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HEADER TRANSFERASE 18-JUL-16 5KWJ
TITLE M.TB AG85C MODIFIED AT C209 BY AMINO-EBSELEN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DIACYLGLYCEROL ACYLTRANSFERASE/MYCOLYLTRANSFERASE AG85C;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: UNP RESIDUES 47-340;
COMPND 5 SYNONYM: DGAT,ACYL-COA:DIACYLGLYCEROL ACYLTRANSFERASE,ANTIGEN 85
COMPND 6 COMPLEX C,AG85C,FIBRONECTIN-BINDING PROTEIN C,FBPS C;
COMPND 7 EC: 2.3.1.122,2.3.1.20;
COMPND 8 ENGINEERED: YES;
COMPND 9 OTHER_DETAILS: EBSELEN DERIVATIVE
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM TUBERCULOSIS;
SOURCE 3 ORGANISM_TAXID: 1773;
SOURCE 4 GENE: FBPC, MPT45, MT0137;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS COVALENT INHIBITOR, ACYL-TRANSFERASE, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR C.M.GOINS,D.R.RONNING
REVDAT 3 27-SEP-17 5KWJ 1 REMARK
REVDAT 2 24-MAY-17 5KWJ 1 JRNL
REVDAT 1 29-MAR-17 5KWJ 0
JRNL AUTH C.M.GOINS,S.DAJNOWICZ,S.THANNA,S.J.SUCHECK,J.M.PARKS,
JRNL AUTH 2 D.R.RONNING
JRNL TITL EXPLORING COVALENT ALLOSTERIC INHIBITION OF ANTIGEN 85C FROM
JRNL TITL 2 MYCOBACTERIUM TUBERCULOSIS BY EBSELEN DERIVATIVES.
JRNL REF ACS INFECT DIS V. 3 378 2017
JRNL REFN ESSN 2373-8227
JRNL PMID 28285521
JRNL DOI 10.1021/ACSINFECDIS.7B00003
REMARK 2
REMARK 2 RESOLUTION. 2.01 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX DEV_1833
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) : 2.01
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.51
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 3 NUMBER OF REFLECTIONS : 42326
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.164
REMARK 3 R VALUE (WORKING SET) : 0.162
REMARK 3 FREE R VALUE : 0.197
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.030
REMARK 3 FREE R VALUE TEST SET COUNT : 2131
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 49.5224 - 4.9552 1.00 2865 140 0.1646 0.1870
REMARK 3 2 4.9552 - 3.9336 1.00 2738 150 0.1399 0.1555
REMARK 3 3 3.9336 - 3.4365 1.00 2725 149 0.1547 0.1820
REMARK 3 4 3.4365 - 3.1224 1.00 2710 138 0.1732 0.2231
REMARK 3 5 3.1224 - 2.8986 1.00 2710 144 0.1729 0.2110
REMARK 3 6 2.8986 - 2.7277 1.00 2657 164 0.1715 0.2163
REMARK 3 7 2.7277 - 2.5911 1.00 2671 132 0.1673 0.2151
REMARK 3 8 2.5911 - 2.4783 1.00 2706 141 0.1735 0.1873
REMARK 3 9 2.4783 - 2.3829 1.00 2683 138 0.1751 0.2211
REMARK 3 10 2.3829 - 2.3007 1.00 2658 145 0.1662 0.2109
REMARK 3 11 2.3007 - 2.2288 1.00 2656 137 0.1612 0.2114
REMARK 3 12 2.2288 - 2.1650 1.00 2696 132 0.1584 0.1900
REMARK 3 13 2.1650 - 2.1080 1.00 2688 153 0.1654 0.2134
REMARK 3 14 2.1080 - 2.0566 1.00 2638 141 0.1641 0.2230
REMARK 3 15 2.0566 - 2.0099 0.90 2394 127 0.1685 0.2460
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) : 0.170
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 19.910
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.008 4604
REMARK 3 ANGLE : 1.090 6298
REMARK 3 CHIRALITY : 0.045 620
REMARK 3 PLANARITY : 0.005 840
REMARK 3 DIHEDRAL : 15.281 1616
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 5KWJ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-JUL-16.
REMARK 100 THE DEPOSITION ID IS D_1000219123.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-DEC-14
REMARK 200 TEMPERATURE (KELVIN) : 80
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 21-ID-F
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97872
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 42348
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.010
REMARK 200 RESOLUTION RANGE LOW (A) : 49.510
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 200 DATA REDUNDANCY : 14.90
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 20.9100
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
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: PHENIX
REMARK 200 STARTING MODEL: 4QDU
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 47.99
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.37
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M AMMONIUM ACETATE, 0.05 HEPES PH
REMARK 280 7.5, 12.5 % W/V POLYETHYLENE GLYCOL 3,350, VAPOR DIFFUSION,
REMARK 280 HANGING DROP, TEMPERATURE 289.15K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 80.97500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 80.97500
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 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 44.23700
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 44.23950
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 44.23700
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 44.23950
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 80.97500
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 44.23700
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 44.23950
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 80.97500
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 44.23700
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 44.23950
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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 350
REMARK 350 BIOMOLECULE: 2
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: 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 ALA A 283
REMARK 465 THR A 284
REMARK 465 PRO A 285
REMARK 465 PRO A 286
REMARK 465 ALA A 287
REMARK 465 ALA A 288
REMARK 465 PRO A 289
REMARK 465 ALA A 290
REMARK 465 ALA A 291
REMARK 465 PRO A 292
REMARK 465 ALA A 293
REMARK 465 ALA A 294
REMARK 465 LEU A 295
REMARK 465 GLU A 296
REMARK 465 HIS A 297
REMARK 465 HIS A 298
REMARK 465 HIS A 299
REMARK 465 HIS A 300
REMARK 465 HIS A 301
REMARK 465 HIS A 302
REMARK 465 ALA B 283
REMARK 465 THR B 284
REMARK 465 PRO B 285
REMARK 465 PRO B 286
REMARK 465 ALA B 287
REMARK 465 ALA B 288
REMARK 465 PRO B 289
REMARK 465 ALA B 290
REMARK 465 ALA B 291
REMARK 465 PRO B 292
REMARK 465 ALA B 293
REMARK 465 ALA B 294
REMARK 465 LEU B 295
REMARK 465 GLU B 296
REMARK 465 HIS B 297
REMARK 465 HIS B 298
REMARK 465 HIS B 299
REMARK 465 HIS B 300
REMARK 465 HIS B 301
REMARK 465 HIS B 302
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 OG SER A 124 OD2 ASP A 216 2.11
REMARK 500 O HOH A 646 O HOH A 655 2.16
REMARK 500 NE ARG A 3 O HOH A 501 2.16
REMARK 500 O HOH B 650 O HOH B 653 2.18
REMARK 500 O HOH A 626 O HOH A 652 2.19
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 PHE A 1 -169.62 57.57
REMARK 500 PRO A 54 44.95 -92.94
REMARK 500 SER A 74 18.29 57.20
REMARK 500 ASN A 87 18.39 -140.80
REMARK 500 ARG A 101 -66.89 -127.63
REMARK 500 SER A 124 -125.43 51.70
REMARK 500 ASN A 152 55.49 -147.19
REMARK 500 PRO A 214 98.05 -69.44
REMARK 500 LEU A 217 144.70 179.65
REMARK 500 PHE B 1 -170.12 58.94
REMARK 500 PRO B 54 43.98 -91.08
REMARK 500 ARG B 101 -65.80 -128.18
REMARK 500 SER B 124 -123.53 49.17
REMARK 500 ASN B 152 56.83 -144.57
REMARK 500 ASP B 216 72.05 46.25
REMARK 500 LEU B 217 -168.94 -121.92
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 ASP B 216 LEU B 217 -138.54
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 6Y3 A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide 6Y3 B 401 and CYS B
REMARK 800 209
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5KWI RELATED DB: PDB
DBREF 5KWJ A 1 294 UNP P9WQN8 A85C_MYCTO 47 340
DBREF 5KWJ B 1 294 UNP P9WQN8 A85C_MYCTO 47 340
SEQADV 5KWJ MET A 0 UNP P9WQN8 INITIATING METHIONINE
SEQADV 5KWJ LEU A 295 UNP P9WQN8 EXPRESSION TAG
SEQADV 5KWJ GLU A 296 UNP P9WQN8 EXPRESSION TAG
SEQADV 5KWJ HIS A 297 UNP P9WQN8 EXPRESSION TAG
SEQADV 5KWJ HIS A 298 UNP P9WQN8 EXPRESSION TAG
SEQADV 5KWJ HIS A 299 UNP P9WQN8 EXPRESSION TAG
SEQADV 5KWJ HIS A 300 UNP P9WQN8 EXPRESSION TAG
SEQADV 5KWJ HIS A 301 UNP P9WQN8 EXPRESSION TAG
SEQADV 5KWJ HIS A 302 UNP P9WQN8 EXPRESSION TAG
SEQADV 5KWJ MET B 0 UNP P9WQN8 INITIATING METHIONINE
SEQADV 5KWJ LEU B 295 UNP P9WQN8 EXPRESSION TAG
SEQADV 5KWJ GLU B 296 UNP P9WQN8 EXPRESSION TAG
SEQADV 5KWJ HIS B 297 UNP P9WQN8 EXPRESSION TAG
SEQADV 5KWJ HIS B 298 UNP P9WQN8 EXPRESSION TAG
SEQADV 5KWJ HIS B 299 UNP P9WQN8 EXPRESSION TAG
SEQADV 5KWJ HIS B 300 UNP P9WQN8 EXPRESSION TAG
SEQADV 5KWJ HIS B 301 UNP P9WQN8 EXPRESSION TAG
SEQADV 5KWJ HIS B 302 UNP P9WQN8 EXPRESSION TAG
SEQRES 1 A 303 MET PHE SER ARG PRO GLY LEU PRO VAL GLU TYR LEU GLN
SEQRES 2 A 303 VAL PRO SER ALA SER MET GLY ARG ASP ILE LYS VAL GLN
SEQRES 3 A 303 PHE GLN GLY GLY GLY PRO HIS ALA VAL TYR LEU LEU ASP
SEQRES 4 A 303 GLY LEU ARG ALA GLN ASP ASP TYR ASN GLY TRP ASP ILE
SEQRES 5 A 303 ASN THR PRO ALA PHE GLU GLU TYR TYR GLN SER GLY LEU
SEQRES 6 A 303 SER VAL ILE MET PRO VAL GLY GLY GLN SER SER PHE TYR
SEQRES 7 A 303 THR ASP TRP TYR GLN PRO SER GLN SER ASN GLY GLN ASN
SEQRES 8 A 303 TYR THR TYR LYS TRP GLU THR PHE LEU THR ARG GLU MET
SEQRES 9 A 303 PRO ALA TRP LEU GLN ALA ASN LYS GLY VAL SER PRO THR
SEQRES 10 A 303 GLY ASN ALA ALA VAL GLY LEU SER MET SER GLY GLY SER
SEQRES 11 A 303 ALA LEU ILE LEU ALA ALA TYR TYR PRO GLN GLN PHE PRO
SEQRES 12 A 303 TYR ALA ALA SER LEU SER GLY PHE LEU ASN PRO SER GLU
SEQRES 13 A 303 GLY TRP TRP PRO THR LEU ILE GLY LEU ALA MET ASN ASP
SEQRES 14 A 303 SER GLY GLY TYR ASN ALA ASN SER MET TRP GLY PRO SER
SEQRES 15 A 303 SER ASP PRO ALA TRP LYS ARG ASN ASP PRO MET VAL GLN
SEQRES 16 A 303 ILE PRO ARG LEU VAL ALA ASN ASN THR ARG ILE TRP VAL
SEQRES 17 A 303 TYR CYS GLY ASN GLY THR PRO SER ASP LEU GLY GLY ASP
SEQRES 18 A 303 ASN ILE PRO ALA LYS PHE LEU GLU GLY LEU THR LEU ARG
SEQRES 19 A 303 THR ASN GLN THR PHE ARG ASP THR TYR ALA ALA ASP GLY
SEQRES 20 A 303 GLY ARG ASN GLY VAL PHE ASN PHE PRO PRO ASN GLY THR
SEQRES 21 A 303 HIS SER TRP PRO TYR TRP ASN GLU GLN LEU VAL ALA MET
SEQRES 22 A 303 LYS ALA ASP ILE GLN HIS VAL LEU ASN GLY ALA THR PRO
SEQRES 23 A 303 PRO ALA ALA PRO ALA ALA PRO ALA ALA LEU GLU HIS HIS
SEQRES 24 A 303 HIS HIS HIS HIS
SEQRES 1 B 303 MET PHE SER ARG PRO GLY LEU PRO VAL GLU TYR LEU GLN
SEQRES 2 B 303 VAL PRO SER ALA SER MET GLY ARG ASP ILE LYS VAL GLN
SEQRES 3 B 303 PHE GLN GLY GLY GLY PRO HIS ALA VAL TYR LEU LEU ASP
SEQRES 4 B 303 GLY LEU ARG ALA GLN ASP ASP TYR ASN GLY TRP ASP ILE
SEQRES 5 B 303 ASN THR PRO ALA PHE GLU GLU TYR TYR GLN SER GLY LEU
SEQRES 6 B 303 SER VAL ILE MET PRO VAL GLY GLY GLN SER SER PHE TYR
SEQRES 7 B 303 THR ASP TRP TYR GLN PRO SER GLN SER ASN GLY GLN ASN
SEQRES 8 B 303 TYR THR TYR LYS TRP GLU THR PHE LEU THR ARG GLU MET
SEQRES 9 B 303 PRO ALA TRP LEU GLN ALA ASN LYS GLY VAL SER PRO THR
SEQRES 10 B 303 GLY ASN ALA ALA VAL GLY LEU SER MET SER GLY GLY SER
SEQRES 11 B 303 ALA LEU ILE LEU ALA ALA TYR TYR PRO GLN GLN PHE PRO
SEQRES 12 B 303 TYR ALA ALA SER LEU SER GLY PHE LEU ASN PRO SER GLU
SEQRES 13 B 303 GLY TRP TRP PRO THR LEU ILE GLY LEU ALA MET ASN ASP
SEQRES 14 B 303 SER GLY GLY TYR ASN ALA ASN SER MET TRP GLY PRO SER
SEQRES 15 B 303 SER ASP PRO ALA TRP LYS ARG ASN ASP PRO MET VAL GLN
SEQRES 16 B 303 ILE PRO ARG LEU VAL ALA ASN ASN THR ARG ILE TRP VAL
SEQRES 17 B 303 TYR CYS GLY ASN GLY THR PRO SER ASP LEU GLY GLY ASP
SEQRES 18 B 303 ASN ILE PRO ALA LYS PHE LEU GLU GLY LEU THR LEU ARG
SEQRES 19 B 303 THR ASN GLN THR PHE ARG ASP THR TYR ALA ALA ASP GLY
SEQRES 20 B 303 GLY ARG ASN GLY VAL PHE ASN PHE PRO PRO ASN GLY THR
SEQRES 21 B 303 HIS SER TRP PRO TYR TRP ASN GLU GLN LEU VAL ALA MET
SEQRES 22 B 303 LYS ALA ASP ILE GLN HIS VAL LEU ASN GLY ALA THR PRO
SEQRES 23 B 303 PRO ALA ALA PRO ALA ALA PRO ALA ALA LEU GLU HIS HIS
SEQRES 24 B 303 HIS HIS HIS HIS
HET 6Y3 A 401 17
HET 6Y3 B 401 17
HETNAM 6Y3 ~{N}-(4-AMINOPHENYL)-2-SELANYL-BENZAMIDE
HETSYN 6Y3 AMINO-EBSELEN (OPEN FORM)
FORMUL 3 6Y3 2(C13 H12 N2 O SE)
FORMUL 5 HOH *328(H2 O)
HELIX 1 AA1 ASN A 47 THR A 53 1 7
HELIX 2 AA2 PRO A 54 TYR A 60 1 7
HELIX 3 AA3 LYS A 94 ARG A 101 1 8
HELIX 4 AA4 ARG A 101 GLY A 112 1 12
HELIX 5 AA5 SER A 124 TYR A 137 1 14
HELIX 6 AA6 TRP A 157 SER A 169 1 13
HELIX 7 AA7 ASN A 173 GLY A 179 1 7
HELIX 8 AA8 ASP A 183 ASN A 189 1 7
HELIX 9 AA9 GLN A 194 ASN A 201 1 8
HELIX 10 AB1 PRO A 223 ASP A 245 1 23
HELIX 11 AB2 SER A 261 MET A 272 1 12
HELIX 12 AB3 MET A 272 GLY A 282 1 11
HELIX 13 AB4 ASN B 47 THR B 53 1 7
HELIX 14 AB5 PRO B 54 TYR B 60 1 7
HELIX 15 AB6 LYS B 94 ARG B 101 1 8
HELIX 16 AB7 ARG B 101 GLY B 112 1 12
HELIX 17 AB8 SER B 124 TYR B 137 1 14
HELIX 18 AB9 TRP B 157 SER B 169 1 13
HELIX 19 AC1 ASN B 173 GLY B 179 1 7
HELIX 20 AC2 ASP B 183 ASN B 189 1 7
HELIX 21 AC3 GLN B 194 ASN B 201 1 8
HELIX 22 AC4 PRO B 223 ASP B 245 1 23
HELIX 23 AC5 SER B 261 MET B 272 1 12
HELIX 24 AC6 MET B 272 GLY B 282 1 11
SHEET 1 AA1 8 VAL A 8 SER A 15 0
SHEET 2 AA1 8 ARG A 20 GLN A 27 -1 O ILE A 22 N VAL A 13
SHEET 3 AA1 8 SER A 65 PRO A 69 -1 O MET A 68 N GLN A 25
SHEET 4 AA1 8 ALA A 33 LEU A 36 1 N LEU A 36 O ILE A 67
SHEET 5 AA1 8 ALA A 119 LEU A 123 1 O ALA A 119 N TYR A 35
SHEET 6 AA1 8 TYR A 143 LEU A 147 1 O ALA A 145 N ALA A 120
SHEET 7 AA1 8 ARG A 204 TYR A 208 1 O ARG A 204 N ALA A 144
SHEET 8 AA1 8 GLY A 250 ASN A 253 1 O VAL A 251 N VAL A 207
SHEET 1 AA2 8 VAL B 8 SER B 15 0
SHEET 2 AA2 8 ARG B 20 GLN B 27 -1 O ILE B 22 N VAL B 13
SHEET 3 AA2 8 SER B 65 PRO B 69 -1 O MET B 68 N GLN B 25
SHEET 4 AA2 8 ALA B 33 LEU B 36 1 N LEU B 36 O ILE B 67
SHEET 5 AA2 8 ALA B 119 LEU B 123 1 O ALA B 119 N TYR B 35
SHEET 6 AA2 8 TYR B 143 LEU B 147 1 O ALA B 145 N ALA B 120
SHEET 7 AA2 8 ARG B 204 TYR B 208 1 O TYR B 208 N SER B 146
SHEET 8 AA2 8 GLY B 250 ASN B 253 1 O VAL B 251 N VAL B 207
LINK SG CYS A 209 SE07 6Y3 A 401 1555 1555 2.30
LINK SG CYS B 209 SE07 6Y3 B 401 1555 1555 2.30
SITE 1 AC1 5 CYS A 209 ARG A 239 PHE A 252 PHE A 254
SITE 2 AC1 5 TYR B 81
SITE 1 AC2 10 TYR A 81 TYR B 208 GLY B 210 ASN B 235
SITE 2 AC2 10 GLN B 236 ARG B 239 PHE B 252 ASN B 253
SITE 3 AC2 10 PHE B 254 HOH B 556
CRYST1 88.474 88.479 161.950 90.00 90.00 90.00 C 2 2 21 16
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 0.011303 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011302 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006175 0.00000
TER 2213 GLY A 282
TER 4426 GLY B 282
MASTER 348 0 2 24 16 0 5 6 4768 2 36 48
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