HEADER TRANSFERASE 31-OCT-09 3KHY
TITLE CRYSTAL STRUCTURE OF A PROPIONATE KINASE FROM FRANCISELLA TULARENSIS
TITLE 2 SUBSP. TULARENSIS SCHU S4
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROPIONATE KINASE;
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 2.7.2.-;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: FRANCISELLA TULARENSIS SUBSP. TULARENSIS;
SOURCE 3 ORGANISM_TAXID: 119856;
SOURCE 4 GENE: FTT1753, FTT_1753, TDCD;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21-CODONPLUS(DE3)-RIPL;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PMCSG7
KEYWDS PROPIONATE KINASE, CSGID, IDP01739, ATP-BINDING, KINASE, NUCLEOTIDE-
KEYWDS 2 BINDING, TRANSFERASE, STRUCTURAL GENOMICS, NATIONAL INSTITUTE OF
KEYWDS 3 ALLERGY AND INFECTIOUS DISEASES, NATIONAL INSTITUTES OF HEALTH,
KEYWDS 4 DEPARTMENT OF HEALTH AND HUMAN SERVICES, CENTER FOR STRUCTURAL
KEYWDS 5 GENOMICS OF INFECTIOUS DISEASES
EXPDTA X-RAY DIFFRACTION
AUTHOR J.S.BRUNZELLE,T.SKARINA,S.SHARMA,Y.WANG,A.SAVCHENKO,W.F.ANDERSON,
AUTHOR 2 CENTER FOR STRUCTURAL GENOMICS OF INFECTIOUS DISEASES (CSGID)
REVDAT 2 01-OCT-14 3KHY 1 AUTHOR JRNL VERSN
REVDAT 1 19-JAN-10 3KHY 0
JRNL AUTH J.S.BRUNZELLE,S.S.SHARMA,T.SKARINA,Y.WANG,A.SAVCHENKO,
JRNL AUTH 2 W.F.ANDERSON,
JRNL AUTH 3 CENTER FOR STRUCTURAL GENOMICS OF INFECTIOUS DISEASES
JRNL AUTH 4 (CSGID)
JRNL TITL CRYSTAL STRUCTURE OF A PROPIONATE KINASE FROM FRANCISELLA
JRNL TITL 2 TULARENSIS SUBSP. TULARENSIS SCHU S4
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.98 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.4_115)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-
REMARK 3 : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,
REMARK 3 : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL
REMARK 3 : MORIARTY,REETAL PAI,RANDY READ,JANE
REMARK 3 : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM
REMARK 3 : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,
REMARK 3 : LAURENT STORONI,TOM TERWILLIGER,PETER
REMARK 3 : ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.98
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 28.51
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.040
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.4
REMARK 3 NUMBER OF REFLECTIONS : 60374
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.155
REMARK 3 R VALUE (WORKING SET) : 0.155
REMARK 3 FREE R VALUE : 0.193
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.080
REMARK 3 FREE R VALUE TEST SET COUNT : 3066
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 28.5134 - 4.2579 1.00 6170 321 0.1533 0.1690
REMARK 3 2 4.2579 - 3.3814 1.00 5937 328 0.1343 0.1647
REMARK 3 3 3.3814 - 2.9545 1.00 5883 317 0.1721 0.2125
REMARK 3 4 2.9545 - 2.6846 1.00 5852 297 0.1827 0.2175
REMARK 3 5 2.6846 - 2.4923 0.99 5766 313 0.1615 0.2098
REMARK 3 6 2.4923 - 2.3454 0.98 5750 311 0.1492 0.2026
REMARK 3 7 2.3454 - 2.2280 0.98 5724 299 0.1410 0.1918
REMARK 3 8 2.2280 - 2.1310 0.97 5654 298 0.1436 0.2027
REMARK 3 9 2.1310 - 2.0490 0.96 5598 290 0.1482 0.1961
REMARK 3 10 2.0490 - 1.9780 0.86 4974 292 0.1639 0.2417
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 : 0.37
REMARK 3 B_SOL : 48.23
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.200
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : NULL
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 20.90
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 : 0.007 6080
REMARK 3 ANGLE : 1.011 8225
REMARK 3 CHIRALITY : 0.071 953
REMARK 3 PLANARITY : 0.004 1051
REMARK 3 DIHEDRAL : 16.764 2191
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 12
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: (chain A and resid 1:61)
REMARK 3 ORIGIN FOR THE GROUP (A): 40.7207 33.2013 67.8238
REMARK 3 T TENSOR
REMARK 3 T11: 0.3343 T22: 0.2106
REMARK 3 T33: 0.1543 T12: -0.0719
REMARK 3 T13: 0.0555 T23: -0.0230
REMARK 3 L TENSOR
REMARK 3 L11: 0.1045 L22: 0.5675
REMARK 3 L33: 0.9269 L12: -0.0967
REMARK 3 L13: 0.0262 L23: -0.0576
REMARK 3 S TENSOR
REMARK 3 S11: -0.2171 S12: -0.0738 S13: 0.1013
REMARK 3 S21: -0.1573 S22: 0.0157 S23: -0.0805
REMARK 3 S31: 0.5254 S32: -0.0736 S33: -0.0055
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: (chain A and resid 62:99)
REMARK 3 ORIGIN FOR THE GROUP (A): 45.5892 31.4784 76.8450
REMARK 3 T TENSOR
REMARK 3 T11: 0.3457 T22: 0.2110
REMARK 3 T33: 0.1809 T12: 0.1221
REMARK 3 T13: 0.0698 T23: -0.0161
REMARK 3 L TENSOR
REMARK 3 L11: 0.4807 L22: 0.6809
REMARK 3 L33: 0.5184 L12: -0.0187
REMARK 3 L13: -0.1759 L23: -0.1717
REMARK 3 S TENSOR
REMARK 3 S11: -0.2282 S12: -0.0720 S13: -0.1876
REMARK 3 S21: -0.0978 S22: 0.1159 S23: -0.1543
REMARK 3 S31: 0.7137 S32: 0.1872 S33: 0.0133
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: (chain A and resid 100:134)
REMARK 3 ORIGIN FOR THE GROUP (A): 39.2680 26.7510 85.3165
REMARK 3 T TENSOR
REMARK 3 T11: 0.6175 T22: 0.1543
REMARK 3 T33: 0.2701 T12: 0.0372
REMARK 3 T13: 0.1005 T23: 0.0082
REMARK 3 L TENSOR
REMARK 3 L11: 0.1389 L22: 0.3225
REMARK 3 L33: 0.8149 L12: 0.0920
REMARK 3 L13: 0.0455 L23: 0.1708
REMARK 3 S TENSOR
REMARK 3 S11: -0.2637 S12: -0.0755 S13: -0.3313
REMARK 3 S21: 0.0009 S22: -0.0233 S23: 0.0098
REMARK 3 S31: 0.8473 S32: -0.1576 S33: -0.0018
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: (chain A and resid 135:224)
REMARK 3 ORIGIN FOR THE GROUP (A): 36.0518 47.7072 91.0271
REMARK 3 T TENSOR
REMARK 3 T11: 0.1148 T22: 0.1266
REMARK 3 T33: 0.1155 T12: 0.0237
REMARK 3 T13: -0.0219 T23: 0.0128
REMARK 3 L TENSOR
REMARK 3 L11: 0.3123 L22: 0.3704
REMARK 3 L33: 0.9780 L12: -0.2913
REMARK 3 L13: -0.1879 L23: -0.2433
REMARK 3 S TENSOR
REMARK 3 S11: 0.0053 S12: -0.0457 S13: 0.0029
REMARK 3 S21: 0.0186 S22: -0.0021 S23: -0.0420
REMARK 3 S31: 0.1594 S32: 0.2369 S33: 0.0054
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: (chain A and resid 225:298)
REMARK 3 ORIGIN FOR THE GROUP (A): 15.5731 48.0464 79.4866
REMARK 3 T TENSOR
REMARK 3 T11: 0.1191 T22: 0.1553
REMARK 3 T33: 0.1271 T12: -0.0200
REMARK 3 T13: 0.0019 T23: -0.0134
REMARK 3 L TENSOR
REMARK 3 L11: 0.7740 L22: 0.3679
REMARK 3 L33: 0.5333 L12: -0.1778
REMARK 3 L13: -0.4589 L23: -0.2236
REMARK 3 S TENSOR
REMARK 3 S11: -0.0444 S12: 0.1505 S13: -0.0882
REMARK 3 S21: -0.0589 S22: -0.0339 S23: -0.0200
REMARK 3 S31: 0.1743 S32: -0.1236 S33: -0.0002
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: (chain A and resid 299:384)
REMARK 3 ORIGIN FOR THE GROUP (A): 35.5737 60.3796 80.5116
REMARK 3 T TENSOR
REMARK 3 T11: 0.0805 T22: 0.1345
REMARK 3 T33: 0.1248 T12: -0.0111
REMARK 3 T13: 0.0021 T23: 0.0056
REMARK 3 L TENSOR
REMARK 3 L11: 0.4646 L22: 0.1759
REMARK 3 L33: 0.9082 L12: -0.0775
REMARK 3 L13: -0.1839 L23: 0.0166
REMARK 3 S TENSOR
REMARK 3 S11: 0.0518 S12: 0.0246 S13: 0.0869
REMARK 3 S21: 0.0259 S22: 0.0210 S23: -0.0720
REMARK 3 S31: -0.0786 S32: 0.1070 S33: -0.0000
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: (chain B and resid 1:77)
REMARK 3 ORIGIN FOR THE GROUP (A): -7.0040 58.1992 119.4931
REMARK 3 T TENSOR
REMARK 3 T11: 0.1927 T22: 0.1033
REMARK 3 T33: 0.1780 T12: -0.0000
REMARK 3 T13: 0.0333 T23: 0.0063
REMARK 3 L TENSOR
REMARK 3 L11: 0.7046 L22: 0.5625
REMARK 3 L33: 1.6605 L12: 0.1941
REMARK 3 L13: 0.5193 L23: -0.1932
REMARK 3 S TENSOR
REMARK 3 S11: 0.2619 S12: -0.1029 S13: -0.0444
REMARK 3 S21: 0.1165 S22: -0.1148 S23: 0.2073
REMARK 3 S31: -0.0609 S32: -0.0087 S33: -0.0009
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: (chain B and resid 78:141)
REMARK 3 ORIGIN FOR THE GROUP (A): -8.5781 56.4183 101.3174
REMARK 3 T TENSOR
REMARK 3 T11: 0.0781 T22: 0.2324
REMARK 3 T33: 0.1567 T12: 0.0132
REMARK 3 T13: 0.0136 T23: -0.0259
REMARK 3 L TENSOR
REMARK 3 L11: 0.8634 L22: 0.7678
REMARK 3 L33: 0.8336 L12: 0.2285
REMARK 3 L13: -0.2449 L23: -0.3068
REMARK 3 S TENSOR
REMARK 3 S11: -0.0222 S12: 0.3246 S13: -0.1535
REMARK 3 S21: -0.0074 S22: -0.0472 S23: 0.0965
REMARK 3 S31: 0.0361 S32: -0.4055 S33: -0.1202
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: (chain B and resid 142:224)
REMARK 3 ORIGIN FOR THE GROUP (A): 9.3632 62.6723 94.2102
REMARK 3 T TENSOR
REMARK 3 T11: 0.0989 T22: 0.1047
REMARK 3 T33: 0.1218 T12: 0.0073
REMARK 3 T13: 0.0101 T23: 0.0145
REMARK 3 L TENSOR
REMARK 3 L11: 0.3924 L22: 0.4003
REMARK 3 L33: 0.5060 L12: 0.0433
REMARK 3 L13: -0.2011 L23: 0.3629
REMARK 3 S TENSOR
REMARK 3 S11: 0.0667 S12: 0.0193 S13: 0.0442
REMARK 3 S21: 0.0128 S22: -0.0110 S23: 0.1090
REMARK 3 S31: -0.0397 S32: -0.1766 S33: 0.0101
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: (chain B and resid 225:299)
REMARK 3 ORIGIN FOR THE GROUP (A): 19.6384 46.0300 106.1427
REMARK 3 T TENSOR
REMARK 3 T11: 0.1706 T22: 0.1296
REMARK 3 T33: 0.1208 T12: -0.0002
REMARK 3 T13: 0.0136 T23: 0.0333
REMARK 3 L TENSOR
REMARK 3 L11: 0.5581 L22: 0.3669
REMARK 3 L33: 0.2066 L12: 0.1890
REMARK 3 L13: -0.2525 L23: 0.0423
REMARK 3 S TENSOR
REMARK 3 S11: -0.0518 S12: -0.1513 S13: -0.0871
REMARK 3 S21: 0.1447 S22: -0.0366 S23: 0.1190
REMARK 3 S31: 0.0441 S32: -0.0241 S33: -0.0106
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: (chain B and resid 300:370)
REMARK 3 ORIGIN FOR THE GROUP (A): 23.3047 69.5328 105.1893
REMARK 3 T TENSOR
REMARK 3 T11: 0.1194 T22: 0.1237
REMARK 3 T33: 0.1369 T12: -0.0195
REMARK 3 T13: 0.0068 T23: -0.0381
REMARK 3 L TENSOR
REMARK 3 L11: 0.5819 L22: 0.6452
REMARK 3 L33: 0.4562 L12: -0.0500
REMARK 3 L13: -0.0335 L23: 0.5194
REMARK 3 S TENSOR
REMARK 3 S11: 0.0483 S12: -0.1663 S13: 0.1894
REMARK 3 S21: 0.0908 S22: 0.0378 S23: -0.1422
REMARK 3 S31: -0.1344 S32: 0.1604 S33: -0.0000
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: (chain B and resid 371:384)
REMARK 3 ORIGIN FOR THE GROUP (A): -4.1779 69.1390 105.5052
REMARK 3 T TENSOR
REMARK 3 T11: 0.2872 T22: 0.1182
REMARK 3 T33: 0.2288 T12: 0.0625
REMARK 3 T13: 0.0734 T23: 0.0491
REMARK 3 L TENSOR
REMARK 3 L11: 0.4636 L22: 0.1596
REMARK 3 L33: 0.6251 L12: 0.0037
REMARK 3 L13: -0.4949 L23: 0.1218
REMARK 3 S TENSOR
REMARK 3 S11: 0.3209 S12: -0.0021 S13: 0.2421
REMARK 3 S21: -0.3385 S22: -0.1798 S23: -0.1031
REMARK 3 S31: -0.4878 S32: 0.0557 S33: 0.0400
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 3KHY COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-NOV-09.
REMARK 100 THE RCSB ID CODE IS RCSB056015.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 23-OCT-09
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 21-ID-G
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97857
REMARK 200 MONOCHROMATOR : DIAMOND-111
REMARK 200 OPTICS : BE-LENES
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RAYONIX MX-300
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 117233
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.970
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 7.600
REMARK 200 R MERGE (I) : 0.12400
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 18.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.97
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.00
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : 7.60
REMARK 200 R MERGE FOR SHELL (I) : 0.49000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 5.700
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: PHENIX (PHENIX.AUTOSOL: 1.4_115)
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 51.90
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.56
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NAFORMATE 4M, 0.3M 195 NDSB, PH 7,
REMARK 280 VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 298K
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 33.53950
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 74.83050
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 43.56350
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 74.83050
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 33.53950
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 43.56350
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 5520 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 30770 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -50.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
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 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 SER B 2 OG
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 B 379 O HOH B 482 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 ALA A 46 -112.59 -113.49
REMARK 500 LEU A 189 -71.81 -82.88
REMARK 500 SER A 264 -150.69 -112.10
REMARK 500 ASN A 371 77.91 -152.96
REMARK 500 ALA B 46 -126.68 -117.29
REMARK 500 HIS B 117 -54.38 -127.82
REMARK 500 ALA B 173 -165.16 -160.36
REMARK 500 HIS B 174 19.50 55.17
REMARK 500 PRO B 224 5.25 -68.22
REMARK 500 SER B 264 -152.70 -109.43
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: IDP01739 RELATED DB: TARGETDB
DBREF 3KHY A 1 384 UNP Q5NE95 Q5NE95_FRATT 1 384
DBREF 3KHY B 1 384 UNP Q5NE95 Q5NE95_FRATT 1 384
SEQRES 1 A 384 MSE SER GLU ILE LEU VAL LEU ASN CYS GLY SER SER SER
SEQRES 2 A 384 VAL LYS PHE ALA LEU ILE ASN PRO HIS THR SER GLN SER
SEQRES 3 A 384 LEU VAL THR GLY LEU ALA GLU ASN ILE ALA THR LYS ASN
SEQRES 4 A 384 CYS LYS VAL VAL PHE LYS ALA GLU HIS LYS ILE VAL LYS
SEQRES 5 A 384 TYR LEU GLU ASN GLY SER TYR LYS ASP VAL PHE GLU MSE
SEQRES 6 A 384 LEU LYS ASP PHE LEU VAL GLU ASN LYS HIS LEU GLU LYS
SEQRES 7 A 384 ILE VAL ALA ILE GLY HIS ARG VAL VAL HIS GLY GLY GLN
SEQRES 8 A 384 TYR PHE SER LYS SER VAL LEU ILE ASN ALA ASP SER LEU
SEQRES 9 A 384 GLU LYS ILE LYS ALA CYS ILE ALA LEU ALA PRO LEU HIS
SEQRES 10 A 384 ASN PRO ALA HIS ILE GLU GLY ILE ARG PHE CYS GLN GLN
SEQRES 11 A 384 ILE PHE PRO GLU LEU PRO GLN VAL ALA VAL PHE ASP THR
SEQRES 12 A 384 ALA PHE HIS GLN THR MSE PRO SER TYR ILE ALA GLU TYR
SEQRES 13 A 384 ALA ILE PRO TYR GLU LEU THR HIS LYS HIS ASN ILE ARG
SEQRES 14 A 384 LYS TYR GLY ALA HIS GLY THR SER HIS LYS TYR VAL SER
SEQRES 15 A 384 GLU GLN ALA ALA LYS ILE LEU THR GLN GLN LYS ALA ASN
SEQRES 16 A 384 VAL ILE VAL ALA HIS LEU GLY ASN GLY CYS SER ILE THR
SEQRES 17 A 384 ALA VAL VAL ASP GLY LYS SER ILE ASP THR SER MSE GLY
SEQRES 18 A 384 LEU THR PRO LEU ASP GLY LEU VAL MSE GLY THR ARG SER
SEQRES 19 A 384 GLY CYS ILE ASP PRO SER ILE PHE ALA TYR ILE SER ASP
SEQRES 20 A 384 ASN LEU GLY TRP SER VAL THR GLU ILE THR ASN MSE LEU
SEQRES 21 A 384 ASN LYS GLN SER GLY LEU LEU GLY ILE CYS GLY HIS ASN
SEQRES 22 A 384 ASP MSE ARG GLU VAL SER GLN LEU ALA ALA LYS GLY ASP
SEQRES 23 A 384 SER LEU ALA LYS LEU ALA ILE GLU ILE PHE SER HIS ARG
SEQRES 24 A 384 VAL ALA LYS PHE VAL ALA SER TYR MSE ILE TYR PHE ASN
SEQRES 25 A 384 LYS LEU ASP ALA LEU VAL PHE THR GLY GLY ILE GLY GLU
SEQRES 26 A 384 ASN ALA ALA ASN ILE ARG LYS ASN ILE ILE SER LYS LEU
SEQRES 27 A 384 ALA ASN LEU GLY PHE MSE ILE ASP HIS GLN LYS ASN SER
SEQRES 28 A 384 ASN SER GLU THR PHE ILE ASN SER LYS ASN SER HIS ASN
SEQRES 29 A 384 ILE MSE VAL ILE ALA THR ASN GLU GLU LEU MSE ILE ALA
SEQRES 30 A 384 GLN GLU THR GLN ASN LEU ILE
SEQRES 1 B 384 MSE SER GLU ILE LEU VAL LEU ASN CYS GLY SER SER SER
SEQRES 2 B 384 VAL LYS PHE ALA LEU ILE ASN PRO HIS THR SER GLN SER
SEQRES 3 B 384 LEU VAL THR GLY LEU ALA GLU ASN ILE ALA THR LYS ASN
SEQRES 4 B 384 CYS LYS VAL VAL PHE LYS ALA GLU HIS LYS ILE VAL LYS
SEQRES 5 B 384 TYR LEU GLU ASN GLY SER TYR LYS ASP VAL PHE GLU MSE
SEQRES 6 B 384 LEU LYS ASP PHE LEU VAL GLU ASN LYS HIS LEU GLU LYS
SEQRES 7 B 384 ILE VAL ALA ILE GLY HIS ARG VAL VAL HIS GLY GLY GLN
SEQRES 8 B 384 TYR PHE SER LYS SER VAL LEU ILE ASN ALA ASP SER LEU
SEQRES 9 B 384 GLU LYS ILE LYS ALA CYS ILE ALA LEU ALA PRO LEU HIS
SEQRES 10 B 384 ASN PRO ALA HIS ILE GLU GLY ILE ARG PHE CYS GLN GLN
SEQRES 11 B 384 ILE PHE PRO GLU LEU PRO GLN VAL ALA VAL PHE ASP THR
SEQRES 12 B 384 ALA PHE HIS GLN THR MSE PRO SER TYR ILE ALA GLU TYR
SEQRES 13 B 384 ALA ILE PRO TYR GLU LEU THR HIS LYS HIS ASN ILE ARG
SEQRES 14 B 384 LYS TYR GLY ALA HIS GLY THR SER HIS LYS TYR VAL SER
SEQRES 15 B 384 GLU GLN ALA ALA LYS ILE LEU THR GLN GLN LYS ALA ASN
SEQRES 16 B 384 VAL ILE VAL ALA HIS LEU GLY ASN GLY CYS SER ILE THR
SEQRES 17 B 384 ALA VAL VAL ASP GLY LYS SER ILE ASP THR SER MSE GLY
SEQRES 18 B 384 LEU THR PRO LEU ASP GLY LEU VAL MSE GLY THR ARG SER
SEQRES 19 B 384 GLY CYS ILE ASP PRO SER ILE PHE ALA TYR ILE SER ASP
SEQRES 20 B 384 ASN LEU GLY TRP SER VAL THR GLU ILE THR ASN MSE LEU
SEQRES 21 B 384 ASN LYS GLN SER GLY LEU LEU GLY ILE CYS GLY HIS ASN
SEQRES 22 B 384 ASP MSE ARG GLU VAL SER GLN LEU ALA ALA LYS GLY ASP
SEQRES 23 B 384 SER LEU ALA LYS LEU ALA ILE GLU ILE PHE SER HIS ARG
SEQRES 24 B 384 VAL ALA LYS PHE VAL ALA SER TYR MSE ILE TYR PHE ASN
SEQRES 25 B 384 LYS LEU ASP ALA LEU VAL PHE THR GLY GLY ILE GLY GLU
SEQRES 26 B 384 ASN ALA ALA ASN ILE ARG LYS ASN ILE ILE SER LYS LEU
SEQRES 27 B 384 ALA ASN LEU GLY PHE MSE ILE ASP HIS GLN LYS ASN SER
SEQRES 28 B 384 ASN SER GLU THR PHE ILE ASN SER LYS ASN SER HIS ASN
SEQRES 29 B 384 ILE MSE VAL ILE ALA THR ASN GLU GLU LEU MSE ILE ALA
SEQRES 30 B 384 GLN GLU THR GLN ASN LEU ILE
MODRES 3KHY MSE A 1 MET SELENOMETHIONINE
MODRES 3KHY MSE A 65 MET SELENOMETHIONINE
MODRES 3KHY MSE A 149 MET SELENOMETHIONINE
MODRES 3KHY MSE A 220 MET SELENOMETHIONINE
MODRES 3KHY MSE A 230 MET SELENOMETHIONINE
MODRES 3KHY MSE A 259 MET SELENOMETHIONINE
MODRES 3KHY MSE A 275 MET SELENOMETHIONINE
MODRES 3KHY MSE A 308 MET SELENOMETHIONINE
MODRES 3KHY MSE A 344 MET SELENOMETHIONINE
MODRES 3KHY MSE A 366 MET SELENOMETHIONINE
MODRES 3KHY MSE A 375 MET SELENOMETHIONINE
MODRES 3KHY MSE B 1 MET SELENOMETHIONINE
MODRES 3KHY MSE B 65 MET SELENOMETHIONINE
MODRES 3KHY MSE B 149 MET SELENOMETHIONINE
MODRES 3KHY MSE B 220 MET SELENOMETHIONINE
MODRES 3KHY MSE B 230 MET SELENOMETHIONINE
MODRES 3KHY MSE B 259 MET SELENOMETHIONINE
MODRES 3KHY MSE B 275 MET SELENOMETHIONINE
MODRES 3KHY MSE B 308 MET SELENOMETHIONINE
MODRES 3KHY MSE B 344 MET SELENOMETHIONINE
MODRES 3KHY MSE B 366 MET SELENOMETHIONINE
MODRES 3KHY MSE B 375 MET SELENOMETHIONINE
HET MSE A 1 8
HET MSE A 65 8
HET MSE A 149 8
HET MSE A 220 8
HET MSE A 230 8
HET MSE A 259 8
HET MSE A 275 8
HET MSE A 308 8
HET MSE A 344 8
HET MSE A 366 8
HET MSE A 375 8
HET MSE B 1 8
HET MSE B 65 8
HET MSE B 149 8
HET MSE B 220 8
HET MSE B 230 8
HET MSE B 259 8
HET MSE B 275 8
HET MSE B 308 8
HET MSE B 344 8
HET MSE B 366 8
HET MSE B 375 8
HETNAM MSE SELENOMETHIONINE
FORMUL 1 MSE 22(C5 H11 N O2 SE)
FORMUL 3 HOH *656(H2 O)
HELIX 1 1 SER A 58 ASN A 73 1 16
HELIX 2 2 HIS A 75 GLU A 77 5 3
HELIX 3 3 ASN A 100 CYS A 110 1 11
HELIX 4 4 ILE A 111 ALA A 114 5 4
HELIX 5 5 HIS A 117 PHE A 132 1 16
HELIX 6 6 THR A 143 MSE A 149 5 7
HELIX 7 7 PRO A 150 GLU A 155 1 6
HELIX 8 8 PRO A 159 LYS A 165 1 7
HELIX 9 9 HIS A 174 LEU A 189 1 16
HELIX 10 10 SER A 240 GLY A 250 1 11
HELIX 11 11 SER A 252 GLN A 263 1 12
HELIX 12 12 SER A 264 GLY A 271 1 8
HELIX 13 13 ASP A 274 LYS A 284 1 11
HELIX 14 14 ASP A 286 MSE A 308 1 23
HELIX 15 15 ILE A 309 PHE A 311 5 3
HELIX 16 16 GLY A 321 ALA A 327 1 7
HELIX 17 17 ALA A 327 LEU A 338 1 12
HELIX 18 18 ALA A 339 GLY A 342 5 4
HELIX 19 19 ASP A 346 ASN A 352 1 7
HELIX 20 20 ASN A 371 LEU A 383 1 13
HELIX 21 21 SER B 58 ASN B 73 1 16
HELIX 22 22 HIS B 75 GLU B 77 5 3
HELIX 23 23 ASN B 100 CYS B 110 1 11
HELIX 24 24 ILE B 111 LEU B 113 5 3
HELIX 25 25 HIS B 117 PHE B 132 1 16
HELIX 26 26 THR B 143 MSE B 149 5 7
HELIX 27 27 PRO B 150 GLU B 155 1 6
HELIX 28 28 PRO B 159 LYS B 165 1 7
HELIX 29 29 HIS B 174 LEU B 189 1 16
HELIX 30 30 SER B 240 GLY B 250 1 11
HELIX 31 31 SER B 252 GLN B 263 1 12
HELIX 32 32 SER B 264 GLY B 271 1 8
HELIX 33 33 ASP B 274 LYS B 284 1 11
HELIX 34 34 ASP B 286 MSE B 308 1 23
HELIX 35 35 ILE B 309 PHE B 311 5 3
HELIX 36 36 GLY B 321 ALA B 327 1 7
HELIX 37 37 ALA B 327 LYS B 337 1 11
HELIX 38 38 LEU B 338 GLY B 342 5 5
HELIX 39 39 ASP B 346 ASN B 352 1 7
HELIX 40 40 ASN B 371 ILE B 384 1 14
SHEET 1 A 8 LYS A 49 TYR A 53 0
SHEET 2 A 8 LYS A 41 LYS A 45 -1 N VAL A 42 O LYS A 52
SHEET 3 A 8 GLN A 25 GLU A 33 -1 N THR A 29 O LYS A 45
SHEET 4 A 8 VAL A 14 ASN A 20 -1 N LEU A 18 O LEU A 27
SHEET 5 A 8 GLU A 3 CYS A 9 -1 N VAL A 6 O ALA A 17
SHEET 6 A 8 ILE A 79 VAL A 86 1 O GLY A 83 N LEU A 7
SHEET 7 A 8 GLN A 137 PHE A 141 1 O VAL A 138 N HIS A 84
SHEET 8 A 8 VAL A 97 LEU A 98 -1 N VAL A 97 O ALA A 139
SHEET 1 B 5 LYS A 214 THR A 218 0
SHEET 2 B 5 CYS A 205 VAL A 211 -1 N VAL A 211 O LYS A 214
SHEET 3 B 5 VAL A 196 LEU A 201 -1 N VAL A 196 O VAL A 210
SHEET 4 B 5 ALA A 316 THR A 320 1 O VAL A 318 N ALA A 199
SHEET 5 B 5 ILE A 365 VAL A 367 1 O MSE A 366 N LEU A 317
SHEET 1 C 8 LYS B 49 TYR B 53 0
SHEET 2 C 8 LYS B 41 LYS B 45 -1 N PHE B 44 O ILE B 50
SHEET 3 C 8 GLN B 25 GLU B 33 -1 N THR B 29 O LYS B 45
SHEET 4 C 8 VAL B 14 ASN B 20 -1 N LEU B 18 O VAL B 28
SHEET 5 C 8 GLU B 3 CYS B 9 -1 N VAL B 6 O ALA B 17
SHEET 6 C 8 ILE B 79 VAL B 86 1 O GLY B 83 N LEU B 7
SHEET 7 C 8 GLN B 137 PHE B 141 1 O VAL B 138 N HIS B 84
SHEET 8 C 8 VAL B 97 LEU B 98 -1 N VAL B 97 O ALA B 139
SHEET 1 D 5 LYS B 214 THR B 218 0
SHEET 2 D 5 CYS B 205 VAL B 211 -1 N ALA B 209 O ILE B 216
SHEET 3 D 5 VAL B 196 LEU B 201 -1 N VAL B 196 O VAL B 210
SHEET 4 D 5 ALA B 316 THR B 320 1 O VAL B 318 N ALA B 199
SHEET 5 D 5 ILE B 365 VAL B 367 1 O MSE B 366 N PHE B 319
LINK C MSE A 1 N SER A 2 1555 1555 1.33
LINK C GLU A 64 N MSE A 65 1555 1555 1.33
LINK C MSE A 65 N LEU A 66 1555 1555 1.33
LINK C THR A 148 N MSE A 149 1555 1555 1.33
LINK C MSE A 149 N PRO A 150 1555 1555 1.34
LINK C SER A 219 N MSE A 220 1555 1555 1.34
LINK C MSE A 220 N GLY A 221 1555 1555 1.33
LINK C VAL A 229 N MSE A 230 1555 1555 1.33
LINK C MSE A 230 N GLY A 231 1555 1555 1.33
LINK C ASN A 258 N MSE A 259 1555 1555 1.33
LINK C MSE A 259 N LEU A 260 1555 1555 1.33
LINK C ASP A 274 N MSE A 275 1555 1555 1.33
LINK C MSE A 275 N ARG A 276 1555 1555 1.33
LINK C TYR A 307 N MSE A 308 1555 1555 1.33
LINK C MSE A 308 N ILE A 309 1555 1555 1.33
LINK C PHE A 343 N MSE A 344 1555 1555 1.33
LINK C MSE A 344 N ILE A 345 1555 1555 1.33
LINK C ILE A 365 N MSE A 366 1555 1555 1.33
LINK C MSE A 366 N VAL A 367 1555 1555 1.32
LINK C LEU A 374 N MSE A 375 1555 1555 1.33
LINK C MSE A 375 N ILE A 376 1555 1555 1.33
LINK C GLU B 64 N MSE B 65 1555 1555 1.33
LINK C MSE B 65 N LEU B 66 1555 1555 1.33
LINK C THR B 148 N MSE B 149 1555 1555 1.33
LINK C MSE B 149 N PRO B 150 1555 1555 1.34
LINK C SER B 219 N MSE B 220 1555 1555 1.33
LINK C MSE B 220 N GLY B 221 1555 1555 1.33
LINK C VAL B 229 N MSE B 230 1555 1555 1.33
LINK C MSE B 230 N GLY B 231 1555 1555 1.33
LINK C ASN B 258 N MSE B 259 1555 1555 1.33
LINK C MSE B 259 N LEU B 260 1555 1555 1.33
LINK C ASP B 274 N MSE B 275 1555 1555 1.33
LINK C MSE B 275 N ARG B 276 1555 1555 1.33
LINK C TYR B 307 N MSE B 308 1555 1555 1.33
LINK C MSE B 308 N AILE B 309 1555 1555 1.32
LINK C MSE B 308 N BILE B 309 1555 1555 1.33
LINK C PHE B 343 N MSE B 344 1555 1555 1.33
LINK C MSE B 344 N ILE B 345 1555 1555 1.33
LINK C ILE B 365 N MSE B 366 1555 1555 1.32
LINK C MSE B 366 N VAL B 367 1555 1555 1.33
LINK C LEU B 374 N MSE B 375 1555 1555 1.33
LINK C MSE B 375 N ILE B 376 1555 1555 1.33
LINK C MSE B 1 N SER B 2 1555 1555 1.33
CRYST1 67.079 87.127 149.661 90.00 90.00 90.00 P 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 0.014908 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011477 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006682 0.00000
HETATM 1 N MSE A 1 60.054 40.281 71.939 1.00 66.23 N
HETATM 2 CA MSE A 1 59.627 39.422 70.836 1.00 67.59 C
HETATM 3 C MSE A 1 58.643 38.336 71.267 1.00 63.11 C
HETATM 4 O MSE A 1 57.981 37.716 70.430 1.00 55.75 O
HETATM 5 CB MSE A 1 60.837 38.787 70.149 1.00 76.34 C
HETATM 6 CG MSE A 1 61.390 39.617 69.000 1.00 82.40 C
HETATM 7 SE MSE A 1 60.224 39.623 67.427 1.00176.86 SE
HETATM 8 CE MSE A 1 60.909 38.030 66.528 1.00 97.88 C
(ATOM LINES ARE NOT SHOWN.)
END
