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HEADER TRANSFERASE 18-JUL-16 5KWI
TITLE M.TB AG85C MODIFIED AT C209 BY ADAMANTYL-EBSELEN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DIACYLGLYCEROL ACYLTRANSFERASE/MYCOLYLTRANSFERASE AG85C;
COMPND 3 CHAIN: A;
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: ADAMANTYL 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 5KWI 1 REMARK
REVDAT 2 24-MAY-17 5KWI 1 JRNL
REVDAT 1 29-MAR-17 5KWI 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. 1.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX DEV_1839
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) : 1.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 40.85
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 81192
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.166
REMARK 3 R VALUE (WORKING SET) : 0.166
REMARK 3 FREE R VALUE : 0.176
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 2.460
REMARK 3 FREE R VALUE TEST SET COUNT : 1998
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 40.8659 - 3.1321 1.00 6064 153 0.1583 0.1496
REMARK 3 2 3.1321 - 2.4861 1.00 5786 146 0.1794 0.1868
REMARK 3 3 2.4861 - 2.1719 1.00 5741 145 0.1668 0.1693
REMARK 3 4 2.1719 - 1.9733 1.00 5664 144 0.1686 0.1807
REMARK 3 5 1.9733 - 1.8319 1.00 5657 142 0.1653 0.2102
REMARK 3 6 1.8319 - 1.7239 1.00 5622 142 0.1602 0.2153
REMARK 3 7 1.7239 - 1.6375 1.00 5629 143 0.1555 0.1672
REMARK 3 8 1.6375 - 1.5662 1.00 5609 141 0.1500 0.1648
REMARK 3 9 1.5662 - 1.5059 1.00 5597 141 0.1537 0.1714
REMARK 3 10 1.5059 - 1.4540 1.00 5581 140 0.1579 0.1857
REMARK 3 11 1.4540 - 1.4085 1.00 5560 141 0.1649 0.1804
REMARK 3 12 1.4085 - 1.3682 1.00 5588 140 0.1783 0.2136
REMARK 3 13 1.3682 - 1.3322 1.00 5592 141 0.1926 0.2252
REMARK 3 14 1.3322 - 1.2997 1.00 5504 139 0.2226 0.2272
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) : 0.120
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 16.100
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 : 0.006 2317
REMARK 3 ANGLE : 1.155 3174
REMARK 3 CHIRALITY : 0.080 316
REMARK 3 PLANARITY : 0.007 420
REMARK 3 DIHEDRAL : 13.479 812
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 5KWI 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_1000219122.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 26-JUN-15
REMARK 200 TEMPERATURE (KELVIN) : 80
REMARK 200 PH : 5.5
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-G
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97857
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 300 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 81206
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.300
REMARK 200 RESOLUTION RANGE LOW (A) : 40.850
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 13.00
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 20.0000
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 (%): 48.99
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.41
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M BIS-TRIS PH 5.5, 25 % W/V
REMARK 280 POLYETHYLENE GLYCOL 3,350, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 289.15K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2
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 -Y+1/2,X+1/2,Z+3/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+1/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+3/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+1/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z+1/2
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 80.10500
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 31.70250
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 31.70250
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 120.15750
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 31.70250
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 31.70250
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 40.05250
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 31.70250
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 31.70250
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 120.15750
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 31.70250
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 31.70250
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 40.05250
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 80.10500
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 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 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 628 O HOH A 777 6467 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 -179.31 63.91
REMARK 500 PRO A 54 40.69 -92.55
REMARK 500 PHE A 76 17.21 55.87
REMARK 500 ARG A 101 -62.84 -130.11
REMARK 500 SER A 124 -127.20 53.07
REMARK 500 ASN A 152 58.62 -144.60
REMARK 500 ARG A 248 13.97 -147.18
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 786 DISTANCE = 5.83 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 6Y1 A 401
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5KWJ RELATED DB: PDB
DBREF 5KWI A 1 294 UNP P9WQN8 A85C_MYCTO 47 340
SEQADV 5KWI MET A 0 UNP P9WQN8 INITIATING METHIONINE
SEQADV 5KWI LEU A 295 UNP P9WQN8 EXPRESSION TAG
SEQADV 5KWI GLU A 296 UNP P9WQN8 EXPRESSION TAG
SEQADV 5KWI HIS A 297 UNP P9WQN8 EXPRESSION TAG
SEQADV 5KWI HIS A 298 UNP P9WQN8 EXPRESSION TAG
SEQADV 5KWI HIS A 299 UNP P9WQN8 EXPRESSION TAG
SEQADV 5KWI HIS A 300 UNP P9WQN8 EXPRESSION TAG
SEQADV 5KWI HIS A 301 UNP P9WQN8 EXPRESSION TAG
SEQADV 5KWI HIS A 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
HET 6Y1 A 401 20
HETNAM 6Y1 ~{N}-(1-ADAMANTYL)-2-SELANYL-BENZAMIDE
HETSYN 6Y1 ADAMANTYL EBSELEN (OPEN FORM)
FORMUL 2 6Y1 C17 H21 N O SE
FORMUL 3 HOH *286(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
SHEET 1 AA1 8 VAL A 8 SER A 15 0
SHEET 2 AA1 8 ARG A 20 GLN A 27 -1 O PHE A 26 N GLU A 9
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 TYR A 208 N SER A 146
SHEET 8 AA1 8 GLY A 250 ASN A 253 1 O VAL A 251 N ILE A 205
LINK SG CYS A 209 SE05 6Y1 A 401 1555 1555 2.27
SITE 1 AC1 8 TYR A 81 GLN A 82 CYS A 209 GLN A 236
SITE 2 AC1 8 ARG A 239 PHE A 252 ASN A 253 PHE A 254
CRYST1 63.405 63.405 160.210 90.00 90.00 90.00 P 43 21 2 8
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 0.015772 0.000000 0.000000 0.00000
SCALE2 0.000000 0.015772 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006242 0.00000
TER 2218 GLY A 282
MASTER 310 0 1 12 8 0 2 6 2509 1 21 24
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