HEADER TRANSFERASE/TRANSFERASE INHIBITOR 05-FEB-15 4Y0A
TITLE SHIKIMATE KINASE FROM ACINETOBACTER BAUMANNII IN COMPLEX WITH
TITLE 2 SHIKIMATE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SHIKIMATE KINASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: SK;
COMPND 5 EC: 2.7.1.71;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ACINETOBACTER BAUMANNII;
SOURCE 3 ORGANISM_TAXID: 557600;
SOURCE 4 STRAIN: AB307-0294;
SOURCE 5 GENE: AROK, ABBFA_000324;
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: PET-SUMO
KEYWDS SHIKIMATE PATHWAY, TRANSFERASE, NUCLEOSIDE MONOPHOSPHATE (NMP) KINASE
KEYWDS 2 FAMILY, AMINO ACID BIOSYNTHESIS, ATP-BINDING, KINASE, NUCLEOTIDE
KEYWDS 3 BINDING, TRANSFERASE-TRANSFERASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR K.A.SUTTON,J.BREEN,U.MACDONALD,J.M.BEANAN,R.OLSON,T.A.RUSSO,
AUTHOR 2 L.W.SCHULTZ,T.C.UMLAND
REVDAT 5 27-SEP-23 4Y0A 1 REMARK
REVDAT 4 27-NOV-19 4Y0A 1 REMARK
REVDAT 3 10-APR-19 4Y0A 1 REMARK
REVDAT 2 07-OCT-15 4Y0A 1 REMARK
REVDAT 1 12-AUG-15 4Y0A 0
JRNL AUTH K.A.SUTTON,J.BREEN,U.MACDONALD,J.M.BEANAN,R.OLSON,T.A.RUSSO,
JRNL AUTH 2 L.W.SCHULTZ,T.C.UMLAND
JRNL TITL STRUCTURE OF SHIKIMATE KINASE, AN IN VIVO ESSENTIAL
JRNL TITL 2 METABOLIC ENZYME IN THE NOSOCOMIAL PATHOGEN ACINETOBACTER
JRNL TITL 3 BAUMANNII, IN COMPLEX WITH SHIKIMATE.
JRNL REF ACTA CRYSTALLOGR.,SECT.D V. 71 1736 2015
JRNL REFN ESSN 1399-0047
JRNL PMID 26249354
JRNL DOI 10.1107/S139900471501189X
REMARK 2
REMARK 2 RESOLUTION. 1.91 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) : 1.91
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 36.02
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.370
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.0
REMARK 3 NUMBER OF REFLECTIONS : 30524
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.194
REMARK 3 R VALUE (WORKING SET) : 0.192
REMARK 3 FREE R VALUE : 0.235
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.940
REMARK 3 FREE R VALUE TEST SET COUNT : 1507
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 36.0268 - 4.2479 0.98 2799 136 0.1975 0.2378
REMARK 3 2 4.2479 - 3.3725 0.99 2709 140 0.1817 0.2373
REMARK 3 3 3.3725 - 2.9464 0.99 2675 142 0.2025 0.2350
REMARK 3 4 2.9464 - 2.6771 0.99 2647 139 0.1970 0.2345
REMARK 3 5 2.6771 - 2.4853 0.98 2607 142 0.1757 0.2350
REMARK 3 6 2.4853 - 2.3388 0.98 2630 141 0.1779 0.2227
REMARK 3 7 2.3388 - 2.2217 0.98 2605 138 0.1766 0.2171
REMARK 3 8 2.2217 - 2.1250 0.98 2613 131 0.1741 0.2099
REMARK 3 9 2.1250 - 2.0432 0.98 2567 147 0.1876 0.2388
REMARK 3 10 2.0432 - 1.9727 0.97 2606 134 0.2152 0.2455
REMARK 3 11 1.9727 - 1.9110 0.96 2559 117 0.2532 0.3035
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) : 0.210
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 22.550
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 32.28
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 46.41
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 : 0.020 1484
REMARK 3 ANGLE : 1.658 2008
REMARK 3 CHIRALITY : 0.083 229
REMARK 3 PLANARITY : 0.009 256
REMARK 3 DIHEDRAL : 15.399 571
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 9
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 11 THROUGH 44 )
REMARK 3 ORIGIN FOR THE GROUP (A): -11.3427 11.7403 8.9187
REMARK 3 T TENSOR
REMARK 3 T11: 0.3564 T22: 0.3141
REMARK 3 T33: 0.3303 T12: 0.0077
REMARK 3 T13: -0.0679 T23: 0.0161
REMARK 3 L TENSOR
REMARK 3 L11: 2.4244 L22: 2.6858
REMARK 3 L33: 1.4329 L12: 0.9177
REMARK 3 L13: 1.4799 L23: 0.0013
REMARK 3 S TENSOR
REMARK 3 S11: -0.0338 S12: -0.1628 S13: 0.1291
REMARK 3 S21: -0.2342 S22: 0.0265 S23: 0.4326
REMARK 3 S31: -0.0900 S32: -0.1878 S33: 0.0205
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 45 THROUGH 60 )
REMARK 3 ORIGIN FOR THE GROUP (A): -5.1119 14.4700 23.4128
REMARK 3 T TENSOR
REMARK 3 T11: 0.3933 T22: 0.2943
REMARK 3 T33: 0.2621 T12: 0.0111
REMARK 3 T13: -0.0213 T23: -0.0022
REMARK 3 L TENSOR
REMARK 3 L11: 7.9535 L22: 4.2239
REMARK 3 L33: 5.8120 L12: 2.3609
REMARK 3 L13: 6.0175 L23: 1.6318
REMARK 3 S TENSOR
REMARK 3 S11: -0.1118 S12: -0.4414 S13: 0.2614
REMARK 3 S21: 0.6040 S22: -0.2394 S23: 0.2328
REMARK 3 S31: -0.6281 S32: -0.7761 S33: 0.2828
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 61 THROUGH 86 )
REMARK 3 ORIGIN FOR THE GROUP (A): 0.7747 7.3046 27.0732
REMARK 3 T TENSOR
REMARK 3 T11: 0.2942 T22: 0.2665
REMARK 3 T33: 0.2426 T12: -0.0298
REMARK 3 T13: -0.0006 T23: 0.0586
REMARK 3 L TENSOR
REMARK 3 L11: 7.8622 L22: 5.9975
REMARK 3 L33: 8.0367 L12: 1.5669
REMARK 3 L13: 4.3251 L23: -1.0640
REMARK 3 S TENSOR
REMARK 3 S11: 0.1225 S12: -0.4240 S13: -0.0414
REMARK 3 S21: 0.6222 S22: -0.0178 S23: 0.0132
REMARK 3 S31: -0.3108 S32: 0.0514 S33: -0.0862
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 87 THROUGH 110 )
REMARK 3 ORIGIN FOR THE GROUP (A): -5.5600 1.8182 17.0272
REMARK 3 T TENSOR
REMARK 3 T11: 0.3124 T22: 0.2757
REMARK 3 T33: 0.3107 T12: -0.0543
REMARK 3 T13: -0.0706 T23: 0.0467
REMARK 3 L TENSOR
REMARK 3 L11: 7.7080 L22: 4.5323
REMARK 3 L33: 2.3399 L12: -1.8720
REMARK 3 L13: 2.1316 L23: -2.7445
REMARK 3 S TENSOR
REMARK 3 S11: 0.1276 S12: -0.4050 S13: -0.6410
REMARK 3 S21: -0.2463 S22: 0.1508 S23: 0.5308
REMARK 3 S31: 0.3074 S32: -0.2822 S33: -0.2031
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 111 THROUGH 127 )
REMARK 3 ORIGIN FOR THE GROUP (A): 3.4102 9.1271 6.8779
REMARK 3 T TENSOR
REMARK 3 T11: 0.3780 T22: 0.2537
REMARK 3 T33: 0.2010 T12: 0.0406
REMARK 3 T13: 0.0174 T23: -0.0097
REMARK 3 L TENSOR
REMARK 3 L11: 4.7723 L22: 6.1893
REMARK 3 L33: 1.8112 L12: 3.5277
REMARK 3 L13: 0.7438 L23: -0.4651
REMARK 3 S TENSOR
REMARK 3 S11: -0.4182 S12: 0.3755 S13: 0.0376
REMARK 3 S21: -1.1496 S22: 0.3146 S23: -0.0581
REMARK 3 S31: 0.0316 S32: 0.2671 S33: 0.1306
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 128 THROUGH 141 )
REMARK 3 ORIGIN FOR THE GROUP (A): 13.5241 16.6249 17.6357
REMARK 3 T TENSOR
REMARK 3 T11: 0.3270 T22: 0.4652
REMARK 3 T33: 0.4619 T12: -0.0420
REMARK 3 T13: -0.0301 T23: 0.0716
REMARK 3 L TENSOR
REMARK 3 L11: 0.5377 L22: 7.5245
REMARK 3 L33: 8.3860 L12: -0.1615
REMARK 3 L13: -0.1060 L23: -1.9712
REMARK 3 S TENSOR
REMARK 3 S11: -0.0586 S12: -0.5418 S13: -0.0220
REMARK 3 S21: 0.3408 S22: -0.0694 S23: -0.4103
REMARK 3 S31: -0.2992 S32: 0.3315 S33: 0.0409
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 142 THROUGH 160 )
REMARK 3 ORIGIN FOR THE GROUP (A): 10.0966 2.8940 10.4252
REMARK 3 T TENSOR
REMARK 3 T11: 0.4216 T22: 0.3763
REMARK 3 T33: 0.4210 T12: 0.1337
REMARK 3 T13: 0.0690 T23: 0.0559
REMARK 3 L TENSOR
REMARK 3 L11: 3.9680 L22: 8.6415
REMARK 3 L33: 5.1250 L12: 2.7007
REMARK 3 L13: 2.1177 L23: 1.9085
REMARK 3 S TENSOR
REMARK 3 S11: 0.1140 S12: -0.0011 S13: -0.7645
REMARK 3 S21: -0.3541 S22: -0.1189 S23: -0.9997
REMARK 3 S31: 0.6223 S32: 0.5363 S33: -0.0215
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 161 THROUGH 171 )
REMARK 3 ORIGIN FOR THE GROUP (A): -0.9020 7.8701 1.2335
REMARK 3 T TENSOR
REMARK 3 T11: 0.7973 T22: 0.4481
REMARK 3 T33: 0.4055 T12: -0.0399
REMARK 3 T13: 0.0306 T23: -0.0463
REMARK 3 L TENSOR
REMARK 3 L11: 9.0495 L22: 4.0446
REMARK 3 L33: 6.6745 L12: 5.1588
REMARK 3 L13: -0.8791 L23: -1.7209
REMARK 3 S TENSOR
REMARK 3 S11: -0.3390 S12: 1.3554 S13: -0.2063
REMARK 3 S21: -1.3212 S22: 0.6031 S23: -0.6458
REMARK 3 S31: -0.2767 S32: 0.1443 S33: -0.1712
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 172 THROUGH 189 )
REMARK 3 ORIGIN FOR THE GROUP (A): -11.5682 8.6676 -1.2347
REMARK 3 T TENSOR
REMARK 3 T11: 0.5196 T22: 0.4119
REMARK 3 T33: 0.3867 T12: 0.0595
REMARK 3 T13: -0.1275 T23: -0.0185
REMARK 3 L TENSOR
REMARK 3 L11: 9.2402 L22: 6.0288
REMARK 3 L33: 5.2060 L12: 5.0755
REMARK 3 L13: 4.5171 L23: 3.7944
REMARK 3 S TENSOR
REMARK 3 S11: -0.1121 S12: 0.6336 S13: -0.4783
REMARK 3 S21: -0.6800 S22: 0.2314 S23: 0.2975
REMARK 3 S31: 0.1946 S32: 0.2905 S33: -0.1318
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 4Y0A COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-FEB-15.
REMARK 100 THE DEPOSITION ID IS D_1000206634.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 08-AUG-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 23-ID-B
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.033
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 300 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : SCALA 3.3.20
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 30525
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.911
REMARK 200 RESOLUTION RANGE LOW (A) : 36.020
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.2
REMARK 200 DATA REDUNDANCY : 6.100
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.07200
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 12.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.91
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.01
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.9
REMARK 200 DATA REDUNDANCY IN SHELL : 6.10
REMARK 200 R MERGE FOR SHELL (I) : 0.43600
REMARK 200 R SYM FOR SHELL (I) : 0.43600
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.800
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: 1KAG
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 74.73
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.87
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M HEPES, 1.5M LITHIUM SULFATE, PH
REMARK 280 7.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 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 5555 X+1/2,Y+1/2,Z+1/2
REMARK 290 6555 -X,-Y+1/2,Z
REMARK 290 7555 -X+1/2,Y,-Z
REMARK 290 8555 X,-Y,-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 40.99000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 56.36000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 42.90500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 56.36000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 40.99000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 42.90500
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 40.99000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 42.90500
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 56.36000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 42.90500
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 40.99000
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 56.36000
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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A 364 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 434 LIES ON A SPECIAL POSITION.
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 HH TYR A 163 O HOH A 302 1.42
REMARK 500 OG1 THR A 167 O HOH A 301 2.08
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 A 111 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 ARG A 111 NE - CZ - NH2 ANGL. DEV. = -3.4 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 SER A 12 36.77 -94.67
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A 459 DISTANCE = 6.61 ANGSTROMS
REMARK 525 HOH A 460 DISTANCE = 6.95 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SKM A 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 203
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 204
DBREF 4Y0A A 11 189 UNP B7GVP4 B7GVP4_ACIB3 11 189
SEQRES 1 A 179 PRO SER LYS ALA PHE GLU THR LEU PRO ASN ILE TYR LEU
SEQRES 2 A 179 VAL GLY PRO MET GLY ALA GLY LYS THR THR VAL GLY ARG
SEQRES 3 A 179 HIS LEU ALA GLU LEU LEU GLY ARG GLU PHE LEU ASP SER
SEQRES 4 A 179 ASP HIS GLU ILE GLU ARG LYS THR GLY ALA THR ILE PRO
SEQRES 5 A 179 TRP ILE PHE GLU LYS GLU GLY GLU VAL GLY PHE ARG THR
SEQRES 6 A 179 ARG GLU THR VAL VAL LEU ASN GLU LEU THR SER ARG LYS
SEQRES 7 A 179 ALA LEU VAL LEU ALA THR GLY GLY GLY ALA ILE THR GLN
SEQRES 8 A 179 ALA PRO ASN ARG GLU PHE LEU LYS GLN ARG GLY ILE VAL
SEQRES 9 A 179 VAL TYR LEU TYR THR PRO VAL GLU LEU GLN LEU GLN ARG
SEQRES 10 A 179 THR TYR ARG ASP LYS ASN ARG PRO LEU LEU GLN VAL GLU
SEQRES 11 A 179 ASN PRO GLU GLN LYS LEU ARG ASP LEU LEU LYS ILE ARG
SEQRES 12 A 179 ASP PRO LEU TYR ARG GLU VAL ALA HIS TYR THR ILE GLU
SEQRES 13 A 179 THR ASN GLN GLY ALA ALA ARG ASP LEU ALA GLN LYS ILE
SEQRES 14 A 179 LEU GLN LEU ILE LEU SER ASN LYS LEU LYS
HET SKM A 201 21
HET SO4 A 202 5
HET SO4 A 203 5
HET SO4 A 204 5
HETNAM SKM (3R,4S,5R)-3,4,5-TRIHYDROXYCYCLOHEX-1-ENE-1-CARBOXYLIC
HETNAM 2 SKM ACID
HETNAM SO4 SULFATE ION
HETSYN SKM SHIKIMATE
FORMUL 2 SKM C7 H10 O5
FORMUL 3 SO4 3(O4 S 2-)
FORMUL 6 HOH *160(H2 O)
HELIX 1 AA1 SER A 12 GLU A 16 5 5
HELIX 2 AA2 GLY A 30 GLY A 43 1 14
HELIX 3 AA3 SER A 49 GLY A 58 1 10
HELIX 4 AA4 THR A 60 THR A 85 1 26
HELIX 5 AA5 GLY A 97 THR A 100 5 4
HELIX 6 AA6 GLN A 101 GLY A 112 1 12
HELIX 7 AA7 PRO A 120 THR A 128 1 9
HELIX 8 AA8 ARG A 134 GLN A 138 5 5
HELIX 9 AA9 ASN A 141 ALA A 161 1 21
HELIX 10 AB1 ALA A 171 LYS A 189 1 19
SHEET 1 AA1 5 GLU A 45 ASP A 48 0
SHEET 2 AA1 5 LEU A 90 ALA A 93 1 O ALA A 93 N LEU A 47
SHEET 3 AA1 5 ILE A 21 VAL A 24 1 N ILE A 21 O LEU A 92
SHEET 4 AA1 5 ILE A 113 TYR A 118 1 O VAL A 115 N TYR A 22
SHEET 5 AA1 5 TYR A 163 GLU A 166 1 O ILE A 165 N TYR A 116
SITE 1 AC1 14 MET A 27 ASP A 50 PHE A 73 ARG A 74
SITE 2 AC1 14 GLY A 96 GLY A 97 PRO A 135 LEU A 136
SITE 3 AC1 14 ARG A 153 HOH A 337 HOH A 350 HOH A 352
SITE 4 AC1 14 HOH A 355 HOH A 361
SITE 1 AC2 6 PRO A 120 VAL A 121 GLU A 122 ARG A 147
SITE 2 AC2 6 HOH A 307 HOH A 343
SITE 1 AC3 10 PRO A 26 GLY A 28 ALA A 29 GLY A 30
SITE 2 AC3 10 LYS A 31 THR A 32 ARG A 134 HOH A 311
SITE 3 AC3 10 HOH A 338 HOH A 368
SITE 1 AC4 10 HIS A 37 ARG A 127 GLN A 169 GLY A 170
SITE 2 AC4 10 ALA A 171 ALA A 172 ARG A 173 HOH A 364
SITE 3 AC4 10 HOH A 376 HOH A 410
CRYST1 81.980 85.810 112.720 90.00 90.00 90.00 I 21 21 21 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 0.012198 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011654 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008872 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
