HEADER ISOMERASE 19-DEC-13 4O53
TITLE CRYSTAL STRUCTURE OF TRICHOMONAS VAGINALIS TRIOSEPHOSPHATE ISOMERASE
TITLE 2 ILE45-LEU MUTANT (TVAG_497370)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TRIOSEPHOSPHATE ISOMERASE;
COMPND 3 CHAIN: A;
COMPND 4 EC: 5.3.1.1;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: TRICHOMONAS VAGINALIS;
SOURCE 3 ORGANISM_TAXID: 5722;
SOURCE 4 GENE: TVAG_497370;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21 STAR ROSSETAII;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET19B
KEYWDS TIM BARREL, ISOMERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR S.LARA-GONZALEZ,G.M.MONTERO-MORAN,P.ESTRELLA-HERNANDEZ,C.G.BENITEZ-
AUTHOR 2 CARDOZA,L.G.BRIEBA
REVDAT 3 28-FEB-24 4O53 1 REMARK SEQADV LINK
REVDAT 2 07-MAR-18 4O53 1 REMARK
REVDAT 1 24-DEC-14 4O53 0
JRNL AUTH S.LARA-GONZALEZ,G.M.MONTERO-MORAN,P.ESTRELLA-HERNANDEZ,
JRNL AUTH 2 C.G.BENITEZ-CARDOZA,L.G.BRIEBA
JRNL TITL ENGINEERING MUTANTS WITH ALTERED DIMER-MONOMER EQUILIBRIUM
JRNL TITL 2 REVEAL THE EXISTENCE OF STABLE MONOMERIC TRIOSEPHOSPHATE
JRNL TITL 3 ISOMERASES
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX DEV_1396
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.40
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.6
REMARK 3 NUMBER OF REFLECTIONS : 19099
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.168
REMARK 3 R VALUE (WORKING SET) : 0.165
REMARK 3 FREE R VALUE : 0.220
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 6.010
REMARK 3 FREE R VALUE TEST SET COUNT : 1147
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 49.4112 - 3.9994 0.99 2392 154 0.1600 0.2176
REMARK 3 2 3.9994 - 3.1746 1.00 2304 146 0.1659 0.1882
REMARK 3 3 3.1746 - 2.7734 1.00 2260 145 0.1755 0.2197
REMARK 3 4 2.7734 - 2.5198 0.99 2240 143 0.1715 0.2500
REMARK 3 5 2.5198 - 2.3392 0.99 2212 141 0.1673 0.2364
REMARK 3 6 2.3392 - 2.2013 0.98 2219 142 0.1505 0.2258
REMARK 3 7 2.2013 - 2.0910 0.98 2184 139 0.1564 0.2314
REMARK 3 8 2.0910 - 2.0000 0.96 2141 137 0.1654 0.2351
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) : 0.190
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 19.370
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 16.93
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 17.23
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 : 0.014 1935
REMARK 3 ANGLE : 1.334 2611
REMARK 3 CHIRALITY : 0.088 298
REMARK 3 PLANARITY : 0.007 341
REMARK 3 DIHEDRAL : 12.291 680
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 2:17)
REMARK 3 ORIGIN FOR THE GROUP (A): -14.9736 23.5440 -15.0934
REMARK 3 T TENSOR
REMARK 3 T11: 0.1216 T22: 0.1797
REMARK 3 T33: 0.1458 T12: 0.0065
REMARK 3 T13: -0.0141 T23: -0.0432
REMARK 3 L TENSOR
REMARK 3 L11: 0.2786 L22: 0.1333
REMARK 3 L33: 0.5393 L12: -0.0674
REMARK 3 L13: -0.1742 L23: -0.1936
REMARK 3 S TENSOR
REMARK 3 S11: 0.0374 S12: 0.0507 S13: 0.0085
REMARK 3 S21: -0.0561 S22: -0.2673 S23: 0.2540
REMARK 3 S31: -0.0728 S32: -0.1609 S33: -0.0020
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: (CHAIN A AND RESID 18:26)
REMARK 3 ORIGIN FOR THE GROUP (A): -25.0130 31.5342 -13.5910
REMARK 3 T TENSOR
REMARK 3 T11: 0.1623 T22: 0.2337
REMARK 3 T33: 0.1985 T12: 0.0520
REMARK 3 T13: -0.0075 T23: 0.0028
REMARK 3 L TENSOR
REMARK 3 L11: 0.1679 L22: 0.1637
REMARK 3 L33: 0.1013 L12: 0.0430
REMARK 3 L13: 0.0205 L23: -0.1131
REMARK 3 S TENSOR
REMARK 3 S11: -0.0913 S12: 0.3344 S13: 0.2638
REMARK 3 S21: -0.0686 S22: -0.0156 S23: 0.0620
REMARK 3 S31: -0.1716 S32: -0.1418 S33: -0.0001
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: (CHAIN A AND RESID 27:35)
REMARK 3 ORIGIN FOR THE GROUP (A): -25.8797 18.1364 -23.3363
REMARK 3 T TENSOR
REMARK 3 T11: 0.1764 T22: 0.3262
REMARK 3 T33: 0.2392 T12: 0.0080
REMARK 3 T13: -0.0331 T23: -0.0900
REMARK 3 L TENSOR
REMARK 3 L11: 0.0356 L22: 0.0881
REMARK 3 L33: 0.4314 L12: -0.0486
REMARK 3 L13: 0.1046 L23: -0.1873
REMARK 3 S TENSOR
REMARK 3 S11: 0.0342 S12: 0.2321 S13: -0.2759
REMARK 3 S21: -0.0295 S22: -0.0239 S23: 0.2737
REMARK 3 S31: 0.3448 S32: -0.2584 S33: 0.0057
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: (CHAIN A AND RESID 36:98)
REMARK 3 ORIGIN FOR THE GROUP (A): -14.9189 20.7197 -4.5600
REMARK 3 T TENSOR
REMARK 3 T11: 0.1203 T22: 0.1197
REMARK 3 T33: 0.1188 T12: -0.0118
REMARK 3 T13: 0.0140 T23: -0.0200
REMARK 3 L TENSOR
REMARK 3 L11: 0.1647 L22: 0.4261
REMARK 3 L33: 0.7857 L12: -0.1069
REMARK 3 L13: -0.0312 L23: 0.5046
REMARK 3 S TENSOR
REMARK 3 S11: -0.0231 S12: 0.1006 S13: 0.0040
REMARK 3 S21: 0.1008 S22: -0.0532 S23: 0.0846
REMARK 3 S31: 0.0570 S32: -0.1140 S33: 0.0004
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: (CHAIN A AND RESID 99:118)
REMARK 3 ORIGIN FOR THE GROUP (A): -1.9018 16.8611 -1.8309
REMARK 3 T TENSOR
REMARK 3 T11: 0.1818 T22: 0.1412
REMARK 3 T33: 0.1562 T12: 0.0123
REMARK 3 T13: 0.0121 T23: 0.0014
REMARK 3 L TENSOR
REMARK 3 L11: 0.3942 L22: 0.4481
REMARK 3 L33: 0.5882 L12: -0.0969
REMARK 3 L13: 0.2637 L23: 0.2438
REMARK 3 S TENSOR
REMARK 3 S11: -0.1511 S12: -0.0069 S13: 0.1236
REMARK 3 S21: 0.0534 S22: 0.0868 S23: -0.2020
REMARK 3 S31: 0.1535 S32: 0.1070 S33: -0.0010
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: (CHAIN A AND RESID 119:133)
REMARK 3 ORIGIN FOR THE GROUP (A): 0.0386 17.6113 -13.7628
REMARK 3 T TENSOR
REMARK 3 T11: 0.1319 T22: 0.1482
REMARK 3 T33: 0.1404 T12: 0.0035
REMARK 3 T13: -0.0153 T23: -0.0211
REMARK 3 L TENSOR
REMARK 3 L11: 0.2289 L22: 0.2424
REMARK 3 L33: 0.6034 L12: 0.0355
REMARK 3 L13: 0.3564 L23: 0.1661
REMARK 3 S TENSOR
REMARK 3 S11: 0.0394 S12: -0.0912 S13: -0.1470
REMARK 3 S21: 0.0771 S22: -0.0808 S23: -0.0314
REMARK 3 S31: 0.0427 S32: 0.0797 S33: 0.0001
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: (CHAIN A AND RESID 134:149)
REMARK 3 ORIGIN FOR THE GROUP (A): 8.2457 13.7399 -15.6443
REMARK 3 T TENSOR
REMARK 3 T11: 0.1644 T22: 0.2390
REMARK 3 T33: 0.3112 T12: 0.0181
REMARK 3 T13: -0.0086 T23: -0.0293
REMARK 3 L TENSOR
REMARK 3 L11: 0.2958 L22: 0.1684
REMARK 3 L33: 1.2130 L12: -0.1790
REMARK 3 L13: -0.5529 L23: 0.4404
REMARK 3 S TENSOR
REMARK 3 S11: -0.1773 S12: 0.1852 S13: -0.3830
REMARK 3 S21: 0.1069 S22: 0.1979 S23: -0.0784
REMARK 3 S31: 0.2193 S32: 0.2786 S33: 0.0271
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: (CHAIN A AND RESID 150:195)
REMARK 3 ORIGIN FOR THE GROUP (A): -0.9834 13.0395 -18.1364
REMARK 3 T TENSOR
REMARK 3 T11: 0.1404 T22: 0.1105
REMARK 3 T33: 0.1486 T12: 0.0194
REMARK 3 T13: 0.0097 T23: -0.0233
REMARK 3 L TENSOR
REMARK 3 L11: 0.7824 L22: 0.6618
REMARK 3 L33: 0.7683 L12: -0.0643
REMARK 3 L13: 0.1664 L23: 0.6280
REMARK 3 S TENSOR
REMARK 3 S11: -0.0791 S12: 0.0817 S13: -0.0548
REMARK 3 S21: 0.0514 S22: 0.0784 S23: -0.0808
REMARK 3 S31: 0.0983 S32: 0.0267 S33: 0.0006
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: (CHAIN A AND RESID 196:206)
REMARK 3 ORIGIN FOR THE GROUP (A): -4.6838 1.5963 -16.3215
REMARK 3 T TENSOR
REMARK 3 T11: 0.2563 T22: 0.1489
REMARK 3 T33: 0.2006 T12: 0.0257
REMARK 3 T13: 0.0473 T23: -0.0034
REMARK 3 L TENSOR
REMARK 3 L11: 0.2169 L22: 0.1295
REMARK 3 L33: 0.8555 L12: -0.1636
REMARK 3 L13: 0.3098 L23: -0.1730
REMARK 3 S TENSOR
REMARK 3 S11: -0.1989 S12: -0.1984 S13: -0.2066
REMARK 3 S21: 0.2215 S22: 0.2219 S23: 0.0534
REMARK 3 S31: 0.5261 S32: 0.1004 S33: 0.0391
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: (CHAIN A AND RESID 207:237)
REMARK 3 ORIGIN FOR THE GROUP (A): -9.5760 19.4391 -24.8531
REMARK 3 T TENSOR
REMARK 3 T11: 0.1222 T22: 0.1655
REMARK 3 T33: 0.1562 T12: 0.0172
REMARK 3 T13: 0.0028 T23: -0.0002
REMARK 3 L TENSOR
REMARK 3 L11: 0.1453 L22: 0.0626
REMARK 3 L33: 0.2621 L12: 0.1020
REMARK 3 L13: 0.0019 L23: 0.0095
REMARK 3 S TENSOR
REMARK 3 S11: -0.0641 S12: 0.2170 S13: 0.0097
REMARK 3 S21: -0.0485 S22: -0.0467 S23: 0.0115
REMARK 3 S31: -0.0362 S32: -0.0273 S33: 0.0001
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: (CHAIN A AND RESID 238:243)
REMARK 3 ORIGIN FOR THE GROUP (A): -19.0751 25.8118 -24.4343
REMARK 3 T TENSOR
REMARK 3 T11: 0.2076 T22: 0.2437
REMARK 3 T33: 0.1531 T12: 0.0178
REMARK 3 T13: -0.0289 T23: -0.0536
REMARK 3 L TENSOR
REMARK 3 L11: 0.6068 L22: 0.6561
REMARK 3 L33: 0.2647 L12: 0.5634
REMARK 3 L13: 0.0528 L23: 0.2325
REMARK 3 S TENSOR
REMARK 3 S11: 0.0071 S12: 0.3006 S13: 0.1630
REMARK 3 S21: -0.3705 S22: -0.0722 S23: 0.3092
REMARK 3 S31: -0.3171 S32: 0.3054 S33: 0.0127
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: (CHAIN A AND RESID 244:252)
REMARK 3 ORIGIN FOR THE GROUP (A): -16.5769 14.6371 -28.7032
REMARK 3 T TENSOR
REMARK 3 T11: 0.1036 T22: 0.2240
REMARK 3 T33: 0.1241 T12: -0.0353
REMARK 3 T13: 0.0075 T23: -0.0803
REMARK 3 L TENSOR
REMARK 3 L11: 0.0279 L22: 0.4681
REMARK 3 L33: 0.6541 L12: -0.1087
REMARK 3 L13: 0.1311 L23: -0.5512
REMARK 3 S TENSOR
REMARK 3 S11: 0.0133 S12: 0.2346 S13: -0.2049
REMARK 3 S21: -0.2113 S22: 0.0861 S23: -0.0385
REMARK 3 S31: 0.1953 S32: -0.1835 S33: 0.0495
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 4O53 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 24-JAN-14.
REMARK 100 THE DEPOSITION ID IS D_1000084052.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 06-APR-11
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5419
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IV++
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA 3.3.16
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 19121
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 55.954
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.9
REMARK 200 DATA REDUNDANCY : 5.200
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.05700
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 18.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.11
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.6
REMARK 200 DATA REDUNDANCY IN SHELL : 4.70
REMARK 200 R MERGE FOR SHELL (I) : 0.15100
REMARK 200 R SYM FOR SHELL (I) : 0.15100
REMARK 200 <I/SIGMA(I)> FOR SHELL : 4.700
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER 2.1.4
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.96
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.51
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M CALCIUM ACETATE, 0.1M SODIUM
REMARK 280 CACODYLATE, 18% PEG 8000, PH 6.5, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 294K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 2 21 21
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 -X,Y+1/2,-Z+1/2
REMARK 290 4555 -X,-Y+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 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 27.97700
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 52.57850
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 27.97700
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 52.57850
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: 4080 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 18160 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -77.0 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 0.00000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 55.95400
REMARK 350 BIOMT3 2 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 1
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 LYS A 22 CG CD CE NZ
REMARK 470 GLU A 25 CG CD OE1 OE2
REMARK 470 GLN A 52 CG CD OE1 NE2
REMARK 470 LYS A 56 CG CD CE NZ
REMARK 470 LYS A 102 CG CD CE NZ
REMARK 470 LYS A 148 CG CD CE NZ
REMARK 470 LYS A 175 CG CD CE NZ
REMARK 470 GLN A 180 CG CD OE1 NE2
REMARK 470 GLU A 184 CG CD OE1 OE2
REMARK 470 LYS A 214 CG CD CE NZ
REMARK 470 GLU A 220 CG CD OE1 OE2
REMARK 470 LYS A 252 CG CD CE NZ
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 LYS A 11 -145.86 56.78
REMARK 500 ARG A 55 131.13 -37.08
REMARK 500 ASP A 99 -72.43 -83.89
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 NA A 303 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLY A 136 O
REMARK 620 2 HOH A 513 O 107.3
REMARK 620 3 HOH A 554 O 68.7 84.9
REMARK 620 4 HOH A 571 O 74.2 78.7 132.3
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA A 302 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLY A 156 O
REMARK 620 2 ASP A 159 OD1 77.6
REMARK 620 3 ASP A 159 OD2 128.0 52.7
REMARK 620 4 HOH A 548 O 72.1 142.3 159.2
REMARK 620 5 HOH A 555 O 87.7 106.8 92.6 94.0
REMARK 620 6 HOH A 557 O 106.4 94.8 93.2 73.4 156.5
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA A 301 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ALA A 222 O
REMARK 620 2 CYS A 224 O 93.4
REMARK 620 3 VAL A 227 O 111.2 95.9
REMARK 620 4 SER A 251 OG 80.0 157.3 106.8
REMARK 620 5 HOH A 560 O 147.7 90.7 100.2 84.1
REMARK 620 N 1 2 3 4
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 303
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4O4V RELATED DB: PDB
REMARK 900 RELATED ID: 4O4W RELATED DB: PDB
REMARK 900 RELATED ID: 4O50 RELATED DB: PDB
REMARK 900 RELATED ID: 4O52 RELATED DB: PDB
REMARK 900 RELATED ID: 4O54 RELATED DB: PDB
REMARK 900 RELATED ID: 4O57 RELATED DB: PDB
REMARK 900 RELATED ID: 3QSR RELATED DB: PDB
DBREF 4O53 A 1 252 UNP A2EGX9 A2EGX9_TRIVA 1 252
SEQADV 4O53 LEU A 45 UNP A2EGX9 ILE 45 ENGINEERED MUTATION
SEQRES 1 A 252 MET ARG THR PHE PHE VAL GLY GLY ASN TRP LYS ALA ASN
SEQRES 2 A 252 PRO LYS THR VAL GLU GLU ALA GLU LYS LEU ILE GLU MET
SEQRES 3 A 252 LEU ASN GLY ALA LYS VAL GLU GLY ASN VAL GLU VAL VAL
SEQRES 4 A 252 VAL ALA ALA PRO PHE LEU PHE LEU PRO THR LEU GLN GLN
SEQRES 5 A 252 LYS LEU ARG LYS ASP TRP LYS VAL SER ALA GLU ASN VAL
SEQRES 6 A 252 PHE THR LYS PRO ASN GLY ALA PHE THR GLY GLU VAL THR
SEQRES 7 A 252 VAL PRO MET ILE LYS SER PHE GLY ILE GLU TRP THR ILE
SEQRES 8 A 252 LEU GLY HIS SER GLU ARG ARG ASP ILE LEU LYS GLU ASP
SEQRES 9 A 252 ASP GLU PHE LEU ALA ALA LYS ALA LYS PHE ALA LEU GLU
SEQRES 10 A 252 ASN GLY MET LYS ILE ILE TYR CYS CYS GLY GLU HIS LEU
SEQRES 11 A 252 SER GLU ARG GLU ALA GLY LYS ALA SER GLU PHE VAL SER
SEQRES 12 A 252 ALA GLN ILE GLU LYS MET ILE PRO ALA ILE PRO ALA GLY
SEQRES 13 A 252 LYS TRP ASP ASP VAL VAL ILE ALA TYR GLU PRO ILE TRP
SEQRES 14 A 252 ALA ILE GLY THR GLY LYS VAL ALA SER THR GLN ASP ALA
SEQRES 15 A 252 GLN GLU MET CYS LYS VAL ILE ARG ASP ILE LEU ALA ALA
SEQRES 16 A 252 LYS VAL GLY ALA ASP ILE ALA ASN LYS VAL ARG ILE LEU
SEQRES 17 A 252 TYR GLY GLY SER VAL LYS PRO ASN ASN CYS ASN GLU LEU
SEQRES 18 A 252 ALA ALA CYS PRO ASP VAL ASP GLY PHE LEU VAL GLY GLY
SEQRES 19 A 252 ALA SER LEU GLU PRO GLY PHE ILE ASN ILE VAL ASN SER
SEQRES 20 A 252 ASN VAL HIS SER LYS
HET NA A 301 1
HET NA A 302 1
HET NA A 303 1
HETNAM NA SODIUM ION
FORMUL 2 NA 3(NA 1+)
FORMUL 5 HOH *181(H2 O)
HELIX 1 1 THR A 16 GLY A 29 1 14
HELIX 2 2 PRO A 43 LEU A 45 5 3
HELIX 3 3 PHE A 46 LEU A 54 1 9
HELIX 4 4 THR A 78 PHE A 85 1 8
HELIX 5 5 HIS A 94 ILE A 100 1 7
HELIX 6 6 ASP A 104 ASN A 118 1 15
HELIX 7 7 HIS A 129 GLY A 136 1 8
HELIX 8 8 LYS A 137 ILE A 150 1 14
HELIX 9 9 PRO A 151 ILE A 153 5 3
HELIX 10 10 LYS A 157 ASP A 159 5 3
HELIX 11 11 PRO A 167 ILE A 171 5 5
HELIX 12 12 SER A 178 GLY A 198 1 21
HELIX 13 13 GLY A 198 VAL A 205 1 8
HELIX 14 14 ASN A 217 CYS A 224 1 8
HELIX 15 15 GLY A 233 PRO A 239 5 7
HELIX 16 16 GLY A 240 ASN A 246 1 7
HELIX 17 17 SER A 247 SER A 251 5 5
SHEET 1 A 9 PHE A 4 ASN A 9 0
SHEET 2 A 9 VAL A 36 ALA A 41 1 O ALA A 41 N GLY A 8
SHEET 3 A 9 LYS A 59 ALA A 62 1 O LYS A 59 N VAL A 40
SHEET 4 A 9 TRP A 89 LEU A 92 1 O TRP A 89 N ALA A 62
SHEET 5 A 9 LYS A 121 CYS A 126 1 O ILE A 123 N LEU A 92
SHEET 6 A 9 VAL A 161 TYR A 165 1 O VAL A 162 N TYR A 124
SHEET 7 A 9 ARG A 206 TYR A 209 1 O LEU A 208 N ILE A 163
SHEET 8 A 9 GLY A 229 VAL A 232 1 O GLY A 229 N TYR A 209
SHEET 9 A 9 PHE A 4 ASN A 9 1 N GLY A 7 O PHE A 230
LINK O GLY A 136 NA NA A 303 1555 1555 2.40
LINK O GLY A 156 NA NA A 302 1555 1555 2.23
LINK OD1 ASP A 159 NA NA A 302 1555 1555 2.40
LINK OD2 ASP A 159 NA NA A 302 1555 1555 2.52
LINK O ALA A 222 NA NA A 301 1555 1555 2.37
LINK O CYS A 224 NA NA A 301 1555 1555 2.34
LINK O VAL A 227 NA NA A 301 1555 1555 2.32
LINK OG SER A 251 NA NA A 301 1555 1555 2.43
LINK NA NA A 301 O HOH A 560 1555 1555 2.49
LINK NA NA A 302 O HOH A 548 1555 1555 2.40
LINK NA NA A 302 O HOH A 555 1555 1555 2.35
LINK NA NA A 302 O HOH A 557 1555 1555 2.35
LINK NA NA A 303 O HOH A 513 1555 1555 2.35
LINK NA NA A 303 O HOH A 554 1555 1555 2.54
LINK NA NA A 303 O HOH A 571 1555 1555 2.45
CISPEP 1 ASN A 13 PRO A 14 0 -8.31
SITE 1 AC1 5 ALA A 222 CYS A 224 VAL A 227 SER A 251
SITE 2 AC1 5 HOH A 560
SITE 1 AC2 5 GLY A 156 ASP A 159 HOH A 548 HOH A 555
SITE 2 AC2 5 HOH A 557
SITE 1 AC3 4 GLY A 136 HOH A 513 HOH A 554 HOH A 571
CRYST1 46.891 55.954 105.157 90.00 90.00 90.00 P 2 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 0.021326 0.000000 0.000000 0.00000
SCALE2 0.000000 0.017872 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009510 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
