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HEADER TRANSFERASE 16-SEP-13 4MQL
TITLE CRYSTAL STRUCTURE OF ANTIGEN 85C-C209S MUTANT
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DIACYLGLYCEROL ACYLTRANSFERASE/MYCOLYLTRANSFERASE AG85C;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: DGAT, ACYL-COA:DIACYLGLYCEROL ACYLTRANSFERASE, ANTIGEN 85
COMPND 5 COMPLEX C, 85C, AG85C, FIBRONECTIN-BINDING PROTEIN C, FBPS C;
COMPND 6 EC: 2.3.1.122, 2.3.1.20;
COMPND 7 ENGINEERED: YES;
COMPND 8 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM TUBERCULOSIS;
SOURCE 3 ORGANISM_TAXID: 1773;
SOURCE 4 GENE: FBPC, MPT45, RV0129C, MT0137, MTCI5.03C;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS ACYLTRANSFERASE, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR L.FAVROT,A.E.GRZEGORZEWICZ,D.H.LAJINESS,R.K.MARVIN,J.BOUCAU,
AUTHOR 2 D.ISAILOVIC,M.JACKSON,D.R.RONNING
REVDAT 2 25-DEC-13 4MQL 1 JRNL
REVDAT 1 13-NOV-13 4MQL 0
JRNL AUTH L.FAVROT,A.E.GRZEGORZEWICZ,D.H.LAJINESS,R.K.MARVIN,J.BOUCAU,
JRNL AUTH 2 D.ISAILOVIC,M.JACKSON,D.R.RONNING
JRNL TITL MECHANISM OF INHIBITION OF MYCOBACTERIUM TUBERCULOSIS
JRNL TITL 2 ANTIGEN 85 BY EBSELEN.
JRNL REF NAT COMMUN V. 4 2748 2013
JRNL REFN ESSN 2041-1723
JRNL PMID 24193546
JRNL DOI 10.1038/NCOMMS3748
REMARK 2
REMARK 2 RESOLUTION. 1.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.8_1069)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-
REMARK 3 : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,
REMARK 3 : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL
REMARK 3 : MORIARTY,REETAL PAI,RANDY READ,JANE
REMARK 3 : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM
REMARK 3 : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,
REMARK 3 : LAURENT STORONI,TOM TERWILLIGER,PETER
REMARK 3 : 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) : 34.09
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.370
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 3 NUMBER OF REFLECTIONS : 79862
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.154
REMARK 3 R VALUE (WORKING SET) : 0.153
REMARK 3 FREE R VALUE : 0.165
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.980
REMARK 3 FREE R VALUE TEST SET COUNT : 3979
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 34.0972 - 3.9456 0.97 2734 140 0.1393 0.1475
REMARK 3 2 3.9456 - 3.1324 0.97 2690 139 0.1448 0.1651
REMARK 3 3 3.1324 - 2.7367 1.00 2712 147 0.1607 0.1688
REMARK 3 4 2.7367 - 2.4865 1.00 2740 148 0.1653 0.1625
REMARK 3 5 2.4865 - 2.3083 1.00 2744 137 0.1588 0.1575
REMARK 3 6 2.3083 - 2.1723 1.00 2729 140 0.1547 0.1881
REMARK 3 7 2.1723 - 2.0635 1.00 2693 155 0.1539 0.1592
REMARK 3 8 2.0635 - 1.9737 1.00 2738 141 0.1494 0.1445
REMARK 3 9 1.9737 - 1.8977 1.00 2688 146 0.1552 0.1612
REMARK 3 10 1.8977 - 1.8322 1.00 2731 139 0.1582 0.1663
REMARK 3 11 1.8322 - 1.7749 1.00 2734 141 0.1544 0.1613
REMARK 3 12 1.7749 - 1.7242 1.00 2691 148 0.1535 0.1669
REMARK 3 13 1.7242 - 1.6788 1.00 2713 147 0.1537 0.1747
REMARK 3 14 1.6788 - 1.6379 1.00 2723 131 0.1468 0.1556
REMARK 3 15 1.6379 - 1.6006 1.00 2723 152 0.1462 0.1607
REMARK 3 16 1.6006 - 1.5666 1.00 2707 142 0.1430 0.1567
REMARK 3 17 1.5666 - 1.5352 1.00 2726 135 0.1460 0.1550
REMARK 3 18 1.5352 - 1.5063 1.00 2693 146 0.1446 0.1872
REMARK 3 19 1.5063 - 1.4794 1.00 2720 141 0.1485 0.1837
REMARK 3 20 1.4794 - 1.4543 1.00 2688 142 0.1566 0.1659
REMARK 3 21 1.4543 - 1.4308 1.00 2730 137 0.1601 0.1742
REMARK 3 22 1.4308 - 1.4088 1.00 2724 147 0.1599 0.1592
REMARK 3 23 1.4088 - 1.3881 1.00 2659 151 0.1676 0.2044
REMARK 3 24 1.3881 - 1.3685 1.00 2730 136 0.1709 0.1824
REMARK 3 25 1.3685 - 1.3500 1.00 2726 138 0.1677 0.1696
REMARK 3 26 1.3500 - 1.3325 1.00 2661 143 0.1657 0.1870
REMARK 3 27 1.3325 - 1.3158 0.99 2691 143 0.1702 0.1673
REMARK 3 28 1.3158 - 1.3000 0.96 2645 127 0.1794 0.1864
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) : 0.080
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 14.700
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 2311
REMARK 3 ANGLE : 1.140 3160
REMARK 3 CHIRALITY : 0.048 311
REMARK 3 PLANARITY : 0.007 419
REMARK 3 DIHEDRAL : 19.019 850
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 4MQL COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-OCT-13.
REMARK 100 THE RCSB ID CODE IS RCSB082242.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 29-OCT-11
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 : 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) : 0.97856
REMARK 200 MONOCHROMATOR : C(111)
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 : 79869
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.300
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 200 DATA REDUNDANCY : 7.400
REMARK 200 R MERGE (I) : 0.05100
REMARK 200 R SYM (I) : 0.05100
REMARK 200 FOR THE DATA SET : 51.4080
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 (PHENIX.REFINE: 1.8_1069)
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.57
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.49
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M BIS-TRIS 6.5, 25% PEG 3350,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
REMARK 290 4555 -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 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 67.88200
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 34.08550
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 67.88200
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 34.08550
REMARK 290 SMTRY3 4 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: 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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A 704 LIES ON A SPECIAL POSITION.
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 MET A -1
REMARK 465 ALA A 0
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 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 86 O HOH A 772 2.12
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 SER A 2 -157.67 -144.69
REMARK 500 ARG A 41 31.22 -96.72
REMARK 500 PRO A 54 37.69 -91.64
REMARK 500 PHE A 76 19.92 54.32
REMARK 500 SER A 86 -53.33 167.27
REMARK 500 ARG A 101 -62.96 -129.81
REMARK 500 SER A 124 -126.94 49.23
REMARK 500 ASN A 152 56.95 -141.04
REMARK 500 SER A 169 78.01 -109.43
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 BTB A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BTB A 402
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4MQM RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF ANTIGEN 85C IN PRESENCE OF EBSELEN
DBREF 4MQL A 0 294 UNP P0A4V4 A85C_MYCTU 46 340
SEQADV 4MQL MET A -1 UNP P0A4V4 EXPRESSION TAG
SEQADV 4MQL SER A 209 UNP P0A4V4 CYS 255 ENGINEERED MUTATION
SEQADV 4MQL LEU A 295 UNP P0A4V4 EXPRESSION TAG
SEQADV 4MQL GLU A 296 UNP P0A4V4 EXPRESSION TAG
SEQADV 4MQL HIS A 297 UNP P0A4V4 EXPRESSION TAG
SEQADV 4MQL HIS A 298 UNP P0A4V4 EXPRESSION TAG
SEQADV 4MQL HIS A 299 UNP P0A4V4 EXPRESSION TAG
SEQADV 4MQL HIS A 300 UNP P0A4V4 EXPRESSION TAG
SEQADV 4MQL HIS A 301 UNP P0A4V4 EXPRESSION TAG
SEQADV 4MQL HIS A 302 UNP P0A4V4 EXPRESSION TAG
SEQRES 1 A 304 MET ALA PHE SER ARG PRO GLY LEU PRO VAL GLU TYR LEU
SEQRES 2 A 304 GLN VAL PRO SER ALA SER MET GLY ARG ASP ILE LYS VAL
SEQRES 3 A 304 GLN PHE GLN GLY GLY GLY PRO HIS ALA VAL TYR LEU LEU
SEQRES 4 A 304 ASP GLY LEU ARG ALA GLN ASP ASP TYR ASN GLY TRP ASP
SEQRES 5 A 304 ILE ASN THR PRO ALA PHE GLU GLU TYR TYR GLN SER GLY
SEQRES 6 A 304 LEU SER VAL ILE MET PRO VAL GLY GLY GLN SER SER PHE
SEQRES 7 A 304 TYR THR ASP TRP TYR GLN PRO SER GLN SER ASN GLY GLN
SEQRES 8 A 304 ASN TYR THR TYR LYS TRP GLU THR PHE LEU THR ARG GLU
SEQRES 9 A 304 MET PRO ALA TRP LEU GLN ALA ASN LYS GLY VAL SER PRO
SEQRES 10 A 304 THR GLY ASN ALA ALA VAL GLY LEU SER MET SER GLY GLY
SEQRES 11 A 304 SER ALA LEU ILE LEU ALA ALA TYR TYR PRO GLN GLN PHE
SEQRES 12 A 304 PRO TYR ALA ALA SER LEU SER GLY PHE LEU ASN PRO SER
SEQRES 13 A 304 GLU GLY TRP TRP PRO THR LEU ILE GLY LEU ALA MET ASN
SEQRES 14 A 304 ASP SER GLY GLY TYR ASN ALA ASN SER MET TRP GLY PRO
SEQRES 15 A 304 SER SER ASP PRO ALA TRP LYS ARG ASN ASP PRO MET VAL
SEQRES 16 A 304 GLN ILE PRO ARG LEU VAL ALA ASN ASN THR ARG ILE TRP
SEQRES 17 A 304 VAL TYR SER GLY ASN GLY THR PRO SER ASP LEU GLY GLY
SEQRES 18 A 304 ASP ASN ILE PRO ALA LYS PHE LEU GLU GLY LEU THR LEU
SEQRES 19 A 304 ARG THR ASN GLN THR PHE ARG ASP THR TYR ALA ALA ASP
SEQRES 20 A 304 GLY GLY ARG ASN GLY VAL PHE ASN PHE PRO PRO ASN GLY
SEQRES 21 A 304 THR HIS SER TRP PRO TYR TRP ASN GLU GLN LEU VAL ALA
SEQRES 22 A 304 MET LYS ALA ASP ILE GLN HIS VAL LEU ASN GLY ALA THR
SEQRES 23 A 304 PRO PRO ALA ALA PRO ALA ALA PRO ALA ALA LEU GLU HIS
SEQRES 24 A 304 HIS HIS HIS HIS HIS
HET BTB A 401 14
HET BTB A 402 14
HETNAM BTB 2-[BIS-(2-HYDROXY-ETHYL)-AMINO]-2-HYDROXYMETHYL-
HETNAM 2 BTB PROPANE-1,3-DIOL
HETSYN BTB BIS-TRIS BUFFER
FORMUL 2 BTB 2(C8 H19 N O5)
FORMUL 4 HOH *278(H2 O)
HELIX 1 1 ASN A 47 THR A 53 1 7
HELIX 2 2 PRO A 54 TYR A 60 1 7
HELIX 3 3 LYS A 94 ARG A 101 1 8
HELIX 4 4 ARG A 101 GLY A 112 1 12
HELIX 5 5 SER A 124 TYR A 137 1 14
HELIX 6 6 TRP A 157 SER A 169 1 13
HELIX 7 7 ASN A 173 GLY A 179 1 7
HELIX 8 8 ASP A 183 ASN A 189 1 7
HELIX 9 9 GLN A 194 ASN A 201 1 8
HELIX 10 10 LYS A 225 ASP A 245 1 21
HELIX 11 11 SER A 261 MET A 272 1 12
HELIX 12 12 MET A 272 GLY A 282 1 11
SHEET 1 A 8 GLU A 9 SER A 15 0
SHEET 2 A 8 ARG A 20 GLN A 27 -1 O PHE A 26 N GLU A 9
SHEET 3 A 8 SER A 65 PRO A 69 -1 O MET A 68 N GLN A 25
SHEET 4 A 8 ALA A 33 LEU A 36 1 N LEU A 36 O ILE A 67
SHEET 5 A 8 ALA A 119 LEU A 123 1 O ALA A 119 N TYR A 35
SHEET 6 A 8 TYR A 143 LEU A 147 1 O ALA A 145 N ALA A 120
SHEET 7 A 8 ARG A 204 TYR A 208 1 O TYR A 208 N SER A 146
SHEET 8 A 8 GLY A 250 ASN A 253 1 O VAL A 251 N VAL A 207
CISPEP 1 THR A 213 PRO A 214 0 -2.57
SITE 1 AC1 11 ASP A 79 TRP A 80 TYR A 81 LYS A 94
SITE 2 AC1 11 MET A 177 TRP A 178 BTB A 402 HOH A 595
SITE 3 AC1 11 HOH A 652 HOH A 740 HOH A 769
SITE 1 AC2 11 ASP A 79 GLU A 96 THR A 97 TYR A 137
SITE 2 AC2 11 ARG A 188 BTB A 401 HOH A 605 HOH A 697
SITE 3 AC2 11 HOH A 733 HOH A 769 HOH A 770
CRYST1 135.764 68.171 35.908 90.00 94.03 90.00 C 1 2 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 0.007366 0.000000 0.000519 0.00000
SCALE2 0.000000 0.014669 0.000000 0.00000
SCALE3 0.000000 0.000000 0.027918 0.00000
TER 2210 GLY A 282
MASTER 303 0 2 12 8 0 6 6 2501 1 28 24
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