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HEADER TRANSFERASE 22-JUN-17 5W8O
TITLE HOMOSERINE TRANSACETYLASE META FROM MYCOBACTERIUM HASSIACUM
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HOMOSERINE O-ACETYLTRANSFERASE;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: UNP RESIDUES 13-372;
COMPND 5 SYNONYM: HOMOSERINE O-TRANS-ACETYLASE,HOMOSERINE TRANSACETYLASE;
COMPND 6 EC: 2.3.1.31;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM HASSIACUM (STRAIN DSM 44199 / CIP
SOURCE 3 105218 / JCM 12690 / 3849);
SOURCE 4 ORGANISM_TAXID: 1122247;
SOURCE 5 STRAIN: DSM 44199 / CIP 105218 / JCM 12690 / 3849;
SOURCE 6 GENE: METX, C731_1248;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: ROSETTA2(DE3);
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PCDF-NT
KEYWDS HOMOSERINE O-ACETYLTRANSFERASE, HOMOSERINE O-TRANS-ACETYLASE, HTA,
KEYWDS 2 METX, METHIONINE BIOSYNTHESIS, RV3341, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR R.W.REED,E.S.RODRIGUEZ,J.LI,K.V.KOROTKOV
REVDAT 2 27-SEP-17 5W8O 1 REMARK
REVDAT 1 12-JUL-17 5W8O 0
JRNL AUTH E.S.RODRIGUEZ,R.W.REED,J.LI,K.V.KOROTKOV
JRNL TITL STRUCTURES OF HOMOSERINE TRANSACETYLASE META FROM
JRNL TITL 2 MYCOBACTERIA
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.47 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX DEV_2722
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) : 1.47
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 47.58
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.110
REMARK 3 COMPLETENESS FOR RANGE (%) : 95.9
REMARK 3 NUMBER OF REFLECTIONS : 118621
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) : 0.153
REMARK 3 FREE R VALUE : 0.183
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.940
REMARK 3 FREE R VALUE TEST SET COUNT : 5840
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 47.6086 - 4.5664 0.96 7325 363 0.1699 0.1750
REMARK 3 2 4.5664 - 3.6249 0.97 7302 349 0.1320 0.1359
REMARK 3 3 3.6249 - 3.1668 0.92 7012 326 0.1444 0.1577
REMARK 3 4 3.1668 - 2.8773 0.97 7384 360 0.1341 0.1695
REMARK 3 5 2.8773 - 2.6711 0.97 7366 339 0.1320 0.1831
REMARK 3 6 2.6711 - 2.5136 0.97 7364 376 0.1304 0.1623
REMARK 3 7 2.5136 - 2.3877 0.93 6976 417 0.1231 0.1623
REMARK 3 8 2.3877 - 2.2838 0.96 7201 405 0.1247 0.1677
REMARK 3 9 2.2838 - 2.1959 0.97 7362 391 0.1225 0.1722
REMARK 3 10 2.1959 - 2.1201 0.97 7346 378 0.1287 0.1651
REMARK 3 11 2.1201 - 2.0538 0.97 7283 425 0.1332 0.1802
REMARK 3 12 2.0538 - 1.9951 0.97 7315 409 0.1345 0.1920
REMARK 3 13 1.9951 - 1.9426 0.98 7354 433 0.1296 0.1711
REMARK 3 14 1.9426 - 1.8952 0.92 6965 418 0.1476 0.2046
REMARK 3 15 1.8952 - 1.8521 0.94 7051 360 0.1530 0.2034
REMARK 3 16 1.8521 - 1.8127 0.96 7298 414 0.1619 0.2207
REMARK 3 17 1.8127 - 1.7764 0.97 7266 395 0.1767 0.2145
REMARK 3 18 1.7764 - 1.7429 0.97 7393 350 0.1840 0.2094
REMARK 3 19 1.7429 - 1.7118 0.97 7358 337 0.1921 0.2447
REMARK 3 20 1.7118 - 1.6827 0.97 7481 357 0.1991 0.2236
REMARK 3 21 1.6827 - 1.6556 0.97 7209 394 0.2048 0.2466
REMARK 3 22 1.6556 - 1.6301 0.97 7371 371 0.2111 0.2235
REMARK 3 23 1.6301 - 1.6062 0.93 7025 345 0.2238 0.2661
REMARK 3 24 1.6062 - 1.5835 0.91 6899 358 0.2430 0.2685
REMARK 3 25 1.5835 - 1.5621 0.94 7246 326 0.2570 0.2692
REMARK 3 26 1.5621 - 1.5418 0.96 7122 365 0.2665 0.3076
REMARK 3 27 1.5418 - 1.5226 0.96 7364 400 0.2882 0.3455
REMARK 3 28 1.5226 - 1.5042 0.96 7212 386 0.2978 0.3259
REMARK 3 29 1.5042 - 1.4867 0.97 7265 386 0.3265 0.3360
REMARK 3 30 1.4867 - 1.4700 0.97 7396 377 0.3382 0.3699
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) : 21.050
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 19.60
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 28.36
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 : 0.005 5264
REMARK 3 ANGLE : 0.765 7173
REMARK 3 CHIRALITY : 0.067 814
REMARK 3 PLANARITY : 0.005 946
REMARK 3 DIHEDRAL : 14.925 1876
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
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 5W8O COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 26-JUN-17.
REMARK 100 THE DEPOSITION ID IS D_1000228583.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 11-JUN-17
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 9.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRL
REMARK 200 BEAMLINE : BL9-2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0000
REMARK 200 MONOCHROMATOR : SI(111) AND SI(220) DOUBLE
REMARK 200 CRYSTAL
REMARK 200 OPTICS : RH COATED FLAT BENT M0, TOROIDAL
REMARK 200 FOCUSING POST-MONOCHROMATOR M1
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS VERSION NOV 1, 2016
REMARK 200 BUILT=20161205
REMARK 200 DATA SCALING SOFTWARE : XSCALE VERSION NOV 1, 2016
REMARK 200 BUILT=20161205
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 118675
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.470
REMARK 200 RESOLUTION RANGE LOW (A) : 47.584
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.3
REMARK 200 DATA REDUNDANCY : 3.776
REMARK 200 R MERGE (I) : 0.04000
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 18.0100
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.47
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.51
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.1
REMARK 200 DATA REDUNDANCY IN SHELL : 3.78
REMARK 200 R MERGE FOR SHELL (I) : 1.01300
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 1.460
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER 2.7.17
REMARK 200 STARTING MODEL: 3I1I
REMARK 200
REMARK 200 REMARK: RECTANGULAR PRISM
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 47.89
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.36
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.15M CALCIUM ACETATE, 21% PEG3350, 3%
REMARK 280 1,6-DIAMINOHEXANE, 0.05M CHES PH 9.5, VAPOR DIFFUSION, HANGING
REMARK 280 DROP, TEMPERATURE 294K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 46.61500
REMARK 290 SMTRY3 2 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: 4330 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 24980 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -71.0 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 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 GLY A 10
REMARK 465 ALA A 11
REMARK 465 MET A 12
REMARK 465 ALA A 13
REMARK 465 GLU A 14
REMARK 465 PRO A 69
REMARK 465 ALA A 70
REMARK 465 GLY A 71
REMARK 465 PRO A 72
REMARK 465 ASN A 73
REMARK 465 TYR A 74
REMARK 465 PRO A 75
REMARK 465 THR A 76
REMARK 465 ASP A 251
REMARK 465 GLU A 252
REMARK 465 ASN A 253
REMARK 465 PRO A 254
REMARK 465 LEU A 255
REMARK 465 LEU A 256
REMARK 465 GLY A 257
REMARK 465 CYS A 338
REMARK 465 ARG A 339
REMARK 465 GLY B 10
REMARK 465 ALA B 11
REMARK 465 MET B 12
REMARK 465 ALA B 13
REMARK 465 GLU B 14
REMARK 465 GLY B 15
REMARK 465 GLU B 16
REMARK 465 ALA B 70
REMARK 465 GLY B 71
REMARK 465 PRO B 72
REMARK 465 ASN B 73
REMARK 465 TYR B 74
REMARK 465 PRO B 75
REMARK 465 THR B 76
REMARK 465 GLY B 337
REMARK 465 CYS B 338
REMARK 465 ARG B 339
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 HG SER A 291 O HOH A 502 1.55
REMARK 500 O HOH B 508 O HOH B 750 1.99
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH A 616 O HOH B 515 1554 1.96
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 ARG A 107 52.14 -119.89
REMARK 500 SER A 157 -130.30 62.69
REMARK 500 ASP A 293 98.35 -170.05
REMARK 500 TYR A 323 76.08 -118.44
REMARK 500 PRO A 336 -8.62 -56.39
REMARK 500 ARG B 107 52.01 -117.65
REMARK 500 SER B 157 -131.10 64.26
REMARK 500 ASP B 293 98.10 -169.23
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 772 DISTANCE = 6.05 ANGSTROMS
REMARK 525 HOH A 773 DISTANCE = 6.44 ANGSTROMS
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 401 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ILE A 22 O
REMARK 620 2 HOH A 551 O 96.8
REMARK 620 3 HOH B 759 O 135.0 126.6
REMARK 620 4 HOH B 766 O 90.9 133.2 69.2
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 402 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 81 O
REMARK 620 2 ASP A 81 OD1 77.6
REMARK 620 3 VAL A 84 O 79.6 102.1
REMARK 620 4 HOH A 635 O 141.8 84.4 71.6
REMARK 620 5 HOH A 726 O 142.9 93.4 137.3 70.7
REMARK 620 6 HOH A 715 O 96.1 170.3 83.8 104.9 87.2
REMARK 620 7 HOH B 518 O 75.3 86.7 150.9 137.4 68.3 84.5
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA B 401 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ILE B 22 O
REMARK 620 2 HOH B 759 O 85.4
REMARK 620 3 HOH B 766 O 89.3 74.2
REMARK 620 4 HOH B 525 O 80.7 142.3 139.9
REMARK 620 5 HOH B 771 O 88.2 80.3 154.5 64.4
REMARK 620 6 HOH A 721 O 168.8 83.4 87.1 108.7 90.5
REMARK 620 7 HOH A 723 O 106.1 144.5 72.5 73.2 132.4 82.9
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 402 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 81 O
REMARK 620 2 ASP B 81 OD1 81.4
REMARK 620 3 VAL B 84 O 82.6 108.4
REMARK 620 4 HOH B 585 O 63.8 138.7 89.4
REMARK 620 5 HOH B 687 O 142.5 75.1 77.7 146.2
REMARK 620 6 HOH B 801 O 148.0 122.3 106.2 85.3 69.0
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 403 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A 701 O
REMARK 620 2 HOH B 522 O 86.8
REMARK 620 3 HOH B 597 O 150.0 112.4
REMARK 620 4 HOH B 750 O 53.5 89.5 101.9
REMARK 620 5 HOH B 508 O 89.6 72.1 75.7 40.4
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 404 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GOL B 403 O1
REMARK 620 2 HOH B 576 O 77.0
REMARK 620 3 HOH B 748 O 124.8 66.7
REMARK 620 4 GOL B 403 O2 79.8 112.7 77.9
REMARK 620 5 HOH A 572 O 88.5 148.5 141.5 91.4
REMARK 620 6 HOH A 711 O 128.8 83.2 87.3 150.8 84.6
REMARK 620 7 HOH B 502 O 57.4 74.6 137.9 134.4 74.0 72.1
REMARK 620 8 HOH B 743 O 150.9 127.8 65.5 76.2 76.0 74.8 136.7
REMARK 620 N 1 2 3 4 5 6 7
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 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NA B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA B 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 403
DBREF 5W8O A 13 372 UNP K5B926 K5B926_MYCHD 13 372
DBREF 5W8O B 13 372 UNP K5B926 K5B926_MYCHD 13 372
SEQADV 5W8O GLY A 10 UNP K5B926 EXPRESSION TAG
SEQADV 5W8O ALA A 11 UNP K5B926 EXPRESSION TAG
SEQADV 5W8O MET A 12 UNP K5B926 EXPRESSION TAG
SEQADV 5W8O GLY B 10 UNP K5B926 EXPRESSION TAG
SEQADV 5W8O ALA B 11 UNP K5B926 EXPRESSION TAG
SEQADV 5W8O MET B 12 UNP K5B926 EXPRESSION TAG
SEQRES 1 A 363 GLY ALA MET ALA GLU GLY GLU LEU GLY ILE VAL ASP ILE
SEQRES 2 A 363 GLY ALA LEU THR LEU GLU SER GLY ALA VAL ILE ASP ASN
SEQRES 3 A 363 VAL GLN ILE ALA VAL GLU ARG TRP GLY GLU LEU SER PRO
SEQRES 4 A 363 SER ARG ASP ASN VAL VAL VAL VAL LEU HIS ALA LEU THR
SEQRES 5 A 363 GLY ASP SER HIS VAL ALA GLY PRO ALA GLY PRO ASN TYR
SEQRES 6 A 363 PRO THR PRO GLY TRP TRP ASP GLY VAL VAL GLY PRO GLY
SEQRES 7 A 363 ALA ALA ILE ASP THR ARG ARG TRP CYS ALA ILE ALA THR
SEQRES 8 A 363 ASN VAL LEU GLY GLY CYS ARG GLY SER THR GLY PRO GLY
SEQRES 9 A 363 SER LEU HIS PRO ASP GLY LYS ALA TRP GLY SER ARG PHE
SEQRES 10 A 363 PRO ALA VAL THR VAL ARG ASP GLN VAL ARG ALA ASP LEU
SEQRES 11 A 363 ALA ALA LEU ASN ALA MET GLY ILE HIS GLN VAL ALA ALA
SEQRES 12 A 363 VAL VAL GLY GLY SER MET GLY GLY ALA ARG ALA LEU GLU
SEQRES 13 A 363 TRP VAL ILE GLY HIS PRO GLU THR VAL ARG ALA GLY LEU
SEQRES 14 A 363 ILE LEU ALA VAL GLY ALA ARG ALA THR ALA ASP GLN ILE
SEQRES 15 A 363 GLY THR GLN SER THR GLN VAL ALA ALA ILE LYS ALA ASP
SEQRES 16 A 363 PRO ASN TRP GLN ASN GLY ASP TYR TYR GLY THR GLY LEU
SEQRES 17 A 363 LYS PRO ASP VAL GLY LEU GLN ILE ALA ARG ARG PHE ALA
SEQRES 18 A 363 HIS LEU THR TYR ARG GLY GLU VAL GLU LEU ASP THR ARG
SEQRES 19 A 363 PHE GLY ASN ALA PRO GLN ASP ASP GLU ASN PRO LEU LEU
SEQRES 20 A 363 GLY GLY ARG TYR ALA VAL GLU SER TYR LEU GLU TYR GLN
SEQRES 21 A 363 GLY ARG LYS LEU VAL ASP ARG PHE ASP ALA GLY THR TYR
SEQRES 22 A 363 VAL THR LEU THR ASP SER LEU SER SER HIS ASP VAL GLY
SEQRES 23 A 363 ARG GLY ARG GLY GLY VAL GLU ALA ALA LEU ARG SER CYS
SEQRES 24 A 363 GLU VAL PRO VAL VAL VAL GLY GLY PHE THR SER ASP ARG
SEQRES 25 A 363 LEU TYR PRO LEU ARG LEU GLN GLU GLU LEU ALA GLU LEU
SEQRES 26 A 363 MET PRO GLY CYS ARG GLY LEU ASN VAL VAL GLU SER ILE
SEQRES 27 A 363 TYR GLY HIS ASP GLY PHE LEU ILE GLU THR GLU ALA VAL
SEQRES 28 A 363 GLY LYS LEU ILE ARG GLN THR LEU GLU LEU ALA SER
SEQRES 1 B 363 GLY ALA MET ALA GLU GLY GLU LEU GLY ILE VAL ASP ILE
SEQRES 2 B 363 GLY ALA LEU THR LEU GLU SER GLY ALA VAL ILE ASP ASN
SEQRES 3 B 363 VAL GLN ILE ALA VAL GLU ARG TRP GLY GLU LEU SER PRO
SEQRES 4 B 363 SER ARG ASP ASN VAL VAL VAL VAL LEU HIS ALA LEU THR
SEQRES 5 B 363 GLY ASP SER HIS VAL ALA GLY PRO ALA GLY PRO ASN TYR
SEQRES 6 B 363 PRO THR PRO GLY TRP TRP ASP GLY VAL VAL GLY PRO GLY
SEQRES 7 B 363 ALA ALA ILE ASP THR ARG ARG TRP CYS ALA ILE ALA THR
SEQRES 8 B 363 ASN VAL LEU GLY GLY CYS ARG GLY SER THR GLY PRO GLY
SEQRES 9 B 363 SER LEU HIS PRO ASP GLY LYS ALA TRP GLY SER ARG PHE
SEQRES 10 B 363 PRO ALA VAL THR VAL ARG ASP GLN VAL ARG ALA ASP LEU
SEQRES 11 B 363 ALA ALA LEU ASN ALA MET GLY ILE HIS GLN VAL ALA ALA
SEQRES 12 B 363 VAL VAL GLY GLY SER MET GLY GLY ALA ARG ALA LEU GLU
SEQRES 13 B 363 TRP VAL ILE GLY HIS PRO GLU THR VAL ARG ALA GLY LEU
SEQRES 14 B 363 ILE LEU ALA VAL GLY ALA ARG ALA THR ALA ASP GLN ILE
SEQRES 15 B 363 GLY THR GLN SER THR GLN VAL ALA ALA ILE LYS ALA ASP
SEQRES 16 B 363 PRO ASN TRP GLN ASN GLY ASP TYR TYR GLY THR GLY LEU
SEQRES 17 B 363 LYS PRO ASP VAL GLY LEU GLN ILE ALA ARG ARG PHE ALA
SEQRES 18 B 363 HIS LEU THR TYR ARG GLY GLU VAL GLU LEU ASP THR ARG
SEQRES 19 B 363 PHE GLY ASN ALA PRO GLN ASP ASP GLU ASN PRO LEU LEU
SEQRES 20 B 363 GLY GLY ARG TYR ALA VAL GLU SER TYR LEU GLU TYR GLN
SEQRES 21 B 363 GLY ARG LYS LEU VAL ASP ARG PHE ASP ALA GLY THR TYR
SEQRES 22 B 363 VAL THR LEU THR ASP SER LEU SER SER HIS ASP VAL GLY
SEQRES 23 B 363 ARG GLY ARG GLY GLY VAL GLU ALA ALA LEU ARG SER CYS
SEQRES 24 B 363 GLU VAL PRO VAL VAL VAL GLY GLY PHE THR SER ASP ARG
SEQRES 25 B 363 LEU TYR PRO LEU ARG LEU GLN GLU GLU LEU ALA GLU LEU
SEQRES 26 B 363 MET PRO GLY CYS ARG GLY LEU ASN VAL VAL GLU SER ILE
SEQRES 27 B 363 TYR GLY HIS ASP GLY PHE LEU ILE GLU THR GLU ALA VAL
SEQRES 28 B 363 GLY LYS LEU ILE ARG GLN THR LEU GLU LEU ALA SER
HET NA A 401 1
HET CA A 402 1
HET CA A 403 1
HET CA A 404 1
HET NA B 401 1
HET CA B 402 1
HET GOL B 403 12
HETNAM NA SODIUM ION
HETNAM CA CALCIUM ION
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 3 NA 2(NA 1+)
FORMUL 4 CA 4(CA 2+)
FORMUL 9 GOL C3 H8 O3
FORMUL 10 HOH *593(H2 O)
HELIX 1 AA1 TRP A 80 GLY A 82 5 3
HELIX 2 AA2 TRP A 122 PHE A 126 5 5
HELIX 3 AA3 THR A 130 MET A 145 1 16
HELIX 4 AA4 SER A 157 HIS A 170 1 14
HELIX 5 AA5 THR A 187 ALA A 203 1 17
HELIX 6 AA6 TRP A 207 ASP A 211 5 5
HELIX 7 AA7 PRO A 219 ARG A 235 1 17
HELIX 8 AA8 GLY A 236 GLY A 245 1 10
HELIX 9 AA9 TYR A 260 ASP A 275 1 16
HELIX 10 AB1 ASP A 278 SER A 291 1 14
HELIX 11 AB2 GLY A 300 SER A 307 1 8
HELIX 12 AB3 PRO A 324 MET A 335 1 12
HELIX 13 AB4 TYR A 348 HIS A 350 5 3
HELIX 14 AB5 ASP A 351 GLU A 356 1 6
HELIX 15 AB6 GLU A 356 SER A 372 1 17
HELIX 16 AB7 TRP B 80 GLY B 82 5 3
HELIX 17 AB8 TRP B 122 PHE B 126 5 5
HELIX 18 AB9 THR B 130 MET B 145 1 16
HELIX 19 AC1 SER B 157 HIS B 170 1 14
HELIX 20 AC2 THR B 187 ALA B 203 1 17
HELIX 21 AC3 TRP B 207 ASP B 211 5 5
HELIX 22 AC4 PRO B 219 ARG B 235 1 17
HELIX 23 AC5 GLY B 236 GLY B 245 1 10
HELIX 24 AC6 ASN B 253 GLY B 257 5 5
HELIX 25 AC7 TYR B 260 ASP B 275 1 16
HELIX 26 AC8 ASP B 278 SER B 291 1 14
HELIX 27 AC9 GLY B 300 SER B 307 1 8
HELIX 28 AD1 PRO B 324 MET B 335 1 12
HELIX 29 AD2 TYR B 348 HIS B 350 5 3
HELIX 30 AD3 ASP B 351 GLU B 356 1 6
HELIX 31 AD4 GLU B 356 SER B 372 1 17
SHEET 1 AA1 8 GLY A 18 THR A 26 0
SHEET 2 AA1 8 VAL A 32 TRP A 43 -1 O VAL A 40 N GLY A 18
SHEET 3 AA1 8 CYS A 96 THR A 100 -1 O ALA A 97 N TRP A 43
SHEET 4 AA1 8 VAL A 53 LEU A 57 1 N VAL A 56 O ILE A 98
SHEET 5 AA1 8 VAL A 150 GLY A 156 1 O ALA A 152 N VAL A 55
SHEET 6 AA1 8 VAL A 174 LEU A 180 1 O LEU A 178 N VAL A 153
SHEET 7 AA1 8 VAL A 312 PHE A 317 1 O VAL A 313 N ILE A 179
SHEET 8 AA1 8 ASN A 342 VAL A 344 1 O VAL A 344 N GLY A 316
SHEET 1 AA2 2 VAL A 84 GLY A 85 0
SHEET 2 AA2 2 ILE A 90 ASP A 91 1 O ILE A 90 N GLY A 85
SHEET 1 AA3 8 GLY B 18 THR B 26 0
SHEET 2 AA3 8 VAL B 32 TRP B 43 -1 O VAL B 40 N GLY B 18
SHEET 3 AA3 8 CYS B 96 THR B 100 -1 O ALA B 97 N TRP B 43
SHEET 4 AA3 8 VAL B 53 LEU B 57 1 N VAL B 56 O ILE B 98
SHEET 5 AA3 8 VAL B 150 GLY B 156 1 O ALA B 152 N VAL B 55
SHEET 6 AA3 8 VAL B 174 LEU B 180 1 O LEU B 178 N VAL B 153
SHEET 7 AA3 8 VAL B 312 PHE B 317 1 O VAL B 313 N ILE B 179
SHEET 8 AA3 8 ASN B 342 VAL B 344 1 O VAL B 344 N GLY B 316
SHEET 1 AA4 2 VAL B 84 GLY B 85 0
SHEET 2 AA4 2 ILE B 90 ASP B 91 1 O ILE B 90 N GLY B 85
LINK O ILE A 22 NA NA A 401 1555 1555 2.33
LINK O ASP A 81 CA CA A 402 1555 1555 2.35
LINK OD1 ASP A 81 CA CA A 402 1555 1555 2.29
LINK O VAL A 84 CA CA A 402 1555 1555 2.42
LINK O ILE B 22 NA NA B 401 1555 1555 2.28
LINK O ASP B 81 CA CA B 402 1555 1555 2.48
LINK OD1 ASP B 81 CA CA B 402 1555 1555 2.60
LINK O VAL B 84 CA CA B 402 1555 1555 2.37
LINK NA NA A 401 O HOH A 551 1555 1555 2.74
LINK CA CA A 402 O HOH A 635 1555 1555 2.44
LINK CA CA A 402 O HOH A 726 1555 1555 2.39
LINK CA CA A 402 O HOH A 715 1555 1555 2.39
LINK CA CA A 403 O HOH A 701 1555 1555 2.48
LINK CA CA A 403 O HOH B 522 1555 1555 2.60
LINK CA CA A 403 O HOH B 597 1555 1555 2.44
LINK CA CA A 403 O HOH B 750 1555 1555 3.06
LINK CA CA A 403 O HOH B 508 1555 1555 2.52
LINK CA CA A 404 O1 GOL B 403 1555 1555 2.28
LINK CA CA A 404 O HOH B 576 1555 1555 2.42
LINK CA CA A 404 O HOH B 748 1555 1555 2.34
LINK CA CA A 404 O2 GOL B 403 1555 1555 2.55
LINK CA CA A 404 O HOH A 572 1555 1555 2.29
LINK CA CA A 404 O HOH A 711 1555 1555 2.33
LINK CA CA A 404 O HOH B 502 1555 1555 2.45
LINK CA CA A 404 O HOH B 743 1555 1555 2.39
LINK NA NA B 401 O HOH B 759 1555 1555 2.47
LINK NA NA B 401 O HOH B 766 1555 1555 2.48
LINK NA NA B 401 O HOH B 525 1555 1555 2.42
LINK NA NA B 401 O HOH B 771 1555 1555 2.56
LINK CA CA B 402 O HOH B 585 1555 1555 2.64
LINK CA CA B 402 O HOH B 687 1555 1555 2.21
LINK CA CA B 402 O HOH B 801 1555 1555 2.77
LINK NA NA A 401 O HOH B 759 1555 1554 2.63
LINK NA NA A 401 O HOH B 766 1555 1554 2.63
LINK CA CA A 402 O HOH B 518 1555 2554 2.39
LINK NA NA B 401 O HOH A 721 1555 1556 2.26
LINK NA NA B 401 O HOH A 723 1555 1556 2.42
SITE 1 AC1 4 ILE A 22 HOH A 551 HOH B 759 HOH B 766
SITE 1 AC2 5 ASP A 81 VAL A 84 HOH A 635 HOH A 715
SITE 2 AC2 5 HOH A 726
SITE 1 AC3 5 HOH A 701 HOH B 508 HOH B 522 HOH B 597
SITE 2 AC3 5 HOH B 750
SITE 1 AC4 7 HOH A 572 HOH A 711 GOL B 403 HOH B 502
SITE 2 AC4 7 HOH B 576 HOH B 743 HOH B 748
SITE 1 AC5 7 HOH A 721 HOH A 723 ILE B 22 HOH B 525
SITE 2 AC5 7 HOH B 759 HOH B 766 HOH B 771
SITE 1 AC6 5 ASP B 81 VAL B 84 HOH B 585 HOH B 687
SITE 2 AC6 5 HOH B 801
SITE 1 AC7 11 GLU A 263 CA A 404 GLN B 194 SER B 195
SITE 2 AC7 11 ASP B 287 SER B 290 HOH B 502 HOH B 510
SITE 3 AC7 11 HOH B 576 HOH B 743 HOH B 748
CRYST1 47.750 93.230 81.590 90.00 94.78 90.00 P 1 21 1 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 0.020942 0.000000 0.001752 0.00000
SCALE2 0.000000 0.010726 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012299 0.00000
TER 5084 SER A 372
TER 10255 SER B 372
MASTER 433 0 7 31 20 0 14 6 5731 2 53 56
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