION TAG
SEQADV 5DJH HIS A -13 UNP P9WKJ0 EXPRESSION TAG
SEQADV 5DJH HIS A -12 UNP P9WKJ0 EXPRESSION TAG
SEQADV 5DJH SER A -10 UNP P9WKJ0 EXPRESSION TAG
SEQADV 5DJH SER A -9 UNP P9WKJ0 EXPRESSION TAG
SEQADV 5DJH GLY A -8 UNP P9WKJ0 EXPRESSION TAG
SEQADV 5DJH LEU A -7 UNP P9WKJ0 EXPRESSION TAG
SEQADV 5DJH VAL A -6 UNP P9WKJ0 EXPRESSION TAG
SEQADV 5DJH PRO A -5 UNP P9WKJ0 EXPRESSION TAG
SEQADV 5DJH ARG A -4 UNP P9WKJ0 EXPRESSION TAG
SEQADV 5DJH GLY A -3 UNP P9WKJ0 EXPRESSION TAG
SEQADV 5DJH SER A -2 UNP P9WKJ0 EXPRESSION TAG
SEQADV 5DJH HIS A -1 UNP P9WKJ0 EXPRESSION TAG
SEQADV 5DJH MET A 0 UNP P9WKJ0 EXPRESSION TAG
SEQADV 5DJH VAL A 1 UNP P9WKJ0 EXPRESSION TAG
SEQRES 1 A 288 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 A 288 LEU VAL PRO ARG GLY SER HIS MET VAL VAL SER PRO ALA
SEQRES 3 A 288 ALA PRO ASP LEU THR ASP ASP LEU THR ASP ALA GLU LEU
SEQRES 4 A 288 ALA ALA ASP LEU ALA ALA ASP ALA GLY LYS LEU LEU LEU
SEQRES 5 A 288 GLN VAL ARG ALA GLU ILE GLY PHE ASP GLN PRO TRP THR
SEQRES 6 A 288 LEU GLY GLU ALA GLY ASP ARG GLN ALA ASN SER LEU LEU
SEQRES 7 A 288 LEU ARG ARG LEU GLN ALA GLU ARG PRO GLY ASP ALA VAL
SEQRES 8 A 288 LEU SER GLU GLU ALA HIS ASP ASP LEU ALA ARG LEU LYS
SEQRES 9 A 288 SER ASP ARG VAL TRP ILE ILE ASP PRO LEU ASP GLY THR
SEQRES 10 A 288 ARG GLU PHE SER THR PRO GLY ARG ASP ASP TRP ALA VAL
SEQRES 11 A 288 HIS ILE ALA LEU TRP ARG ARG SER SER ASN GLY GLN PRO
SEQRES 12 A 288 GLU ILE THR ASP ALA ALA VAL ALA LEU PRO ALA ARG GLY
SEQRES 13 A 288 ASN VAL VAL TYR ARG THR ASP THR VAL THR SER GLY ALA
SEQRES 14 A 288 ALA PRO ALA GLY VAL PRO GLY THR LEU ARG ILE ALA VAL
SEQRES 15 A 288 SER ALA THR ARG PRO PRO ALA VAL LEU HIS ARG ILE ARG
SEQRES 16 A 288 GLN THR LEU ALA ILE GLN PRO VAL SER ILE GLY SER ALA
SEQRES 17 A 288 GLY ALA LYS ALA MET ALA VAL ILE ASP GLY TYR VAL ASP
SEQRES 18 A 288 ALA TYR LEU HIS ALA GLY GLY GLN TRP GLU TRP ASP SER
SEQRES 19 A 288 ALA ALA PRO ALA GLY VAL MET LEU ALA ALA GLY MET HIS
SEQRES 20 A 288 ALA SER ARG LEU ASP GLY SER PRO LEU ARG TYR ASN GLN
SEQRES 21 A 288 LEU ASP PRO TYR LEU PRO ASP LEU LEU MET CYS ARG ALA
SEQRES 22 A 288 GLU VAL ALA PRO ILE LEU LEU GLY ALA ILE ALA ASP ALA
SEQRES 23 A 288 TRP ARG
HET MG A 301 1
HET MG A 302 1
HET MG A 303 1
HET AMP A 304 23
HET PO4 A 305 5
HETNAM MG MAGNESIUM ION
HETNAM AMP ADENOSINE MONOPHOSPHATE
HETNAM PO4 PHOSPHATE ION
FORMUL 2 MG 3(MG 2+)
FORMUL 5 AMP C10 H14 N5 O7 P
FORMUL 6 PO4 O4 P 3-
FORMUL 7 HOH *269(H2 O)
HELIX 1 AA1 THR A 14 GLY A 38 1 25
HELIX 2 AA2 GLN A 41 ARG A 65 1 25
HELIX 3 AA3 LEU A 79 SER A 84 5 6
HELIX 4 AA4 GLY A 95 SER A 100 1 6
HELIX 5 AA5 ALA A 168 ARG A 174 1 7
HELIX 6 AA6 SER A 186 ASP A 196 1 11
HELIX 7 AA7 TRP A 209 ALA A 223 1 15
HELIX 8 AA8 VAL A 254 ALA A 265 1 12
SHEET 1 AA1 5 ALA A 69 SER A 72 0
SHEET 2 AA1 5 ARG A 86 ASP A 94 1 O TRP A 88 N LEU A 71
SHEET 3 AA1 5 ALA A 108 ARG A 115 -1 O ALA A 108 N ASP A 94
SHEET 4 AA1 5 GLU A 123 LEU A 131 -1 O ASP A 126 N LEU A 113
SHEET 5 AA1 5 VAL A 137 ARG A 140 -1 O TYR A 139 N VAL A 129
SHEET 1 AA2 5 ILE A 179 ILE A 184 0
SHEET 2 AA2 5 LEU A 157 SER A 162 1 N ILE A 159 O VAL A 182
SHEET 3 AA2 5 ALA A 201 HIS A 204 1 O ALA A 201 N ALA A 160
SHEET 4 AA2 5 LEU A 247 CYS A 250 -1 O MET A 249 N TYR A 202
SHEET 5 AA2 5 HIS A 226 SER A 228 -1 N HIS A 226 O CYS A 250
LINK OE1 GLU A 73 MG MG A 301 1555 1555 1.96
LINK OE2 GLU A 73 MG MG A 303 1555 1555 2.13
LINK OD1 ASP A 91 MG MG A 301 1555 1555 2.08
LINK OD2 ASP A 91 MG MG A 302 1555 1555 2.06
LINK O LEU A 93 MG MG A 301 1555 1555 2.06
LINK OD1 ASP A 94 MG MG A 302 1555 1555 2.07
LINK OD1 ASP A 212 MG MG A 302 1555 1555 1.98
LINK MG MG A 301 O2 PO4 A 305 1555 1555 2.14
LINK MG MG A 301 O3 PO4 A 305 1555 1555 2.22
LINK MG MG A 301 O HOH A 439 1555 1555 2.06
LINK MG MG A 302 O3' AMP A 304 1555 1555 2.17
LINK MG MG A 302 O2 PO4 A 305 1555 1555 2.00
LINK MG MG A 302 O HOH A 442 1555 1555 2.25
LINK MG MG A 303 O4 PO4 A 305 1555 1555 1.87
LINK MG MG A 303 O HOH A 414 1555 1555 2.15
LINK MG MG A 303 O HOH A 466 1555 1555 2.16
LINK MG MG A 303 O HOH A 493 1555 1655 2.20
LINK MG MG A 303 O HOH A 497 1555 1555 2.07
CISPEP 1 SER A 117 PRO A 122 0 -6.71
SITE 1 AC1 6 GLU A 73 ASP A 91 LEU A 93 MG A 302
SITE 2 AC1 6 PO4 A 305 HOH A 439
SITE 1 AC2 7 ASP A 91 ASP A 94 ASP A 212 MG A 301
SITE 2 AC2 7 AMP A 304 PO4 A 305 HOH A 442
SITE 1 AC3 6 GLU A 73 PO4 A 305 HOH A 414 HOH A 466
SITE 2 AC3 6 HOH A 493 HOH A 497
SITE 1 AC4 23 ASP A 94 SER A 162 ARG A 165 GLY A 185
SITE 2 AC4 23 SER A 186 ALA A 187 LYS A 190 HIS A 204
SITE 3 AC4 23 GLY A 206 GLY A 207 GLN A 208 ASP A 212
SITE 4 AC4 23 MG A 302 PO4 A 305 HOH A 418 HOH A 419
SITE 5 AC4 23 HOH A 436 HOH A 442 HOH A 445 HOH A 454
SITE 6 AC4 23 HOH A 466 HOH A 469 HOH A 529
SITE 1 AC5 15 GLU A 73 ASP A 91 LEU A 93 ASP A 94
SITE 2 AC5 15 GLY A 95 THR A 96 MG A 301 MG A 302
SITE 3 AC5 15 MG A 303 AMP A 304 HOH A 414 HOH A 421
SITE 4 AC5 15 HOH A 442 HOH A 466 HOH A 497
CRYST1 40.636 58.140 101.198 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 0.024609 0.000000 0.000000 0.00000
SCALE2 0.000000 0.017200 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009882 0.00000
(ATOM LINES ARE NOT SHOWN.)
END