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HEADER HYDROLASE 22-AUG-22 8E5W
TITLE CRYSTAL STRUCTURE OF DEHYDROALANINE HIP1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEASE;
COMPND 3 CHAIN: A;
COMPND 4 EC: 3.4.-.-,3.4.14.-;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM TUBERCULOSIS;
SOURCE 3 ORGANISM_TAXID: 1773;
SOURCE 4 GENE: TAP, ERS007688_01841;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 511693
KEYWDS SERINE PROTEASE HIP1, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR N.E.GOLDFARB,C.L.BROOKS,D.A.OSTROV
REVDAT 1 07-DEC-22 8E5W 0
JRNL AUTH C.L.BROOKS,D.A.OSTROV,N.C.SCHUMANN,S.KAKKAD,D.LI,K.PENA,
JRNL AUTH 2 B.P.WILLIAMS,N.E.GOLDFARB
JRNL TITL 2.1 ANGSTROM CRYSTAL STRUCTURE OF THE MYCOBACTERIUM
JRNL TITL 2 TUBERCULOSIS SERINE HYDROLASE, HIP1, IN ITS ANHYDRO-FORM
JRNL TITL 3 (ANHYDROHIP1).
JRNL REF BIOCHEM.BIOPHYS.RES.COMMUN. V. 630 57 2022
JRNL REFN ESSN 1090-2104
JRNL PMID 36148729
JRNL DOI 10.1016/J.BBRC.2022.09.021
REMARK 2
REMARK 2 RESOLUTION. 2.15 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.20.1_4487
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) : 2.15
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.46
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 3 NUMBER OF REFLECTIONS : 44545
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.162
REMARK 3 R VALUE (WORKING SET) : 0.160
REMARK 3 FREE R VALUE : 0.190
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.050
REMARK 3 FREE R VALUE TEST SET COUNT : 2248
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 29.4600 - 5.4100 1.00 2828 142 0.2004 0.2042
REMARK 3 2 5.4000 - 4.3000 1.00 2704 153 0.1476 0.1734
REMARK 3 3 4.2900 - 3.7500 1.00 2699 121 0.1368 0.1511
REMARK 3 4 3.7500 - 3.4100 1.00 2662 143 0.1422 0.1830
REMARK 3 5 3.4100 - 3.1700 1.00 2652 145 0.1594 0.1929
REMARK 3 6 3.1700 - 2.9800 1.00 2661 132 0.1560 0.1941
REMARK 3 7 2.9800 - 2.8300 1.00 2602 158 0.1632 0.1940
REMARK 3 8 2.8300 - 2.7100 1.00 2634 135 0.1604 0.1793
REMARK 3 9 2.7100 - 2.6000 0.99 2661 129 0.1570 0.1992
REMARK 3 10 2.6000 - 2.5100 1.00 2627 128 0.1576 0.1959
REMARK 3 11 2.5100 - 2.4400 0.99 2583 141 0.1606 0.2025
REMARK 3 12 2.4300 - 2.3700 0.99 2603 150 0.1634 0.2029
REMARK 3 13 2.3700 - 2.3000 0.99 2624 133 0.1615 0.1952
REMARK 3 14 2.3000 - 2.2500 0.99 2587 147 0.1709 0.2105
REMARK 3 15 2.2500 - 2.2000 0.99 2596 139 0.1792 0.2034
REMARK 3 16 2.2000 - 2.1500 0.99 2574 152 0.1882 0.2319
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) : 0.160
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 16.990
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 22.99
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 30.09
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 : NULL NULL
REMARK 3 ANGLE : NULL NULL
REMARK 3 CHIRALITY : NULL NULL
REMARK 3 PLANARITY : NULL NULL
REMARK 3 DIHEDRAL : NULL NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 7
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 44 THROUGH 149 )
REMARK 3 ORIGIN FOR THE GROUP (A): 20.4117 -27.7591 -10.6093
REMARK 3 T TENSOR
REMARK 3 T11: 0.1995 T22: 0.1773
REMARK 3 T33: 0.2769 T12: -0.0643
REMARK 3 T13: -0.0570 T23: 0.0644
REMARK 3 L TENSOR
REMARK 3 L11: 1.7582 L22: 1.9927
REMARK 3 L33: 3.2403 L12: 0.1142
REMARK 3 L13: 0.3232 L23: 0.4747
REMARK 3 S TENSOR
REMARK 3 S11: -0.0773 S12: 0.1464 S13: 0.3225
REMARK 3 S21: -0.2328 S22: 0.0762 S23: 0.2468
REMARK 3 S31: 0.0097 S32: -0.2575 S33: 0.0072
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 150 THROUGH 259 )
REMARK 3 ORIGIN FOR THE GROUP (A): 31.7953 -29.5053 2.9819
REMARK 3 T TENSOR
REMARK 3 T11: 0.1862 T22: 0.1847
REMARK 3 T33: 0.1883 T12: -0.0120
REMARK 3 T13: -0.0038 T23: -0.0159
REMARK 3 L TENSOR
REMARK 3 L11: 1.3074 L22: 0.8143
REMARK 3 L33: 0.4332 L12: 0.8262
REMARK 3 L13: 0.3478 L23: 0.0380
REMARK 3 S TENSOR
REMARK 3 S11: 0.0042 S12: -0.1118 S13: 0.1167
REMARK 3 S21: 0.0381 S22: -0.0202 S23: 0.1601
REMARK 3 S31: 0.0253 S32: -0.1271 S33: 0.0178
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 260 THROUGH 284 )
REMARK 3 ORIGIN FOR THE GROUP (A): 51.0228 -40.7150 -4.4345
REMARK 3 T TENSOR
REMARK 3 T11: 0.2505 T22: 0.1526
REMARK 3 T33: 0.1885 T12: 0.0026
REMARK 3 T13: -0.0013 T23: 0.0222
REMARK 3 L TENSOR
REMARK 3 L11: 6.6403 L22: 0.9273
REMARK 3 L33: 4.9343 L12: 2.5546
REMARK 3 L13: -5.7663 L23: -2.3144
REMARK 3 S TENSOR
REMARK 3 S11: -0.0099 S12: -0.1267 S13: -0.1137
REMARK 3 S21: 0.0201 S22: -0.0487 S23: 0.0094
REMARK 3 S31: 0.2598 S32: 0.1023 S33: 0.0956
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 285 THROUGH 329 )
REMARK 3 ORIGIN FOR THE GROUP (A): 61.8098 -25.8421 -5.0385
REMARK 3 T TENSOR
REMARK 3 T11: 0.1631 T22: 0.1575
REMARK 3 T33: 0.1453 T12: -0.0208
REMARK 3 T13: 0.0142 T23: 0.0469
REMARK 3 L TENSOR
REMARK 3 L11: 1.2663 L22: 2.9367
REMARK 3 L33: 2.1376 L12: -0.1124
REMARK 3 L13: -0.2850 L23: 1.8700
REMARK 3 S TENSOR
REMARK 3 S11: -0.0411 S12: 0.0524 S13: 0.0765
REMARK 3 S21: -0.0180 S22: 0.0614 S23: -0.2067
REMARK 3 S31: -0.0381 S32: 0.2881 S33: -0.0029
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 330 THROUGH 401 )
REMARK 3 ORIGIN FOR THE GROUP (A): 46.6421 -25.9881 -5.8092
REMARK 3 T TENSOR
REMARK 3 T11: 0.1724 T22: 0.1282
REMARK 3 T33: 0.1470 T12: -0.0143
REMARK 3 T13: -0.0314 T23: 0.0019
REMARK 3 L TENSOR
REMARK 3 L11: 1.6116 L22: 0.6301
REMARK 3 L33: 1.8025 L12: 0.0630
REMARK 3 L13: -0.8668 L23: 0.1100
REMARK 3 S TENSOR
REMARK 3 S11: -0.0010 S12: 0.0498 S13: 0.0963
REMARK 3 S21: -0.1134 S22: -0.0618 S23: 0.0555
REMARK 3 S31: -0.0230 S32: -0.0282 S33: 0.0614
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 402 THROUGH 431 )
REMARK 3 ORIGIN FOR THE GROUP (A): 54.0258 -35.8731 10.4532
REMARK 3 T TENSOR
REMARK 3 T11: 0.1961 T22: 0.1291
REMARK 3 T33: 0.1587 T12: -0.0172
REMARK 3 T13: -0.0116 T23: 0.0393
REMARK 3 L TENSOR
REMARK 3 L11: 1.0958 L22: 3.6664
REMARK 3 L33: 5.7259 L12: -0.2795
REMARK 3 L13: -0.8524 L23: 0.7108
REMARK 3 S TENSOR
REMARK 3 S11: -0.0880 S12: -0.1113 S13: -0.2119
REMARK 3 S21: 0.1952 S22: -0.0202 S23: -0.0852
REMARK 3 S31: 0.5537 S32: 0.0622 S33: 0.1347
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 432 THROUGH 520 )
REMARK 3 ORIGIN FOR THE GROUP (A): 32.4777 -44.9674 -6.6440
REMARK 3 T TENSOR
REMARK 3 T11: 0.2269 T22: 0.1504
REMARK 3 T33: 0.1858 T12: -0.0523
REMARK 3 T13: -0.0044 T23: 0.0016
REMARK 3 L TENSOR
REMARK 3 L11: 1.2972 L22: 0.9842
REMARK 3 L33: 0.9391 L12: 0.2018
REMARK 3 L13: 0.1867 L23: -0.0678
REMARK 3 S TENSOR
REMARK 3 S11: 0.0186 S12: 0.0391 S13: -0.1732
REMARK 3 S21: -0.1252 S22: 0.0279 S23: 0.0153
REMARK 3 S31: 0.2314 S32: -0.0971 S33: -0.0379
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 8E5W COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-AUG-22.
REMARK 100 THE DEPOSITION ID IS D_1000267804.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 06-JUL-17
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X6A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9436
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 16M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 44570
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.150
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 200 DATA REDUNDANCY : 6.100
REMARK 200 R MERGE (I) : 0.11600
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 7.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.15
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.19
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.9
REMARK 200 DATA REDUNDANCY IN SHELL : 5.40
REMARK 200 R MERGE FOR SHELL (I) : 0.56400
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 5UNO
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 68.35
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.89
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: AMMONIUM SULFATE PEG 8000 SODIUM
REMARK 280 CACODYLATE TRIHYDRATE PH 6.5, VAPOR DIFFUSION, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+2/3
REMARK 290 6555 -X,-X+Y,-Z+1/3
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 42.60067
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 85.20133
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 85.20133
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 42.60067
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 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 35
REMARK 465 PRO A 36
REMARK 465 LEU A 37
REMARK 465 GLY A 38
REMARK 465 SER A 39
REMARK 465 PRO A 40
REMARK 465 GLU A 41
REMARK 465 PHE A 42
REMARK 465 GLU A 43
REMARK 465 SER A 57
REMARK 465 SER A 58
REMARK 465 ASN A 59
REMARK 465 PRO A 60
REMARK 465 GLN A 61
REMARK 465 VAL A 62
REMARK 465 LYS A 63
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 45 CG CD CE NZ
REMARK 470 GLN A 48 CG CD OE1 NE2
REMARK 470 ARG A 56 CG CD NE CZ NH1 NH2
REMARK 470 ILE A 64 CG1 CG2 CD1
REMARK 470 PRO A 65 CG CD
REMARK 470 ASP A 83 CG OD1 OD2
REMARK 470 SER A 228 OG
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 145 -112.04 54.60
REMARK 500 CYS A 153 -53.27 -124.08
REMARK 500 SER A 228 -115.29 50.16
REMARK 500 THR A 491 160.65 73.89
REMARK 500 VAL A 492 -19.25 -154.95
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 A1242 DISTANCE = 6.01 ANGSTROMS
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 7SFM RELATED DB: PDB
REMARK 900 IDENTICAL STRUCTURE AND DATA. RE-REFINED TO INCLUDE MISSING
REMARK 900 COMPONENTS AND MUTATION
REMARK 900 RELATED ID: 5BKM RELATED DB: PDB
REMARK 900 SAME STRUCTURE AND MUTATION. DIFFERENT RYSTAL, HIGHER RESOLUTION
REMARK 900 DATA
REMARK 900 RELATED ID: 5UNO RELATED DB: PDB
REMARK 900 SAME PROTEIN, WITH MUTATION
DBREF1 8E5W A 43 520 UNP A0A654TLU9_MYCTX
DBREF2 8E5W A A0A654TLU9 41 518
SEQADV 8E5W GLY A 35 UNP A0A654TLU EXPRESSION TAG
SEQADV 8E5W PRO A 36 UNP A0A654TLU EXPRESSION TAG
SEQADV 8E5W LEU A 37 UNP A0A654TLU EXPRESSION TAG
SEQADV 8E5W GLY A 38 UNP A0A654TLU EXPRESSION TAG
SEQADV 8E5W SER A 39 UNP A0A654TLU EXPRESSION TAG
SEQADV 8E5W PRO A 40 UNP A0A654TLU EXPRESSION TAG
SEQADV 8E5W GLU A 41 UNP A0A654TLU EXPRESSION TAG
SEQADV 8E5W PHE A 42 UNP A0A654TLU EXPRESSION TAG
SEQRES 1 A 486 GLY PRO LEU GLY SER PRO GLU PHE GLU PRO LYS LEU GLY
SEQRES 2 A 486 GLN PRO VAL GLU TRP THR PRO CYS ARG SER SER ASN PRO
SEQRES 3 A 486 GLN VAL LYS ILE PRO GLY GLY ALA LEU CYS GLY LYS LEU
SEQRES 4 A 486 ALA VAL PRO VAL ASP TYR ASP ARG PRO ASP GLY ASP VAL
SEQRES 5 A 486 ALA ALA LEU ALA LEU ILE ARG PHE PRO ALA THR GLY ASP
SEQRES 6 A 486 LYS ILE GLY SER LEU VAL ILE ASN PRO GLY GLY PRO GLY
SEQRES 7 A 486 GLU SER GLY ILE GLU ALA ALA LEU GLY VAL PHE GLN THR
SEQRES 8 A 486 LEU PRO LYS ARG VAL HIS GLU ARG PHE ASP LEU VAL GLY
SEQRES 9 A 486 PHE ASP PRO ARG GLY VAL ALA SER SER ARG PRO ALA ILE
SEQRES 10 A 486 TRP CYS ASN SER ASP ALA ASP ASN ASP ARG LEU ARG ALA
SEQRES 11 A 486 GLU PRO GLN VAL ASP TYR SER ARG GLU GLY VAL ALA HIS
SEQRES 12 A 486 ILE GLU ASN GLU THR LYS GLN PHE VAL GLY ARG CYS VAL
SEQRES 13 A 486 ASP LYS MET GLY LYS ASN PHE LEU ALA HIS VAL GLY THR
SEQRES 14 A 486 VAL ASN VAL ALA LYS ASP LEU ASP ALA ILE ARG ALA ALA
SEQRES 15 A 486 LEU GLY ASP ASP LYS LEU THR TYR LEU GLY TYR SER TYR
SEQRES 16 A 486 GLY THR ARG ILE GLY SER ALA TYR ALA GLU GLU PHE PRO
SEQRES 17 A 486 GLN ARG VAL ARG ALA MET ILE LEU ASP GLY ALA VAL ASP
SEQRES 18 A 486 PRO ASN ALA ASP PRO ILE GLU ALA GLU LEU ARG GLN ALA
SEQRES 19 A 486 LYS GLY PHE GLN ASP ALA PHE ASN ASN TYR ALA ALA ASP
SEQRES 20 A 486 CYS ALA LYS ASN ALA GLY CYS PRO LEU GLY ALA ASP PRO
SEQRES 21 A 486 ALA LYS ALA VAL GLU VAL TYR HIS SER LEU VAL ASP PRO
SEQRES 22 A 486 LEU VAL ASP PRO ASP ASN PRO ARG ILE SER ARG PRO ALA
SEQRES 23 A 486 ARG THR LYS ASP PRO ARG GLY LEU SER TYR SER ASP ALA
SEQRES 24 A 486 ILE VAL GLY THR ILE MET ALA LEU TYR SER PRO ASN LEU
SEQRES 25 A 486 TRP GLN HIS LEU THR ASP GLY LEU SER GLU LEU VAL ASP
SEQRES 26 A 486 ASN ARG GLY ASP THR LEU LEU ALA LEU ALA ASP MET TYR
SEQRES 27 A 486 MET ARG ARG ASP SER HIS GLY ARG TYR ASN ASN SER GLY
SEQRES 28 A 486 ASP ALA ARG VAL ALA ILE ASN CYS VAL ASP GLN PRO PRO
SEQRES 29 A 486 VAL THR ASP ARG ASP LYS VAL ILE ASP GLU ASP ARG ARG
SEQRES 30 A 486 ALA ARG GLU ILE ALA PRO PHE MET SER TYR GLY LYS PHE
SEQRES 31 A 486 THR GLY ASP ALA PRO LEU GLY THR CYS ALA PHE TRP PRO
SEQRES 32 A 486 VAL PRO PRO THR SER GLN PRO HIS ALA VAL SER ALA PRO
SEQRES 33 A 486 GLY LEU VAL PRO THR VAL VAL VAL SER THR THR HIS ASP
SEQRES 34 A 486 PRO ALA THR PRO TYR LYS ALA GLY VAL ASP LEU ALA ASN
SEQRES 35 A 486 GLN LEU ARG GLY SER LEU LEU THR PHE ASP GLY THR GLN
SEQRES 36 A 486 HIS THR VAL VAL PHE GLN GLY ASP SER CYS ILE ASP GLU
SEQRES 37 A 486 TYR VAL THR ALA TYR LEU ILE GLY GLY THR THR PRO PRO
SEQRES 38 A 486 SER GLY ALA LYS CYS
HET PLM A 601 49
HET SO4 A 602 5
HET PEG A 603 17
HET PEG A 604 17
HETNAM PLM PALMITIC ACID
HETNAM SO4 SULFATE ION
HETNAM PEG DI(HYDROXYETHYL)ETHER
FORMUL 2 PLM C16 H32 O2
FORMUL 3 SO4 O4 S 2-
FORMUL 4 PEG 2(C4 H10 O3)
FORMUL 6 HOH *542(H2 O)
HELIX 1 AA1 SER A 114 LEU A 126 1 13
HELIX 2 AA2 PRO A 127 ARG A 133 1 7
HELIX 3 AA3 SER A 155 ALA A 164 1 10
HELIX 4 AA4 SER A 171 MET A 193 1 23
HELIX 5 AA5 GLY A 194 HIS A 200 1 7
HELIX 6 AA6 GLY A 202 LEU A 217 1 16
HELIX 7 AA7 TYR A 229 PHE A 241 1 13
HELIX 8 AA8 ASP A 259 LYS A 284 1 26
HELIX 9 AA9 ASP A 293 ALA A 295 5 3
HELIX 10 AB1 LYS A 296 ASP A 306 1 11
HELIX 11 AB2 PRO A 307 VAL A 309 5 3
HELIX 12 AB3 SER A 329 LEU A 341 1 13
HELIX 13 AB4 TYR A 342 ASN A 345 5 4
HELIX 14 AB5 LEU A 346 ASP A 359 1 14
HELIX 15 AB6 GLY A 362 ARG A 374 1 13
HELIX 16 AB7 ASN A 383 ASP A 395 1 13
HELIX 17 AB8 ASP A 401 ALA A 416 1 16
HELIX 18 AB9 PRO A 417 SER A 420 5 4
HELIX 19 AC1 GLY A 431 TRP A 436 5 6
HELIX 20 AC2 PRO A 467 ARG A 479 1 13
HELIX 21 AC3 ASP A 497 GLY A 511 1 15
SHEET 1 AA110 THR A 53 PRO A 54 0
SHEET 2 AA110 LEU A 69 PRO A 76 -1 O CYS A 70 N THR A 53
SHEET 3 AA110 VAL A 86 PHE A 94 -1 O LEU A 89 N LEU A 73
SHEET 4 AA110 PHE A 134 PHE A 139 -1 O LEU A 136 N PHE A 94
SHEET 5 AA110 GLY A 102 ASN A 107 1 N LEU A 104 O ASP A 135
SHEET 6 AA110 LEU A 222 TYR A 227 1 O THR A 223 N VAL A 105
SHEET 7 AA110 VAL A 245 ASP A 251 1 O ASP A 251 N GLY A 226
SHEET 8 AA110 VAL A 456 THR A 460 1 O VAL A 458 N LEU A 250
SHEET 9 AA110 SER A 481 PHE A 485 1 O SER A 481 N VAL A 457
SHEET 10 AA110 LYS A 519 CYS A 520 1 O CYS A 520 N THR A 484
SSBOND 1 CYS A 55 CYS A 70 1555 1555 2.03
SSBOND 2 CYS A 153 CYS A 189 1555 1555 2.03
SSBOND 3 CYS A 282 CYS A 288 1555 1555 2.03
SSBOND 4 CYS A 393 CYS A 433 1555 1555 2.04
SSBOND 5 CYS A 499 CYS A 520 1555 1555 2.04
CISPEP 1 GLY A 110 PRO A 111 0 -2.02
CISPEP 2 ARG A 148 PRO A 149 0 -5.15
CRYST1 104.891 104.891 127.802 90.00 90.00 120.00 P 31 2 1 6
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 0.009534 0.005504 0.000000 0.00000
SCALE2 0.000000 0.011009 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007825 0.00000
TER 6933 CYS A 520
MASTER 398 0 4 21 10 0 0 6 4109 1 98 38
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