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HEADER TRANSFERASE 15-MAY-14 4QE3
TITLE CRYSTAL STRUCTURE OF ANTIGEN 85C-H260Q 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: 83332;
SOURCE 4 STRAIN: H37RV;
SOURCE 5 GENE: FBPC, MPT45, MTCI5.03C, RV0129C;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS MYCOLYLTRANSFERASE/DIACYLGLYCEROL ACYLTRANSFERASE, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR L.FAVROT,D.H.LAJINESS,D.R.RONNING
REVDAT 1 09-JUL-14 4QE3 0
JRNL AUTH L.FAVROT,D.H.LAJINESS,D.R.RONNING
JRNL TITL INACTIVATION OF THE MYCOBACTERIUM TUBERCULOSIS ANTIGEN 85
JRNL TITL 2 COMPLEX BY COVALENT, ALLOSTERIC INHIBITORS.
JRNL REF J.BIOL.CHEM. 2014
JRNL REFN ESSN 1083-351X
REMARK 2
REMARK 2 RESOLUTION. 1.35 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.9_1692)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT 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) : 1.35
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 38.15
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.330
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.7
REMARK 3 NUMBER OF REFLECTIONS : 68398
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.173
REMARK 3 R VALUE (WORKING SET) : 0.171
REMARK 3 FREE R VALUE : 0.198
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.990
REMARK 3 FREE R VALUE TEST SET COUNT : 3413
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 38.1687 - 3.8951 0.98 2920 156 0.1580 0.1894
REMARK 3 2 3.8951 - 3.0921 0.97 2757 147 0.1679 0.2059
REMARK 3 3 3.0921 - 2.7013 1.00 2807 147 0.1763 0.1943
REMARK 3 4 2.7013 - 2.4544 1.00 2819 149 0.1794 0.2213
REMARK 3 5 2.4544 - 2.2785 1.00 2779 146 0.1695 0.2058
REMARK 3 6 2.2785 - 2.1442 0.96 2687 140 0.1679 0.2009
REMARK 3 7 2.1442 - 2.0368 1.00 2781 146 0.1656 0.1726
REMARK 3 8 2.0368 - 1.9481 1.00 2759 145 0.1686 0.1884
REMARK 3 9 1.9481 - 1.8731 0.99 2762 145 0.1689 0.1791
REMARK 3 10 1.8731 - 1.8085 1.00 2755 146 0.1669 0.1866
REMARK 3 11 1.8085 - 1.7520 1.00 2749 144 0.1684 0.2195
REMARK 3 12 1.7520 - 1.7019 1.00 2753 145 0.1720 0.1949
REMARK 3 13 1.7019 - 1.6571 1.00 2752 145 0.1596 0.1769
REMARK 3 14 1.6571 - 1.6167 1.00 2762 145 0.1606 0.1849
REMARK 3 15 1.6167 - 1.5799 1.00 2728 144 0.1612 0.1722
REMARK 3 16 1.5799 - 1.5463 1.00 2715 143 0.1622 0.2013
REMARK 3 17 1.5463 - 1.5153 1.00 2784 145 0.1703 0.2244
REMARK 3 18 1.5153 - 1.4867 1.00 2726 144 0.1790 0.1818
REMARK 3 19 1.4867 - 1.4602 1.00 2737 145 0.1803 0.2020
REMARK 3 20 1.4602 - 1.4354 0.99 2723 143 0.1895 0.1899
REMARK 3 21 1.4354 - 1.4123 0.98 2670 142 0.2087 0.2295
REMARK 3 22 1.4123 - 1.3906 0.93 2546 137 0.2183 0.2435
REMARK 3 23 1.3906 - 1.3701 0.87 2396 116 0.2327 0.2732
REMARK 3 24 1.3701 - 1.3508 0.78 2118 108 0.2512 0.2228
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) : 18.040
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 2199
REMARK 3 ANGLE : 1.115 3014
REMARK 3 CHIRALITY : 0.048 308
REMARK 3 PLANARITY : 0.007 394
REMARK 3 DIHEDRAL : 13.466 767
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 4QE3 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-MAY-14.
REMARK 100 THE RCSB ID CODE IS RCSB085938.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 30-JUL-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 4.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 23-ID-D
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97936
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL MONOCHROMATOR
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
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 : NULL
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.350
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 (%) : 97.9
REMARK 200 DATA REDUNDANCY : 5.500
REMARK 200 R MERGE (I) : 0.07800
REMARK 200 R SYM (I) : 0.07800
REMARK 200 FOR THE DATA SET : 16.0370
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.35
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.40
REMARK 200 COMPLETENESS FOR SHELL (%) : 85.5
REMARK 200 DATA REDUNDANCY IN SHELL : 3.90
REMARK 200 R MERGE FOR SHELL (I) : 0.51300
REMARK 200 R SYM FOR SHELL (I) : 0.51300
REMARK 200 FOR SHELL : 2.814
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: EPMR
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 48.47
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.39
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG 3350, 0.1M SODIUM ACETATE
REMARK 280 TRIHYDRATE, 6MM CHAPSO, PH 4.5, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
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 30.36250
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 38.15350
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 34.06400
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 38.15350
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 30.36250
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 34.06400
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 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 PHE A 1
REMARK 465 SER A 2
REMARK 465 ARG A 3
REMARK 465 PRO A 4
REMARK 465 GLY A 5
REMARK 465 GLY A 212
REMARK 465 THR A 213
REMARK 465 PRO A 214
REMARK 465 SER A 215
REMARK 465 ASP A 216
REMARK 465 LEU A 217
REMARK 465 GLY A 218
REMARK 465 GLY A 219
REMARK 465 ASP A 220
REMARK 465 ASN A 221
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 HIS A 295
REMARK 465 HIS A 296
REMARK 465 HIS A 297
REMARK 465 HIS A 298
REMARK 465 HIS A 299
REMARK 465 HIS A 300
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 PRO A 7 40.26 -76.34
REMARK 500 PRO A 54 35.15 -91.91
REMARK 500 PHE A 76 18.57 54.50
REMARK 500 GLN A 85 66.61 -58.66
REMARK 500 SER A 86 -75.30 175.33
REMARK 500 ARG A 101 -63.94 -129.19
REMARK 500 SER A 124 -123.85 48.48
REMARK 500 ASN A 152 58.66 -142.10
REMARK 500 SER A 169 75.21 -100.44
REMARK 500 ARG A 248 16.51 -141.54
REMARK 500
REMARK 500 REMARK: NULL
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 1N7 A 401
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1N7 A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACY A 402
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4QDO RELATED DB: PDB
REMARK 900 RELATED ID: 4QDT RELATED DB: PDB
REMARK 900 RELATED ID: 4QDU RELATED DB: PDB
REMARK 900 RELATED ID: 4QDX RELATED DB: PDB
REMARK 900 RELATED ID: 4QDZ RELATED DB: PDB
REMARK 900 RELATED ID: 4QEK RELATED DB: PDB
DBREF 4QE3 A 0 294 UNP P9WQN9 A85C_MYCTU 46 340
SEQADV 4QE3 MET A -1 UNP P9WQN9 EXPRESSION TAG
SEQADV 4QE3 GLN A 260 UNP P9WQN9 HIS 306 ENGINEERED MUTATION
SEQADV 4QE3 HIS A 295 UNP P9WQN9 EXPRESSION TAG
SEQADV 4QE3 HIS A 296 UNP P9WQN9 EXPRESSION TAG
SEQADV 4QE3 HIS A 297 UNP P9WQN9 EXPRESSION TAG
SEQADV 4QE3 HIS A 298 UNP P9WQN9 EXPRESSION TAG
SEQADV 4QE3 HIS A 299 UNP P9WQN9 EXPRESSION TAG
SEQADV 4QE3 HIS A 300 UNP P9WQN9 EXPRESSION TAG
SEQRES 1 A 302 MET ALA PHE SER ARG PRO GLY LEU PRO VAL GLU TYR LEU
SEQRES 2 A 302 GLN VAL PRO SER ALA SER MET GLY ARG ASP ILE LYS VAL
SEQRES 3 A 302 GLN PHE GLN GLY GLY GLY PRO HIS ALA VAL TYR LEU LEU
SEQRES 4 A 302 ASP GLY LEU ARG ALA GLN ASP ASP TYR ASN GLY TRP ASP
SEQRES 5 A 302 ILE ASN THR PRO ALA PHE GLU GLU TYR TYR GLN SER GLY
SEQRES 6 A 302 LEU SER VAL ILE MET PRO VAL GLY GLY GLN SER SER PHE
SEQRES 7 A 302 TYR THR ASP TRP TYR GLN PRO SER GLN SER ASN GLY GLN
SEQRES 8 A 302 ASN TYR THR TYR LYS TRP GLU THR PHE LEU THR ARG GLU
SEQRES 9 A 302 MET PRO ALA TRP LEU GLN ALA ASN LYS GLY VAL SER PRO
SEQRES 10 A 302 THR GLY ASN ALA ALA VAL GLY LEU SER MET SER GLY GLY
SEQRES 11 A 302 SER ALA LEU ILE LEU ALA ALA TYR TYR PRO GLN GLN PHE
SEQRES 12 A 302 PRO TYR ALA ALA SER LEU SER GLY PHE LEU ASN PRO SER
SEQRES 13 A 302 GLU GLY TRP TRP PRO THR LEU ILE GLY LEU ALA MET ASN
SEQRES 14 A 302 ASP SER GLY GLY TYR ASN ALA ASN SER MET TRP GLY PRO
SEQRES 15 A 302 SER SER ASP PRO ALA TRP LYS ARG ASN ASP PRO MET VAL
SEQRES 16 A 302 GLN ILE PRO ARG LEU VAL ALA ASN ASN THR ARG ILE TRP
SEQRES 17 A 302 VAL TYR CYS GLY ASN GLY THR PRO SER ASP LEU GLY GLY
SEQRES 18 A 302 ASP ASN ILE PRO ALA LYS PHE LEU GLU GLY LEU THR LEU
SEQRES 19 A 302 ARG THR ASN GLN THR PHE ARG ASP THR TYR ALA ALA ASP
SEQRES 20 A 302 GLY GLY ARG ASN GLY VAL PHE ASN PHE PRO PRO ASN GLY
SEQRES 21 A 302 THR GLN SER TRP PRO TYR TRP ASN GLU GLN LEU VAL ALA
SEQRES 22 A 302 MET LYS ALA ASP ILE GLN HIS VAL LEU ASN GLY ALA THR
SEQRES 23 A 302 PRO PRO ALA ALA PRO ALA ALA PRO ALA ALA HIS HIS HIS
SEQRES 24 A 302 HIS HIS HIS
HET 1N7 A 401 26
HET ACY A 402 4
HETNAM 1N7 CHAPSO
HETNAM ACY ACETIC ACID
HETSYN 1N7 2-HYDROXY-N,N-DIMETHYL-3-SULFO-N-(3-{[(3BETA,5BETA,
HETSYN 2 1N7 7BETA,12BETA)-3,7,12-TRIHYDROXY-24-OXOCHOLAN-24-
HETSYN 3 1N7 YL]AMINO}PROPYL)PROPAN-1-AMINIUM
FORMUL 2 1N7 C32 H59 N2 O8 S 1+
FORMUL 3 ACY C2 H4 O2
FORMUL 4 HOH *234(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 PRO A 223 ASP A 245 1 23
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
SITE 1 AC1 10 THR A 100 ARG A 101 GLN A 108 GLN A 140
SITE 2 AC1 10 ASN A 167 GLY A 170 GLY A 171 HOH A 555
SITE 3 AC1 10 HOH A 581 HOH A 613
SITE 1 AC2 2 ASP A 50 HOH A 708
CRYST1 60.725 68.128 76.307 90.00 90.00 90.00 P 21 21 21 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 0.016468 0.000000 0.000000 0.00000
SCALE2 0.000000 0.014678 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013105 0.00000
TER 2098 GLY A 282
MASTER 307 0 2 12 8 0 4 6 2355 1 30 24
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