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HEADER TRANSFERASE 21-MAY-21 7MYG
TITLE M. TB AG85C MODIFIED BY THL-10D
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DIACYLGLYCEROL ACYLTRANSFERASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: DIACYLGLYCEROL ACYLTRANSFERASE/MYCOLYLTRANSFERASE AG85A,
COMPND 5 DIACYLGLYCEROL ACYLTRANSFERASE/MYCOLYLTRANSFERASE AG85C,ESTERASE
COMPND 6 FAMILY PROTEIN,SECRETED ANTIGEN 85-C FBPC (85C) (ANTIGEN 85 COMPLEX
COMPND 7 C) (AG58C) (MYCOLYL TRANSFERASE 85C) (FIBRONECTIN-BINDING PROTEIN C);
COMPND 8 EC: 2.3.1.-;
COMPND 9 ENGINEERED: YES;
COMPND 10 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM TUBERCULOSIS;
SOURCE 3 ORGANISM_TAXID: 1773;
SOURCE 4 GENE: FBPC, FBPC_1, DSI38_14625, E5M05_00190, E5M52_01085,
SOURCE 5 E5M78_01085, ERS007657_00618, ERS007663_00913, ERS007665_00182,
SOURCE 6 ERS007703_02124, ERS007722_01715, ERS007741_01210, ERS013471_00870,
SOURCE 7 ERS024276_00850, ERS027659_01767, ERS094182_00158, F6W99_02771,
SOURCE 8 FRD82_05760, GCL30_02455, SAMEA2683035_00278;
SOURCE 9 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 10 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS MYCOLYLTRANSFERASE, ALPHA/BETA-HYDROLASE FOLD, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR T.D.SUDASINGHE,D.R.RONNING
REVDAT 2 20-OCT-21 7MYG 1 JRNL
REVDAT 1 15-SEP-21 7MYG 0
JRNL AUTH S.S.KHAN,T.D.SUDASINGHE,A.D.LANDGRAF,D.R.RONNING,S.J.SUCHECK
JRNL TITL TOTAL SYNTHESIS OF TETRAHYDROLIPSTATIN, ITS DERIVATIVES, AND
JRNL TITL 2 EVALUATION OF THEIR ABILITY TO POTENTIATE MULTIPLE
JRNL TITL 3 ANTIBIOTIC CLASSES AGAINST MYCOBACTERIUM SPECIES.
JRNL REF ACS INFECT DIS. V. 7 2876 2021
JRNL REFN ESSN 2373-8227
JRNL PMID 34478259
JRNL DOI 10.1021/ACSINFECDIS.1C00283
REMARK 2
REMARK 2 RESOLUTION. 2.51 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.19.1_4122
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) : 2.51
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 59.46
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.330
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.9
REMARK 3 NUMBER OF REFLECTIONS : 19226
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) : 0.156
REMARK 3 FREE R VALUE : 0.222
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.130
REMARK 3 FREE R VALUE TEST SET COUNT : 1947
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 59.4600 - 6.0400 0.99 1278 161 0.1737 0.2310
REMARK 3 2 6.0400 - 4.8000 1.00 1283 138 0.1814 0.1964
REMARK 3 3 4.8000 - 4.1900 1.00 1256 146 0.1610 0.2119
REMARK 3 4 4.1900 - 3.8100 1.00 1265 147 0.1579 0.2256
REMARK 3 5 3.8100 - 3.5300 1.00 1266 137 0.1449 0.1918
REMARK 3 6 3.5300 - 3.3300 1.00 1259 141 0.1357 0.2235
REMARK 3 7 3.3300 - 3.1600 0.99 1245 140 0.1416 0.1881
REMARK 3 8 3.1600 - 3.0200 0.98 1236 130 0.1528 0.2300
REMARK 3 9 3.0200 - 2.9100 0.97 1221 139 0.1494 0.2432
REMARK 3 10 2.9100 - 2.8100 0.97 1190 144 0.1545 0.2257
REMARK 3 11 2.8100 - 2.7200 0.97 1220 135 0.1508 0.2398
REMARK 3 12 2.7200 - 2.6400 0.95 1210 127 0.1508 0.2442
REMARK 3 13 2.6400 - 2.5700 0.95 1191 131 0.1419 0.2893
REMARK 3 14 2.5700 - 2.5100 0.93 1159 131 0.1399 0.2858
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) : 0.230
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 22.660
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 28.74
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 : NULL
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : 1
REMARK 3 NCS GROUP : 1
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: (CHAIN A AND (RESID 7 THROUGH 259 OR
REMARK 3 RESID 261 THROUGH 282))
REMARK 3 SELECTION : (CHAIN B AND (RESID 7 THROUGH 259 OR
REMARK 3 RESID 261 THROUGH 282))
REMARK 3 ATOM PAIRS NUMBER : 2430
REMARK 3 RMSD : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 7MYG COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 21-MAY-21.
REMARK 100 THE DEPOSITION ID IS D_1000257025.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 16-FEB-21
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
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) : 0.9787
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 : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 19458
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.510
REMARK 200 RESOLUTION RANGE LOW (A) : 59.460
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.0
REMARK 200 DATA REDUNDANCY : 5.500
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 15.3500
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.51
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.60
REMARK 200 COMPLETENESS FOR SHELL (%) : 94.3
REMARK 200 DATA REDUNDANCY IN SHELL : 5.20
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: 1DQZ
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 46.67
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.31
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 8% V/V TACSIMATE (PH 7.0) AND 20 % W/V
REMARK 280 POLYETHYLENE GLYCOL 3,350, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 298.15K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 35.30300
REMARK 290 SMTRY3 2 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 ASN A 211
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 ILE A 222
REMARK 465 GLY B 5
REMARK 465 LEU B 6
REMARK 465 ASN B 211
REMARK 465 GLY B 212
REMARK 465 THR B 213
REMARK 465 PRO B 214
REMARK 465 SER B 215
REMARK 465 ASP B 216
REMARK 465 LEU B 217
REMARK 465 GLY B 218
REMARK 465 GLY B 219
REMARK 465 ASP B 220
REMARK 465 ASN B 221
REMARK 465 ILE B 222
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 LEU A 6 CG CD1 CD2
REMARK 470 SER A 156 CB OG
REMARK 470 SER B 156 CB 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 LEU A 6 141.17 178.05
REMARK 500 ARG A 41 39.70 -98.83
REMARK 500 PRO A 54 42.35 -89.34
REMARK 500 SER A 86 -41.77 -178.73
REMARK 500 ARG A 101 -53.55 -126.27
REMARK 500 SER A 124 -125.79 51.36
REMARK 500 ASN A 152 56.07 -145.40
REMARK 500 SER A 156 -116.92 60.90
REMARK 500 ARG B 41 40.94 -99.59
REMARK 500 PRO B 54 40.45 -88.63
REMARK 500 SER B 86 -41.78 -179.90
REMARK 500 SER B 124 -128.11 52.19
REMARK 500 ASN B 152 56.13 -144.15
REMARK 500 SER B 156 -125.69 65.73
REMARK 500 PHE B 254 67.06 -116.66
REMARK 500
REMARK 500 REMARK: NULL
DBREF1 7MYG A 5 282 UNP A0A045JX50_MYCTX
DBREF2 7MYG A A0A045JX50 51 328
DBREF1 7MYG B 5 282 UNP A0A045JX50_MYCTX
DBREF2 7MYG B A0A045JX50 51 328
SEQADV 7MYG SER A 156 UNP A0A045JX5 GLY 202 CONFLICT
SEQADV 7MYG SER B 156 UNP A0A045JX5 GLY 202 CONFLICT
SEQRES 1 A 278 GLY LEU PRO VAL GLU TYR LEU GLN VAL PRO SER ALA SER
SEQRES 2 A 278 MET GLY ARG ASP ILE LYS VAL GLN PHE GLN GLY GLY GLY
SEQRES 3 A 278 PRO HIS ALA VAL TYR LEU LEU ASP GLY LEU ARG ALA GLN
SEQRES 4 A 278 ASP ASP TYR ASN GLY TRP ASP ILE ASN THR PRO ALA PHE
SEQRES 5 A 278 GLU GLU TYR TYR GLN SER GLY LEU SER VAL ILE MET PRO
SEQRES 6 A 278 VAL GLY GLY GLN SER SER PHE TYR THR ASP TRP TYR GLN
SEQRES 7 A 278 PRO SER GLN SER ASN GLY GLN ASN TYR THR TYR LYS TRP
SEQRES 8 A 278 GLU THR PHE LEU THR ARG GLU MET PRO ALA TRP LEU GLN
SEQRES 9 A 278 ALA ASN LYS GLY VAL SER PRO THR GLY ASN ALA ALA VAL
SEQRES 10 A 278 GLY LEU SER MET SER GLY GLY SER ALA LEU ILE LEU ALA
SEQRES 11 A 278 ALA TYR TYR PRO GLN GLN PHE PRO TYR ALA ALA SER LEU
SEQRES 12 A 278 SER GLY PHE LEU ASN PRO SER GLU SER TRP TRP PRO THR
SEQRES 13 A 278 LEU ILE GLY LEU ALA MET ASN ASP SER GLY GLY TYR ASN
SEQRES 14 A 278 ALA ASN SER MET TRP GLY PRO SER SER ASP PRO ALA TRP
SEQRES 15 A 278 LYS ARG ASN ASP PRO MET VAL GLN ILE PRO ARG LEU VAL
SEQRES 16 A 278 ALA ASN ASN THR ARG ILE TRP VAL TYR CYS GLY ASN GLY
SEQRES 17 A 278 THR PRO SER ASP LEU GLY GLY ASP ASN ILE PRO ALA LYS
SEQRES 18 A 278 PHE LEU GLU GLY LEU THR LEU ARG THR ASN GLN THR PHE
SEQRES 19 A 278 ARG ASP THR TYR ALA ALA ASP GLY GLY ARG ASN GLY VAL
SEQRES 20 A 278 PHE ASN PHE PRO PRO ASN GLY THR HIS SER TRP PRO TYR
SEQRES 21 A 278 TRP ASN GLU GLN LEU VAL ALA MET LYS ALA ASP ILE GLN
SEQRES 22 A 278 HIS VAL LEU ASN GLY
SEQRES 1 B 278 GLY LEU PRO VAL GLU TYR LEU GLN VAL PRO SER ALA SER
SEQRES 2 B 278 MET GLY ARG ASP ILE LYS VAL GLN PHE GLN GLY GLY GLY
SEQRES 3 B 278 PRO HIS ALA VAL TYR LEU LEU ASP GLY LEU ARG ALA GLN
SEQRES 4 B 278 ASP ASP TYR ASN GLY TRP ASP ILE ASN THR PRO ALA PHE
SEQRES 5 B 278 GLU GLU TYR TYR GLN SER GLY LEU SER VAL ILE MET PRO
SEQRES 6 B 278 VAL GLY GLY GLN SER SER PHE TYR THR ASP TRP TYR GLN
SEQRES 7 B 278 PRO SER GLN SER ASN GLY GLN ASN TYR THR TYR LYS TRP
SEQRES 8 B 278 GLU THR PHE LEU THR ARG GLU MET PRO ALA TRP LEU GLN
SEQRES 9 B 278 ALA ASN LYS GLY VAL SER PRO THR GLY ASN ALA ALA VAL
SEQRES 10 B 278 GLY LEU SER MET SER GLY GLY SER ALA LEU ILE LEU ALA
SEQRES 11 B 278 ALA TYR TYR PRO GLN GLN PHE PRO TYR ALA ALA SER LEU
SEQRES 12 B 278 SER GLY PHE LEU ASN PRO SER GLU SER TRP TRP PRO THR
SEQRES 13 B 278 LEU ILE GLY LEU ALA MET ASN ASP SER GLY GLY TYR ASN
SEQRES 14 B 278 ALA ASN SER MET TRP GLY PRO SER SER ASP PRO ALA TRP
SEQRES 15 B 278 LYS ARG ASN ASP PRO MET VAL GLN ILE PRO ARG LEU VAL
SEQRES 16 B 278 ALA ASN ASN THR ARG ILE TRP VAL TYR CYS GLY ASN GLY
SEQRES 17 B 278 THR PRO SER ASP LEU GLY GLY ASP ASN ILE PRO ALA LYS
SEQRES 18 B 278 PHE LEU GLU GLY LEU THR LEU ARG THR ASN GLN THR PHE
SEQRES 19 B 278 ARG ASP THR TYR ALA ALA ASP GLY GLY ARG ASN GLY VAL
SEQRES 20 B 278 PHE ASN PHE PRO PRO ASN GLY THR HIS SER TRP PRO TYR
SEQRES 21 B 278 TRP ASN GLU GLN LEU VAL ALA MET LYS ALA ASP ILE GLN
SEQRES 22 B 278 HIS VAL LEU ASN GLY
HET GOL A 301 6
HET GOL A 302 6
HET GOL A 303 6
HET GOL A 304 6
HET GOL A 305 6
HET GOL A 306 6
HET GOL A 307 6
HET GOL B 301 6
HET GOL B 302 6
HET GOL B 303 6
HET GOL B 304 6
HET GOL B 305 6
HET GOL B 306 6
HET GOL B 307 6
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 3 GOL 14(C3 H8 O3)
FORMUL 17 HOH *122(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 202 1 9
HELIX 10 AB1 ALA A 224 ASP A 245 1 22
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 ALA B 224 ASP B 245 1 22
HELIX 23 AC5 SER B 261 GLY B 282 1 22
SHEET 1 AA1 8 GLU A 9 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 VAL A 207
SHEET 1 AA2 8 GLU B 9 SER B 15 0
SHEET 2 AA2 8 ARG B 20 GLN B 27 -1 O VAL B 24 N LEU B 11
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
CRYST1 59.458 70.606 68.590 90.00 89.97 90.00 P 1 21 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 0.016819 0.000000 -0.000008 0.00000
SCALE2 0.000000 0.014163 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014579 0.00000
TER 2085 GLY A 282
TER 4161 GLY B 282
MASTER 286 0 14 23 16 0 0 6 4351 2 84 44
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