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HEADER TRANSFERASE 22-JUN-17 5W8P
TITLE HOMOSERINE TRANSACETYLASE META FROM MYCOBACTERIUM ABSCESSUS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HOMOSERINE O-ACETYLTRANSFERASE;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: UNP RESIDUES 13-379;
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 ABSCESSUS;
SOURCE 3 ORGANISM_TAXID: 561007;
SOURCE 4 STRAIN: ATCC 19977 / DSM 44196 / CIP 104536 / JCM 13569 / NCTC 13031
SOURCE 5 / TMC 1543;
SOURCE 6 ATCC: 19977;
SOURCE 7 GENE: METX, MAB_3688;
SOURCE 8 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 9 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 10 EXPRESSION_SYSTEM_STRAIN: ROSETTA2(DE3);
SOURCE 11 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 12 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 E.S.RODRIGUEZ,R.W.REED,K.V.KOROTKOV
REVDAT 2 27-SEP-17 5W8P 1 REMARK
REVDAT 1 12-JUL-17 5W8P 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. 1.69 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) : 1.69
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.48
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.170
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.0
REMARK 3 NUMBER OF REFLECTIONS : 128098
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.159
REMARK 3 R VALUE (WORKING SET) : 0.158
REMARK 3 FREE R VALUE : 0.174
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.030
REMARK 3 FREE R VALUE TEST SET COUNT : 6439
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 49.5012 - 5.2492 0.97 7663 464 0.1786 0.1804
REMARK 3 2 5.2492 - 4.1671 0.99 7847 423 0.1285 0.1389
REMARK 3 3 4.1671 - 3.6405 0.99 7803 491 0.1290 0.1331
REMARK 3 4 3.6405 - 3.3078 0.96 7636 412 0.1394 0.1502
REMARK 3 5 3.3078 - 3.0707 0.99 7925 368 0.1467 0.1526
REMARK 3 6 3.0707 - 2.8897 0.99 7920 358 0.1445 0.1617
REMARK 3 7 2.8897 - 2.7450 0.99 7922 420 0.1431 0.1504
REMARK 3 8 2.7450 - 2.6255 0.99 7856 437 0.1447 0.1706
REMARK 3 9 2.6255 - 2.5244 0.99 7832 467 0.1408 0.1807
REMARK 3 10 2.5244 - 2.4373 0.99 7848 424 0.1427 0.1840
REMARK 3 11 2.4373 - 2.3611 0.96 7751 387 0.1457 0.1749
REMARK 3 12 2.3611 - 2.2936 0.98 7907 336 0.1381 0.1624
REMARK 3 13 2.2936 - 2.2332 0.99 7878 434 0.1380 0.1771
REMARK 3 14 2.2332 - 2.1788 0.98 7828 411 0.1421 0.1640
REMARK 3 15 2.1788 - 2.1292 0.99 7831 377 0.1420 0.1553
REMARK 3 16 2.1292 - 2.0839 0.98 7869 385 0.1524 0.1746
REMARK 3 17 2.0839 - 2.0422 0.98 7845 381 0.1668 0.1928
REMARK 3 18 2.0422 - 2.0037 0.98 7902 361 0.1731 0.1844
REMARK 3 19 2.0037 - 1.9679 0.99 7776 458 0.1799 0.2148
REMARK 3 20 1.9679 - 1.9345 0.98 7881 383 0.1813 0.1949
REMARK 3 21 1.9345 - 1.9033 0.98 7742 375 0.1917 0.2104
REMARK 3 22 1.9033 - 1.8741 0.96 7653 404 0.2094 0.2246
REMARK 3 23 1.8741 - 1.8465 0.98 7739 497 0.2082 0.2320
REMARK 3 24 1.8465 - 1.8205 0.98 7737 441 0.2171 0.2301
REMARK 3 25 1.8205 - 1.7959 0.98 7839 414 0.2268 0.2372
REMARK 3 26 1.7959 - 1.7726 0.98 7752 424 0.2419 0.2519
REMARK 3 27 1.7726 - 1.7504 0.97 7718 441 0.2500 0.2604
REMARK 3 28 1.7504 - 1.7293 0.98 7821 403 0.2619 0.2705
REMARK 3 29 1.7293 - 1.7092 0.98 7746 426 0.2716 0.2751
REMARK 3 30 1.7092 - 1.6900 0.96 7687 402 0.2843 0.3172
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) : 16.900
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 18.87
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 23.93
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 : 0.006 5642
REMARK 3 ANGLE : 0.789 7697
REMARK 3 CHIRALITY : 0.052 851
REMARK 3 PLANARITY : 0.005 1026
REMARK 3 DIHEDRAL : 9.816 3272
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 5W8P 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_1000228596.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 12-JUN-17
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 9.0
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 : 128103
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.690
REMARK 200 RESOLUTION RANGE LOW (A) : 49.480
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 200 DATA REDUNDANCY : 5.647
REMARK 200 R MERGE (I) : 0.12400
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 8.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.69
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.73
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.9
REMARK 200 DATA REDUNDANCY IN SHELL : 5.79
REMARK 200 R MERGE FOR SHELL (I) : 0.96300
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 1.780
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: 5W8O
REMARK 200
REMARK 200 REMARK: HEXAGONAL PRISM
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 64.70
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.48
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.2M SODIUM DIHYDROGEN PHOSPHATE, 0.8M
REMARK 280 DIPOTASSIUM HYDROGEN PHOSPHATE, 0.2M LITHIUM SULFATE, 0.1 M CHES
REMARK 280 PH 9.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 294K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 65
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+1/6
REMARK 290 6555 X-Y,X,Z+5/6
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 34.20000
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 17.10000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 25.65000
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 8.55000
REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 42.75000
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: 5450 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 26960 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -42.0 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 LYS B 379
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 HE ARG A 282 O HOH A 504 1.59
REMARK 500 O HOH A 587 O HOH A 769 2.18
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 B 652 O HOH B 700 4664 2.03
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 HIS A 97 -32.66 -130.32
REMARK 500 SER A 160 -134.47 61.66
REMARK 500 ASP A 214 56.16 -107.17
REMARK 500 PRO A 222 45.79 -80.74
REMARK 500 ALA A 263 -109.17 -117.11
REMARK 500 ASP A 300 99.28 -167.55
REMARK 500 HIS B 97 -30.74 -130.11
REMARK 500 SER B 160 -134.66 64.87
REMARK 500 ASP B 214 49.71 -108.74
REMARK 500 ALA B 263 -118.15 -113.94
REMARK 500 ASP B 300 99.23 -168.90
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 902 DISTANCE = 5.88 ANGSTROMS
REMARK 525 HOH B 885 DISTANCE = 6.02 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 K A 401 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ALA A 339 O
REMARK 620 2 ASP A 340 O 74.9
REMARK 620 3 LEU A 342 O 88.0 96.1
REMARK 620 4 CYS A 345 O 85.9 160.8 83.5
REMARK 620 5 HOH A 784 O 153.1 131.0 95.1 68.0
REMARK 620 6 HOH A 827 O 90.8 73.9 169.9 106.5 90.5
REMARK 620 7 HOH A 812 O 139.6 65.6 88.3 133.5 67.2 86.1
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K B 401 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ALA B 339 O
REMARK 620 2 ASP B 340 O 73.0
REMARK 620 3 LEU B 342 O 88.1 95.3
REMARK 620 4 CYS B 345 O 90.2 163.2 82.6
REMARK 620 5 HOH B 803 O 136.8 64.4 89.0 132.0
REMARK 620 6 HOH B 809 O 76.8 92.1 160.4 85.0 110.5
REMARK 620 7 HOH B 810 O 161.6 121.9 100.2 74.8 60.4 91.1
REMARK 620 N 1 2 3 4 5 6
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue K A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 A 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 A 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 A 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 A 406
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 407
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue K B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 B 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 403
DBREF 5W8P A 13 379 UNP B1MG17 B1MG17_MYCA9 13 379
DBREF 5W8P B 13 379 UNP B1MG17 B1MG17_MYCA9 13 379
SEQADV 5W8P GLY A 10 UNP B1MG17 EXPRESSION TAG
SEQADV 5W8P ALA A 11 UNP B1MG17 EXPRESSION TAG
SEQADV 5W8P MET A 12 UNP B1MG17 EXPRESSION TAG
SEQADV 5W8P GLY B 10 UNP B1MG17 EXPRESSION TAG
SEQADV 5W8P ALA B 11 UNP B1MG17 EXPRESSION TAG
SEQADV 5W8P MET B 12 UNP B1MG17 EXPRESSION TAG
SEQRES 1 A 370 GLY ALA MET ALA LEU PRO GLN GLY ASP GLU ILE ALA TYR
SEQRES 2 A 370 VAL PRO ILE GLY SER ILE THR LEU GLU SER GLY ALA VAL
SEQRES 3 A 370 ILE ASP ASP VAL THR ILE ALA VAL GLN SER TRP GLY GLU
SEQRES 4 A 370 LEU SER PRO ARG ARG ASP ASN VAL VAL PHE VAL CYS HIS
SEQRES 5 A 370 ALA LEU THR ALA ASP SER HIS VAL VAL GLY PRO ALA GLY
SEQRES 6 A 370 PRO ASP HIS ILE THR GLY GLY TRP TRP GLU GLY ILE ILE
SEQRES 7 A 370 GLY PRO GLY ALA ALA ILE ASP THR ASP HIS TRP CYS ALA
SEQRES 8 A 370 VAL ALA THR ASN VAL LEU GLY GLY CYS ARG GLY THR THR
SEQRES 9 A 370 GLY PRO THR SER LEU ALA ARG ASP GLY LYS PRO TRP GLY
SEQRES 10 A 370 SER ARG PHE PRO GLU VAL SER VAL ARG ASP GLN VAL ASN
SEQRES 11 A 370 ALA ASP VAL ALA ALA LEU ALA GLN LEU GLY ILE THR GLU
SEQRES 12 A 370 VAL ALA ALA VAL VAL GLY GLY SER MET GLY GLY ALA ARG
SEQRES 13 A 370 ALA LEU GLU TRP ALA VAL MET HIS PRO ASP ALA VAL ARG
SEQRES 14 A 370 ALA ALA LEU VAL LEU ALA VAL GLY ALA ARG ALA THR GLY
SEQRES 15 A 370 ASP GLN ILE GLY THR GLN SER THR GLN ILE ALA ALA ILE
SEQRES 16 A 370 GLN THR ASP PRO ASP TRP GLN GLY GLY ASP TYR HIS GLY
SEQRES 17 A 370 SER GLY ARG SER PRO GLY LYS GLY LEU ASN LEU ALA ARG
SEQRES 18 A 370 ARG ILE ALA HIS LEU THR TYR ARG GLY GLU VAL GLU LEU
SEQRES 19 A 370 ASP THR ARG PHE GLY ASN ASP PRO GLN VAL GLY PRO ASP
SEQRES 20 A 370 GLY PRO GLU ASP PRO TRP ALA ASP GLY ARG TYR ALA VAL
SEQRES 21 A 370 GLN SER TYR LEU GLU HIS GLN GLY ASN LYS PHE VAL ARG
SEQRES 22 A 370 ARG PHE ASP ALA GLY SER TYR VAL ILE LEU THR GLU SER
SEQRES 23 A 370 LEU ASN ARG HIS ASP VAL GLY ARG GLY ARG GLY GLY VAL
SEQRES 24 A 370 GLU LYS ALA LEU ARG GLY CYS PRO VAL PRO VAL VAL VAL
SEQRES 25 A 370 GLY GLY ILE THR SER ASP ARG LEU TYR PRO LEU ARG LEU
SEQRES 26 A 370 GLN GLU GLU LEU ALA ASP LEU LEU PRO GLY CYS THR GLY
SEQRES 27 A 370 LEU ARG VAL VAL GLU SER VAL HIS GLY HIS ASP ALA PHE
SEQRES 28 A 370 LEU ILE GLU PHE ASP ALA VAL SER GLU LEU VAL ARG GLU
SEQRES 29 A 370 THR LEU ALA LEU ALA LYS
SEQRES 1 B 370 GLY ALA MET ALA LEU PRO GLN GLY ASP GLU ILE ALA TYR
SEQRES 2 B 370 VAL PRO ILE GLY SER ILE THR LEU GLU SER GLY ALA VAL
SEQRES 3 B 370 ILE ASP ASP VAL THR ILE ALA VAL GLN SER TRP GLY GLU
SEQRES 4 B 370 LEU SER PRO ARG ARG ASP ASN VAL VAL PHE VAL CYS HIS
SEQRES 5 B 370 ALA LEU THR ALA ASP SER HIS VAL VAL GLY PRO ALA GLY
SEQRES 6 B 370 PRO ASP HIS ILE THR GLY GLY TRP TRP GLU GLY ILE ILE
SEQRES 7 B 370 GLY PRO GLY ALA ALA ILE ASP THR ASP HIS TRP CYS ALA
SEQRES 8 B 370 VAL ALA THR ASN VAL LEU GLY GLY CYS ARG GLY THR THR
SEQRES 9 B 370 GLY PRO THR SER LEU ALA ARG ASP GLY LYS PRO TRP GLY
SEQRES 10 B 370 SER ARG PHE PRO GLU VAL SER VAL ARG ASP GLN VAL ASN
SEQRES 11 B 370 ALA ASP VAL ALA ALA LEU ALA GLN LEU GLY ILE THR GLU
SEQRES 12 B 370 VAL ALA ALA VAL VAL GLY GLY SER MET GLY GLY ALA ARG
SEQRES 13 B 370 ALA LEU GLU TRP ALA VAL MET HIS PRO ASP ALA VAL ARG
SEQRES 14 B 370 ALA ALA LEU VAL LEU ALA VAL GLY ALA ARG ALA THR GLY
SEQRES 15 B 370 ASP GLN ILE GLY THR GLN SER THR GLN ILE ALA ALA ILE
SEQRES 16 B 370 GLN THR ASP PRO ASP TRP GLN GLY GLY ASP TYR HIS GLY
SEQRES 17 B 370 SER GLY ARG SER PRO GLY LYS GLY LEU ASN LEU ALA ARG
SEQRES 18 B 370 ARG ILE ALA HIS LEU THR TYR ARG GLY GLU VAL GLU LEU
SEQRES 19 B 370 ASP THR ARG PHE GLY ASN ASP PRO GLN VAL GLY PRO ASP
SEQRES 20 B 370 GLY PRO GLU ASP PRO TRP ALA ASP GLY ARG TYR ALA VAL
SEQRES 21 B 370 GLN SER TYR LEU GLU HIS GLN GLY ASN LYS PHE VAL ARG
SEQRES 22 B 370 ARG PHE ASP ALA GLY SER TYR VAL ILE LEU THR GLU SER
SEQRES 23 B 370 LEU ASN ARG HIS ASP VAL GLY ARG GLY ARG GLY GLY VAL
SEQRES 24 B 370 GLU LYS ALA LEU ARG GLY CYS PRO VAL PRO VAL VAL VAL
SEQRES 25 B 370 GLY GLY ILE THR SER ASP ARG LEU TYR PRO LEU ARG LEU
SEQRES 26 B 370 GLN GLU GLU LEU ALA ASP LEU LEU PRO GLY CYS THR GLY
SEQRES 27 B 370 LEU ARG VAL VAL GLU SER VAL HIS GLY HIS ASP ALA PHE
SEQRES 28 B 370 LEU ILE GLU PHE ASP ALA VAL SER GLU LEU VAL ARG GLU
SEQRES 29 B 370 THR LEU ALA LEU ALA LYS
HET K A 401 1
HET PO4 A 402 5
HET PO4 A 403 5
HET PO4 A 404 5
HET PO4 A 405 5
HET PO4 A 406 5
HET GOL A 407 14
HET K B 401 1
HET PO4 B 402 5
HET GOL B 403 14
HETNAM K POTASSIUM ION
HETNAM PO4 PHOSPHATE ION
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 3 K 2(K 1+)
FORMUL 4 PO4 6(O4 P 3-)
FORMUL 9 GOL 2(C3 H8 O3)
FORMUL 13 HOH *787(H2 O)
HELIX 1 AA1 TRP A 125 PHE A 129 5 5
HELIX 2 AA2 SER A 133 LEU A 148 1 16
HELIX 3 AA3 SER A 160 HIS A 173 1 14
HELIX 4 AA4 THR A 190 THR A 206 1 17
HELIX 5 AA5 TRP A 210 ASP A 214 5 5
HELIX 6 AA6 PRO A 222 ARG A 238 1 17
HELIX 7 AA7 GLY A 239 PHE A 247 1 9
HELIX 8 AA8 TYR A 267 ARG A 282 1 16
HELIX 9 AA9 ASP A 285 ARG A 298 1 14
HELIX 10 AB1 GLY A 307 GLY A 314 1 8
HELIX 11 AB2 PRO A 331 LEU A 342 1 12
HELIX 12 AB3 HIS A 355 HIS A 357 5 3
HELIX 13 AB4 ASP A 358 GLU A 363 1 6
HELIX 14 AB5 GLU A 363 LYS A 379 1 17
HELIX 15 AB6 TRP B 125 PHE B 129 5 5
HELIX 16 AB7 SER B 133 LEU B 148 1 16
HELIX 17 AB8 SER B 160 HIS B 173 1 14
HELIX 18 AB9 THR B 190 THR B 206 1 17
HELIX 19 AC1 ASP B 207 ASP B 214 5 8
HELIX 20 AC2 PRO B 222 ARG B 238 1 17
HELIX 21 AC3 GLY B 239 PHE B 247 1 9
HELIX 22 AC4 TYR B 267 ARG B 282 1 16
HELIX 23 AC5 ASP B 285 ARG B 298 1 14
HELIX 24 AC6 GLY B 307 GLY B 314 1 8
HELIX 25 AC7 PRO B 331 LEU B 342 1 12
HELIX 26 AC8 HIS B 355 HIS B 357 5 3
HELIX 27 AC9 ASP B 358 GLU B 363 1 6
HELIX 28 AD1 GLU B 363 ALA B 378 1 16
SHEET 1 AA1 8 ALA A 21 THR A 29 0
SHEET 2 AA1 8 VAL A 35 TRP A 46 -1 O ILE A 41 N VAL A 23
SHEET 3 AA1 8 CYS A 99 THR A 103 -1 O ALA A 100 N TRP A 46
SHEET 4 AA1 8 VAL A 56 CYS A 60 1 N VAL A 59 O VAL A 101
SHEET 5 AA1 8 VAL A 153 GLY A 159 1 O VAL A 157 N CYS A 60
SHEET 6 AA1 8 VAL A 177 LEU A 183 1 O LEU A 181 N VAL A 156
SHEET 7 AA1 8 VAL A 319 ILE A 324 1 O VAL A 320 N VAL A 182
SHEET 8 AA1 8 ARG A 349 VAL A 351 1 O VAL A 351 N GLY A 323
SHEET 1 AA2 2 ILE A 87 GLY A 88 0
SHEET 2 AA2 2 ILE A 93 ASP A 94 1 O ILE A 93 N GLY A 88
SHEET 1 AA3 2 VAL A 253 GLY A 254 0
SHEET 2 AA3 2 GLY A 257 PRO A 258 -1 O GLY A 257 N GLY A 254
SHEET 1 AA4 8 ALA B 21 THR B 29 0
SHEET 2 AA4 8 VAL B 35 TRP B 46 -1 O ILE B 41 N VAL B 23
SHEET 3 AA4 8 CYS B 99 THR B 103 -1 O ALA B 100 N TRP B 46
SHEET 4 AA4 8 VAL B 56 CYS B 60 1 N VAL B 59 O VAL B 101
SHEET 5 AA4 8 VAL B 153 GLY B 159 1 O VAL B 157 N CYS B 60
SHEET 6 AA4 8 VAL B 177 LEU B 183 1 O LEU B 181 N VAL B 156
SHEET 7 AA4 8 VAL B 319 ILE B 324 1 O VAL B 320 N VAL B 182
SHEET 8 AA4 8 ARG B 349 VAL B 351 1 O VAL B 351 N GLY B 323
SHEET 1 AA5 2 ILE B 87 GLY B 88 0
SHEET 2 AA5 2 ILE B 93 ASP B 94 1 O ILE B 93 N GLY B 88
SHEET 1 AA6 2 VAL B 253 GLY B 254 0
SHEET 2 AA6 2 GLY B 257 PRO B 258 -1 O GLY B 257 N GLY B 254
LINK O ALA A 339 K K A 401 1555 1555 2.67
LINK O ASP A 340 K K A 401 1555 1555 3.07
LINK O LEU A 342 K K A 401 1555 1555 2.67
LINK O CYS A 345 K K A 401 1555 1555 2.74
LINK O ALA B 339 K K B 401 1555 1555 2.65
LINK O ASP B 340 K K B 401 1555 1555 3.09
LINK O LEU B 342 K K B 401 1555 1555 2.66
LINK O CYS B 345 K K B 401 1555 1555 2.79
LINK K K A 401 O HOH A 784 1555 1555 2.90
LINK K K A 401 O HOH A 827 1555 1555 2.90
LINK K K A 401 O HOH A 812 1555 1555 2.98
LINK K K B 401 O HOH B 803 1555 1555 3.05
LINK K K B 401 O HOH B 809 1555 1555 2.72
LINK K K B 401 O HOH B 810 1555 1555 2.82
SITE 1 AC1 7 ALA A 339 ASP A 340 LEU A 342 CYS A 345
SITE 2 AC1 7 HOH A 784 HOH A 812 HOH A 827
SITE 1 AC2 3 HIS A 275 ASN A 278 ARG A 282
SITE 1 AC3 9 THR A 29 TYR A 215 HIS A 216 GLY A 217
SITE 2 AC3 9 HOH A 545 HOH A 569 HOH A 589 HOH A 625
SITE 3 AC3 9 HOH A 637
SITE 1 AC4 3 GLY A 10 LYS A 279 ARG A 283
SITE 1 AC5 3 ARG A 188 GLU A 337 HOH A 537
SITE 1 AC6 3 ALA A 11 ARG A 53 HIS A 275
SITE 1 AC7 11 ASP A 37 GLY A 108 CYS A 109 ARG A 110
SITE 2 AC7 11 GLY A 111 THR A 112 THR A 116 SER A 117
SITE 3 AC7 11 ARG A 120 HOH A 526 HOH A 579
SITE 1 AC8 7 ALA B 339 ASP B 340 LEU B 342 CYS B 345
SITE 2 AC8 7 HOH B 803 HOH B 809 HOH B 810
SITE 1 AC9 3 HIS B 275 ASN B 278 ARG B 282
SITE 1 AD1 9 TYR B 215 HIS B 216 GLY B 217 SER B 218
SITE 2 AD1 9 GLY B 219 ARG B 220 HOH B 518 HOH B 561
SITE 3 AD1 9 HOH B 632
CRYST1 197.920 197.920 51.300 90.00 90.00 120.00 P 65 12
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 0.005053 0.002917 0.000000 0.00000
SCALE2 0.000000 0.005834 0.000000 0.00000
SCALE3 0.000000 0.000000 0.019493 0.00000
TER 5423 LYS A 379
TER 10823 ALA B 378
MASTER 383 0 10 28 24 0 18 6 6319 2 76 58
END |