HEADER OXIDOREDUCTASE/OXIDOREDUCTASE INHIBITOR 10-MAY-15 4ZQP
TITLE CRYSTAL STRUCTURE OF THE CATALYTIC DOMAIN OF THE INOSINE MONOPHOSPHATE
TITLE 2 DEHYDROGENASE FROM MYCOBACTERIUM TUBERCULOSIS IN THE COMPLEX WITH IMP
TITLE 3 AND THE INHIBITOR MAD1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: INOSINE-5'-MONOPHOSPHATE DEHYDROGENASE,INOSINE-5'-
COMPND 3 MONOPHOSPHATE DEHYDROGENASE;
COMPND 4 CHAIN: A;
COMPND 5 FRAGMENT: UNP RESIDUES 1-125 AND 253-529 LINKED BY LINKER (GLY GLY);
COMPND 6 SYNONYM: IMPDH,IMPDH;
COMPND 7 EC: 1.1.1.205,1.1.1.205;
COMPND 8 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM TUBERCULOSIS (STRAIN ATCC 25618 /
SOURCE 3 H37RV);
SOURCE 4 ORGANISM_TAXID: 83332;
SOURCE 5 STRAIN: ATCC 25618 / H37RV;
SOURCE 6 GENE: GUAB, GUAB2, RV3411C, MTCY78.17;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: BL21(DE3) GOLD;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PMCSG7
KEYWDS IMPDH, DELTA CBS, MAD1, STRUCTURAL GENOMICS, CENTER FOR MEMBRANE
KEYWDS 2 PROTEINS OF INFECTIOUS DISEASES, CENTER FOR STRUCTURAL GENOMICS OF
KEYWDS 3 INFECTIOUS DISEASES, CSGID, OXIDOREDUCTASE-OXIDOREDUCTASE INHIBITOR
KEYWDS 4 COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.KIM,M.MAKOWSKA-GRZYSKA,M.GU,M.KAVITHA,L.HEDSTROM,W.F.ANDERSON,
AUTHOR 2 A.JOACHIMIAK,CENTER FOR STRUCTURAL GENOMICS OF INFECTIOUS DISEASES
AUTHOR 3 (CSGID)
REVDAT 5 30-MAR-22 4ZQP 1 LINK
REVDAT 4 22-NOV-17 4ZQP 1 REMARK
REVDAT 3 08-FEB-17 4ZQP 1 AUTHOR
REVDAT 2 16-DEC-15 4ZQP 1 JRNL
REVDAT 1 17-JUN-15 4ZQP 0
JRNL AUTH M.MAKOWSKA-GRZYSKA,Y.KIM,S.K.GORLA,Y.WEI,K.MANDAPATI,
JRNL AUTH 2 M.ZHANG,N.MALTSEVA,G.MODI,H.I.BOSHOFF,M.GU,C.ALDRICH,
JRNL AUTH 3 G.D.CUNY,L.HEDSTROM,A.JOACHIMIAK
JRNL TITL MYCOBACTERIUM TUBERCULOSIS IMPDH IN COMPLEXES WITH
JRNL TITL 2 SUBSTRATES, PRODUCTS AND ANTITUBERCULAR COMPOUNDS.
JRNL REF PLOS ONE V. 10 38976 2015
JRNL REFN ESSN 1932-6203
JRNL PMID 26440283
JRNL DOI 10.1371/JOURNAL.PONE.0138976
REMARK 2
REMARK 2 RESOLUTION. 1.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX DEV_1745
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) : 1.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 35.76
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.3
REMARK 3 NUMBER OF REFLECTIONS : 25083
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.145
REMARK 3 R VALUE (WORKING SET) : 0.143
REMARK 3 FREE R VALUE : 0.189
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.070
REMARK 3 FREE R VALUE TEST SET COUNT : 1272
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 35.7665 - 3.9267 0.97 2719 153 0.1345 0.1897
REMARK 3 2 3.9267 - 3.1173 0.99 2730 146 0.1356 0.1650
REMARK 3 3 3.1173 - 2.7235 0.99 2730 145 0.1445 0.1855
REMARK 3 4 2.7235 - 2.4745 0.99 2724 145 0.1373 0.1835
REMARK 3 5 2.4745 - 2.2972 1.00 2761 114 0.1322 0.1748
REMARK 3 6 2.2972 - 2.1618 1.00 2708 162 0.1330 0.1691
REMARK 3 7 2.1618 - 2.0535 1.00 2738 134 0.1538 0.2130
REMARK 3 8 2.0535 - 1.9641 0.96 2598 156 0.1887 0.2441
REMARK 3 9 1.9641 - 1.9000 0.77 2103 117 0.2186 0.2857
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) : 0.180
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 19.810
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 22.26
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 28.10
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 : 0.010 2716
REMARK 3 ANGLE : 1.380 3709
REMARK 3 CHIRALITY : 0.059 438
REMARK 3 PLANARITY : 0.005 480
REMARK 3 DIHEDRAL : 14.392 990
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 8
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND ( RESID 28 THROUGH 52 )
REMARK 3 ORIGIN FOR THE GROUP (A): -44.3649 -34.7787 -11.8932
REMARK 3 T TENSOR
REMARK 3 T11: 0.2539 T22: 0.2517
REMARK 3 T33: 0.1780 T12: 0.0091
REMARK 3 T13: 0.0130 T23: 0.0136
REMARK 3 L TENSOR
REMARK 3 L11: 6.3639 L22: 0.3742
REMARK 3 L33: 0.6090 L12: -1.4433
REMARK 3 L13: 1.9835 L23: -0.4726
REMARK 3 S TENSOR
REMARK 3 S11: 0.0522 S12: 0.4917 S13: -0.0956
REMARK 3 S21: -0.0714 S22: -0.0501 S23: -0.0149
REMARK 3 S31: 0.0198 S32: 0.0981 S33: -0.0188
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND ( RESID 53 THROUGH 99 )
REMARK 3 ORIGIN FOR THE GROUP (A): -18.1955 -22.8638 1.0800
REMARK 3 T TENSOR
REMARK 3 T11: 0.1545 T22: 0.2077
REMARK 3 T33: 0.2265 T12: -0.0097
REMARK 3 T13: -0.0144 T23: 0.0069
REMARK 3 L TENSOR
REMARK 3 L11: 1.3284 L22: 2.5927
REMARK 3 L33: 0.8230 L12: -0.5592
REMARK 3 L13: -0.5639 L23: 0.7155
REMARK 3 S TENSOR
REMARK 3 S11: 0.0378 S12: -0.0512 S13: 0.2242
REMARK 3 S21: 0.0022 S22: 0.0520 S23: -0.3555
REMARK 3 S31: -0.0313 S32: 0.1309 S33: -0.1146
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND ( RESID 100 THROUGH 262 )
REMARK 3 ORIGIN FOR THE GROUP (A): -23.8328 -7.4896 7.7214
REMARK 3 T TENSOR
REMARK 3 T11: 0.2403 T22: 0.1912
REMARK 3 T33: 0.3265 T12: -0.0355
REMARK 3 T13: -0.0348 T23: -0.0328
REMARK 3 L TENSOR
REMARK 3 L11: 3.0188 L22: 3.1816
REMARK 3 L33: 1.5718 L12: -1.4011
REMARK 3 L13: -0.5963 L23: 0.0562
REMARK 3 S TENSOR
REMARK 3 S11: -0.0720 S12: -0.2136 S13: 0.5444
REMARK 3 S21: 0.2141 S22: 0.0960 S23: -0.5075
REMARK 3 S31: -0.2420 S32: 0.2225 S33: -0.0147
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND ( RESID 263 THROUGH 326 )
REMARK 3 ORIGIN FOR THE GROUP (A): -31.0094 -6.6527 -5.4024
REMARK 3 T TENSOR
REMARK 3 T11: 0.2540 T22: 0.1713
REMARK 3 T33: 0.2788 T12: 0.0170
REMARK 3 T13: 0.0267 T23: 0.0370
REMARK 3 L TENSOR
REMARK 3 L11: 1.9424 L22: 2.6862
REMARK 3 L33: 2.8646 L12: 0.6321
REMARK 3 L13: 0.9560 L23: 1.4389
REMARK 3 S TENSOR
REMARK 3 S11: 0.0394 S12: 0.0585 S13: 0.3362
REMARK 3 S21: -0.1565 S22: -0.1039 S23: -0.1242
REMARK 3 S31: -0.3541 S32: 0.0044 S33: 0.0723
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' AND ( RESID 327 THROUGH 422 )
REMARK 3 ORIGIN FOR THE GROUP (A): -31.1323 -24.4610 3.2519
REMARK 3 T TENSOR
REMARK 3 T11: 0.1479 T22: 0.1328
REMARK 3 T33: 0.1367 T12: 0.0043
REMARK 3 T13: -0.0128 T23: 0.0085
REMARK 3 L TENSOR
REMARK 3 L11: 1.8613 L22: 1.4657
REMARK 3 L33: 0.6691 L12: 0.0613
REMARK 3 L13: -0.2630 L23: 0.3291
REMARK 3 S TENSOR
REMARK 3 S11: 0.0290 S12: -0.1699 S13: -0.0302
REMARK 3 S21: 0.1597 S22: -0.0014 S23: -0.0656
REMARK 3 S31: 0.0387 S32: 0.0252 S33: -0.0231
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'A' AND ( RESID 423 THROUGH 469 )
REMARK 3 ORIGIN FOR THE GROUP (A): -38.7509 -19.2027 14.5482
REMARK 3 T TENSOR
REMARK 3 T11: 0.2254 T22: 0.1951
REMARK 3 T33: 0.1879 T12: 0.0033
REMARK 3 T13: 0.0188 T23: -0.0395
REMARK 3 L TENSOR
REMARK 3 L11: 7.9003 L22: 2.6528
REMARK 3 L33: 3.5688 L12: -0.7605
REMARK 3 L13: 2.0796 L23: -0.6864
REMARK 3 S TENSOR
REMARK 3 S11: -0.0224 S12: -0.2139 S13: 0.0957
REMARK 3 S21: 0.1970 S22: 0.0910 S23: 0.3379
REMARK 3 S31: -0.2642 S32: -0.2421 S33: -0.0810
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'A' AND ( RESID 470 THROUGH 487 )
REMARK 3 ORIGIN FOR THE GROUP (A): -16.5919 -32.3144 4.3573
REMARK 3 T TENSOR
REMARK 3 T11: 0.1729 T22: 0.2118
REMARK 3 T33: 0.2381 T12: 0.0063
REMARK 3 T13: -0.0326 T23: -0.0024
REMARK 3 L TENSOR
REMARK 3 L11: 2.2041 L22: 3.8835
REMARK 3 L33: 6.4748 L12: -1.1535
REMARK 3 L13: -1.7884 L23: 3.6194
REMARK 3 S TENSOR
REMARK 3 S11: -0.0403 S12: -0.3066 S13: -0.0445
REMARK 3 S21: 0.1051 S22: 0.2263 S23: -0.3776
REMARK 3 S31: -0.0336 S32: 0.4541 S33: -0.1947
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'A' AND ( RESID 488 THROUGH 528 )
REMARK 3 ORIGIN FOR THE GROUP (A): -26.2653 -40.5580 1.2941
REMARK 3 T TENSOR
REMARK 3 T11: 0.2050 T22: 0.1460
REMARK 3 T33: 0.2011 T12: 0.0208
REMARK 3 T13: 0.0276 T23: -0.0350
REMARK 3 L TENSOR
REMARK 3 L11: 1.8074 L22: 2.0783
REMARK 3 L33: 1.4114 L12: 0.8509
REMARK 3 L13: -0.0440 L23: -1.0259
REMARK 3 S TENSOR
REMARK 3 S11: 0.1078 S12: -0.1533 S13: 0.0997
REMARK 3 S21: 0.2171 S22: -0.0128 S23: 0.0910
REMARK 3 S31: -0.0570 S32: -0.0282 S33: -0.0883
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 4ZQP COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-MAY-15.
REMARK 100 THE DEPOSITION ID IS D_1000209724.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 14-APR-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.2
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 19-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97899
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL MONOCHRIMATOR
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 : HKL-3000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 25094
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900
REMARK 200 RESOLUTION RANGE LOW (A) : 35.760
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.0
REMARK 200 DATA REDUNDANCY : 3.800
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.10300
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 14.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.93
REMARK 200 COMPLETENESS FOR SHELL (%) : 78.3
REMARK 200 DATA REDUNDANCY IN SHELL : 1.90
REMARK 200 R MERGE FOR SHELL (I) : 0.53600
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.840
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: HKL-3000, MOLREP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 37.79
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.98
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M NA/K PHOSPHATE PH 6.2, 25 %(V/V)
REMARK 280 1,2 PROPANDIOL, 10 %(V/V) GLYCEROL, VAPOR DIFFUSION, SITTING
REMARK 280 DROP, TEMPERATURE 289K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 4
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 -Y,X,Z
REMARK 290 4555 Y,-X,Z
REMARK 290 5555 X+1/2,Y+1/2,Z+1/2
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -Y+1/2,X+1/2,Z+1/2
REMARK 290 8555 Y+1/2,-X+1/2,Z+1/2
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 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 44.11250
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 44.11250
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 42.31500
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 44.11250
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 44.11250
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 42.31500
REMARK 290 SMTRY1 7 0.000000 -1.000000 0.000000 44.11250
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 44.11250
REMARK 290 SMTRY3 7 0.000000 0.000000 1.000000 42.31500
REMARK 290 SMTRY1 8 0.000000 1.000000 0.000000 44.11250
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 44.11250
REMARK 290 SMTRY3 8 0.000000 0.000000 1.000000 42.31500
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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 28010 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 42780 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -149.0 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 350 BIOMT1 2 -1.000000 0.000000 0.000000 -88.22500
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 -88.22500
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 3 0.000000 -1.000000 0.000000 -88.22500
REMARK 350 BIOMT2 3 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT3 3 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 4 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT2 4 -1.000000 0.000000 0.000000 -88.22500
REMARK 350 BIOMT3 4 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 SER A -2
REMARK 465 ASN A -1
REMARK 465 ALA A 0
REMARK 465 MET A 1
REMARK 465 SER A 2
REMARK 465 ARG A 3
REMARK 465 GLY A 4
REMARK 465 MET A 5
REMARK 465 SER A 6
REMARK 465 GLY A 7
REMARK 465 LEU A 8
REMARK 465 GLU A 9
REMARK 465 ASP A 10
REMARK 465 SER A 11
REMARK 465 SER A 12
REMARK 465 ASP A 13
REMARK 465 LEU A 14
REMARK 465 VAL A 15
REMARK 465 VAL A 16
REMARK 465 SER A 17
REMARK 465 PRO A 18
REMARK 465 TYR A 19
REMARK 465 VAL A 20
REMARK 465 ARG A 21
REMARK 465 MET A 22
REMARK 465 GLY A 23
REMARK 465 GLY A 24
REMARK 465 LEU A 25
REMARK 465 THR A 26
REMARK 465 THR A 27
REMARK 465 GLY A 432
REMARK 465 ARG A 433
REMARK 465 GLY A 434
REMARK 465 GLY A 435
REMARK 465 ALA A 436
REMARK 465 THR A 437
REMARK 465 SER A 438
REMARK 465 TYR A 439
REMARK 465 SER A 440
REMARK 465 LYS A 441
REMARK 465 ASP A 442
REMARK 465 ARG A 443
REMARK 465 TYR A 444
REMARK 465 PHE A 445
REMARK 465 ALA A 446
REMARK 465 ASP A 447
REMARK 465 ASP A 448
REMARK 465 ALA A 449
REMARK 465 LEU A 450
REMARK 465 SER A 451
REMARK 465 GLU A 452
REMARK 465 ASP A 453
REMARK 465 ARG A 529
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 46 -166.97 -126.45
REMARK 500 PRO A 79 49.06 -84.98
REMARK 500 VAL A 88 -54.98 -131.17
REMARK 500 GLU A 90 -160.65 -115.02
REMARK 500 ALA A 315 10.37 -142.49
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 K A 603 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLY A 336 O
REMARK 620 2 GLY A 338 O 97.6
REMARK 620 3 CYS A 341 O 110.3 91.0
REMARK 620 4 GLU A 511 O 105.6 84.8 144.2
REMARK 620 5 SER A 512 O 104.9 77.7 144.2 7.2
REMARK 620 6 HIS A 513 O 112.0 80.9 137.7 7.2 8.0
REMARK 620 7 HOH A 769 O 54.0 126.3 65.8 141.6 146.5 148.0
REMARK 620 N 1 2 3 4 5 6
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue IMP A 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue KP3 A 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue K A 603
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 A 604
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 605
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PGO A 606
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4ZQM RELATED DB: PDB
REMARK 900 THE SAME PROTEIN IN THE COMPLEX WITH XMP AND NAD
REMARK 900 RELATED ID: 4ZQN RELATED DB: PDB
REMARK 900 THE SAME PROTEIN IN THE COMPLEX WITH IMP AND THE INHIBITOR P41
REMARK 900 RELATED ID: 4ZQO RELATED DB: PDB
REMARK 900 THE SAME PROTEIN IN THE COMPLEX WITH IMP AND THE INHIBITOR Q67
REMARK 900 RELATED ID: CSGID-IDP91646 RELATED DB: TARGETTRACK
DBREF 4ZQP A 1 125 UNP P9WKI7 IMDH_MYCTU 1 125
DBREF 4ZQP A 253 529 UNP P9WKI7 IMDH_MYCTU 253 529
SEQADV 4ZQP SER A -2 UNP P9WKI7 EXPRESSION TAG
SEQADV 4ZQP ASN A -1 UNP P9WKI7 EXPRESSION TAG
SEQADV 4ZQP ALA A 0 UNP P9WKI7 EXPRESSION TAG
SEQADV 4ZQP GLY A 126 UNP P9WKI7 LINKER
SEQADV 4ZQP GLY A 127 UNP P9WKI7 LINKER
SEQRES 1 A 407 SER ASN ALA MET SER ARG GLY MET SER GLY LEU GLU ASP
SEQRES 2 A 407 SER SER ASP LEU VAL VAL SER PRO TYR VAL ARG MET GLY
SEQRES 3 A 407 GLY LEU THR THR ASP PRO VAL PRO THR GLY GLY ASP ASP
SEQRES 4 A 407 PRO HIS LYS VAL ALA MET LEU GLY LEU THR PHE ASP ASP
SEQRES 5 A 407 VAL LEU LEU LEU PRO ALA ALA SER ASP VAL VAL PRO ALA
SEQRES 6 A 407 THR ALA ASP THR SER SER GLN LEU THR LYS LYS ILE ARG
SEQRES 7 A 407 LEU LYS VAL PRO LEU VAL SER SER ALA MET ASP THR VAL
SEQRES 8 A 407 THR GLU SER ARG MET ALA ILE ALA MET ALA ARG ALA GLY
SEQRES 9 A 407 GLY MET GLY VAL LEU HIS ARG ASN LEU PRO VAL ALA GLU
SEQRES 10 A 407 GLN ALA GLY GLN VAL GLU MET VAL LYS ARG SER GLY GLY
SEQRES 11 A 407 LEU LEU VAL GLY ALA ALA VAL GLY VAL GLY GLY ASP ALA
SEQRES 12 A 407 TRP VAL ARG ALA MET MET LEU VAL ASP ALA GLY VAL ASP
SEQRES 13 A 407 VAL LEU VAL VAL ASP THR ALA HIS ALA HIS ASN ARG LEU
SEQRES 14 A 407 VAL LEU ASP MET VAL GLY LYS LEU LYS SER GLU VAL GLY
SEQRES 15 A 407 ASP ARG VAL GLU VAL VAL GLY GLY ASN VAL ALA THR ARG
SEQRES 16 A 407 SER ALA ALA ALA ALA LEU VAL ASP ALA GLY ALA ASP ALA
SEQRES 17 A 407 VAL LYS VAL GLY VAL GLY PRO GLY SER ILE CYS THR THR
SEQRES 18 A 407 ARG VAL VAL ALA GLY VAL GLY ALA PRO GLN ILE THR ALA
SEQRES 19 A 407 ILE LEU GLU ALA VAL ALA ALA CYS ARG PRO ALA GLY VAL
SEQRES 20 A 407 PRO VAL ILE ALA ASP GLY GLY LEU GLN TYR SER GLY ASP
SEQRES 21 A 407 ILE ALA LYS ALA LEU ALA ALA GLY ALA SER THR ALA MET
SEQRES 22 A 407 LEU GLY SER LEU LEU ALA GLY THR ALA GLU ALA PRO GLY
SEQRES 23 A 407 GLU LEU ILE PHE VAL ASN GLY LYS GLN TYR LYS SER TYR
SEQRES 24 A 407 ARG GLY MET GLY SER LEU GLY ALA MET ARG GLY ARG GLY
SEQRES 25 A 407 GLY ALA THR SER TYR SER LYS ASP ARG TYR PHE ALA ASP
SEQRES 26 A 407 ASP ALA LEU SER GLU ASP LYS LEU VAL PRO GLU GLY ILE
SEQRES 27 A 407 GLU GLY ARG VAL PRO PHE ARG GLY PRO LEU SER SER VAL
SEQRES 28 A 407 ILE HIS GLN LEU THR GLY GLY LEU ARG ALA ALA MET GLY
SEQRES 29 A 407 TYR THR GLY SER PRO THR ILE GLU VAL LEU GLN GLN ALA
SEQRES 30 A 407 GLN PHE VAL ARG ILE THR PRO ALA GLY LEU LYS GLU SER
SEQRES 31 A 407 HIS PRO HIS ASP VAL ALA MET THR VAL GLU ALA PRO ASN
SEQRES 32 A 407 TYR TYR ALA ARG
HET IMP A 601 23
HET KP3 A 602 44
HET K A 603 1
HET PO4 A 604 5
HET GOL A 605 6
HET PGO A 606 5
HETNAM IMP INOSINIC ACID
HETNAM KP3 5'-O-({1-[(2E)-4-(4-HYDROXY-6-METHOXY-7-METHYL-3-OXO-1,
HETNAM 2 KP3 3-DIHYDRO-2-BENZOFURAN-5-YL)-2-METHYLBUT-2-EN-1-YL]-
HETNAM 3 KP3 1H-1,2,3-TRIAZOL-4-YL}METHYL)ADENOSINE
HETNAM K POTASSIUM ION
HETNAM PO4 PHOSPHATE ION
HETNAM GOL GLYCEROL
HETNAM PGO S-1,2-PROPANEDIOL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 2 IMP C10 H13 N4 O8 P
FORMUL 3 KP3 C28 H32 N8 O8
FORMUL 4 K K 1+
FORMUL 5 PO4 O4 P 3-
FORMUL 6 GOL C3 H8 O3
FORMUL 7 PGO C3 H8 O2
FORMUL 8 HOH *169(H2 O)
HELIX 1 AA1 THR A 46 ASP A 48 5 3
HELIX 2 AA2 VAL A 60 ALA A 64 5 5
HELIX 3 AA3 GLU A 90 ALA A 100 1 11
HELIX 4 AA4 PRO A 111 ARG A 124 1 14
HELIX 5 AA5 GLY A 262 GLY A 276 1 15
HELIX 6 AA6 ASN A 289 GLY A 304 1 16
HELIX 7 AA7 THR A 316 GLY A 327 1 12
HELIX 8 AA8 THR A 342 ALA A 347 1 6
HELIX 9 AA9 PRO A 352 ARG A 365 1 14
HELIX 10 AB1 PRO A 366 GLY A 368 5 3
HELIX 11 AB2 TYR A 379 ALA A 389 1 11
HELIX 12 AB3 GLY A 397 GLY A 402 1 6
HELIX 13 AB4 SER A 426 ARG A 431 1 6
HELIX 14 AB5 PRO A 469 GLY A 489 1 21
HELIX 15 AB6 THR A 492 GLN A 497 1 6
HELIX 16 AB7 THR A 505 HIS A 513 1 9
SHEET 1 AA1 2 VAL A 50 LEU A 52 0
SHEET 2 AA1 2 PHE A 501 ARG A 503 -1 O VAL A 502 N LEU A 51
SHEET 1 AA2 2 SER A 68 GLN A 69 0
SHEET 2 AA2 2 ARG A 75 LEU A 76 -1 O LEU A 76 N SER A 68
SHEET 1 AA3 9 LEU A 80 SER A 82 0
SHEET 2 AA3 9 MET A 103 LEU A 106 1 O MET A 103 N SER A 82
SHEET 3 AA3 9 GLY A 256 VAL A 259 1 O ALA A 258 N LEU A 106
SHEET 4 AA3 9 VAL A 279 ASP A 283 1 O ASP A 283 N VAL A 259
SHEET 5 AA3 9 GLU A 308 VAL A 314 1 O VAL A 310 N LEU A 280
SHEET 6 AA3 9 ALA A 330 VAL A 333 1 O LYS A 332 N GLY A 311
SHEET 7 AA3 9 VAL A 371 ASP A 374 1 O ILE A 372 N VAL A 333
SHEET 8 AA3 9 THR A 393 LEU A 396 1 O THR A 393 N ALA A 373
SHEET 9 AA3 9 LEU A 80 SER A 82 1 N VAL A 81 O LEU A 396
SHEET 1 AA4 3 LEU A 410 VAL A 413 0
SHEET 2 AA4 3 LYS A 416 ARG A 422 -1 O TYR A 418 N ILE A 411
SHEET 3 AA4 3 GLU A 461 PRO A 465 -1 O VAL A 464 N LYS A 419
LINK O GLY A 336 K K A 603 1555 1555 2.81
LINK O GLY A 338 K K A 603 1555 1555 2.66
LINK O CYS A 341 K K A 603 1555 1555 2.88
LINK O GLU A 511 K K A 603 1555 4545 2.72
LINK O SER A 512 K K A 603 1555 4545 2.90
LINK O HIS A 513 K K A 603 1555 4545 2.94
LINK K K A 603 O HOH A 769 1555 1555 3.24
CISPEP 1 GLY A 312 ASN A 313 0 0.55
SITE 1 AC1 24 SER A 83 MET A 85 GLY A 338 SER A 339
SITE 2 AC1 24 ILE A 340 CYS A 341 ASP A 374 GLY A 375
SITE 3 AC1 24 GLY A 376 MET A 395 GLY A 397 SER A 398
SITE 4 AC1 24 TYR A 421 GLY A 423 MET A 424 GLY A 425
SITE 5 AC1 24 GLU A 458 GLY A 459 KP3 A 602 HOH A 717
SITE 6 AC1 24 HOH A 744 HOH A 763 HOH A 807 HOH A 828
SITE 1 AC2 20 VAL A 59 ARG A 108 VAL A 261 ASP A 283
SITE 2 AC2 20 THR A 284 ALA A 285 ASN A 289 ASN A 313
SITE 3 AC2 20 GLY A 334 VAL A 335 GLY A 336 CYS A 341
SITE 4 AC2 20 THR A 343 MET A 424 GLY A 425 GLU A 458
SITE 5 AC2 20 ALA A 483 GLY A 486 TYR A 487 IMP A 601
SITE 1 AC3 6 GLY A 336 GLY A 338 CYS A 341 GLU A 511
SITE 2 AC3 6 SER A 512 HIS A 513
SITE 1 AC4 4 LEU A 399 PRO A 524 TYR A 527 HOH A 706
SITE 1 AC5 9 ASP A 48 GLN A 378 TYR A 379 ASP A 382
SITE 2 AC5 9 LYS A 510 HIS A 515 ASP A 516 HOH A 709
SITE 3 AC5 9 HOH A 778
SITE 1 AC6 7 ASP A 48 ASP A 49 THR A 505 PRO A 506
SITE 2 AC6 7 ALA A 507 LEU A 509 HOH A 868
CRYST1 88.225 88.225 84.630 90.00 90.00 90.00 I 4 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 0.011335 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011335 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011816 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
