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HEADER TRANSFERASE 16-SEP-13 4MQM
TITLE CRYSTAL STRUCTURE OF ANTIGEN 85C IN PRESENCE OF EBSELEN
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
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 4MQM 1 JRNL
REVDAT 1 13-NOV-13 4MQM 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. 1.35 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) : 1.35
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.70
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.8
REMARK 3 NUMBER OF REFLECTIONS : 68678
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.171
REMARK 3 R VALUE (WORKING SET) : 0.170
REMARK 3 FREE R VALUE : 0.191
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.990
REMARK 3 FREE R VALUE TEST SET COUNT : 3429
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 29.7036 - 3.8805 0.96 2857 152 0.1716 0.1872
REMARK 3 2 3.8805 - 3.0811 0.98 2778 146 0.1825 0.1855
REMARK 3 3 3.0811 - 2.6920 1.00 2789 148 0.1871 0.1938
REMARK 3 4 2.6920 - 2.4460 1.00 2790 147 0.1807 0.1982
REMARK 3 5 2.4460 - 2.2707 1.00 2748 144 0.1673 0.1942
REMARK 3 6 2.2707 - 2.1369 1.00 2746 145 0.1628 0.1950
REMARK 3 7 2.1369 - 2.0299 1.00 2754 145 0.1629 0.2021
REMARK 3 8 2.0299 - 1.9415 1.00 2761 145 0.1644 0.1856
REMARK 3 9 1.9415 - 1.8668 1.00 2758 145 0.1637 0.1754
REMARK 3 10 1.8668 - 1.8024 1.00 2744 145 0.1525 0.1884
REMARK 3 11 1.8024 - 1.7460 1.00 2716 143 0.1551 0.2025
REMARK 3 12 1.7460 - 1.6961 1.00 2738 145 0.1394 0.1872
REMARK 3 13 1.6961 - 1.6515 1.00 2737 143 0.1319 0.1475
REMARK 3 14 1.6515 - 1.6112 1.00 2737 145 0.1271 0.1795
REMARK 3 15 1.6112 - 1.5746 1.00 2709 142 0.1211 0.1768
REMARK 3 16 1.5746 - 1.5411 1.00 2737 143 0.1311 0.1851
REMARK 3 17 1.5411 - 1.5102 1.00 2703 143 0.1463 0.1707
REMARK 3 18 1.5102 - 1.4817 1.00 2722 144 0.1573 0.2118
REMARK 3 19 1.4817 - 1.4553 1.00 2735 142 0.1634 0.1853
REMARK 3 20 1.4553 - 1.4306 1.00 2703 142 0.1665 0.1884
REMARK 3 21 1.4306 - 1.4075 1.00 2691 141 0.1812 0.2455
REMARK 3 22 1.4075 - 1.3859 0.99 2690 142 0.2053 0.2288
REMARK 3 23 1.3859 - 1.3655 0.97 2643 136 0.2316 0.2868
REMARK 3 24 1.3655 - 1.3463 0.83 2263 116 0.2542 0.2728
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) : 19.070
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 : 0.005 2176
REMARK 3 ANGLE : 1.061 2976
REMARK 3 CHIRALITY : 0.077 297
REMARK 3 PLANARITY : 0.006 394
REMARK 3 DIHEDRAL : 13.352 764
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 4MQM 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 RCSB082243.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 17-JUN-12
REMARK 200 TEMPERATURE (KELVIN) : 100
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-G
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97922
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 : 68823
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.346
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 (%) : 99.2
REMARK 200 DATA REDUNDANCY : 10.500
REMARK 200 R MERGE (I) : 0.06900
REMARK 200 R SYM (I) : 0.06900
REMARK 200 FOR THE DATA SET : 29.6000
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) : 50.00
REMARK 200 COMPLETENESS FOR SHELL (%) : 93.6
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 (%): 47.17
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.33
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 25% PEG 1500, PH 7.5, VAPOR DIFFUSION,
REMARK 280 HANGING DROP, 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 30.32150
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 37.55200
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 34.05950
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 37.55200
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 30.32150
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 34.05950
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 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 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 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 ARG A 3 CB CG CD NE CZ NH1 NH2
REMARK 470 HIS A 260 ND1 CD2 CE1 NE2
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 LEU A 6 NH1 ARG A 239 3746 2.14
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 PRO A 54 36.31 -92.68
REMARK 500 SER A 74 19.87 58.21
REMARK 500 PHE A 76 18.08 55.81
REMARK 500 ARG A 101 -61.91 -129.49
REMARK 500 SER A 124 -124.52 49.06
REMARK 500 ASN A 152 59.09 -141.83
REMARK 500 SER A 169 77.23 -106.55
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4MQL RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF ANTIGEN 85C-C209S MUTANT
DBREF 4MQM A 0 294 UNP P0A4V4 A85C_MYCTU 46 340
SEQADV 4MQM MET A -1 UNP P0A4V4 EXPRESSION TAG
SEQADV 4MQM LEU A 295 UNP P0A4V4 EXPRESSION TAG
SEQADV 4MQM GLU A 296 UNP P0A4V4 EXPRESSION TAG
SEQADV 4MQM HIS A 297 UNP P0A4V4 EXPRESSION TAG
SEQADV 4MQM HIS A 298 UNP P0A4V4 EXPRESSION TAG
SEQADV 4MQM HIS A 299 UNP P0A4V4 EXPRESSION TAG
SEQADV 4MQM HIS A 300 UNP P0A4V4 EXPRESSION TAG
SEQADV 4MQM HIS A 301 UNP P0A4V4 EXPRESSION TAG
SEQADV 4MQM 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 CYS 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
FORMUL 2 HOH *163(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 VAL A 24 N LEU A 11
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 LEU A 6 PRO A 7 0 0.79
CRYST1 60.643 68.119 75.104 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 0.016490 0.000000 0.000000 0.00000
SCALE2 0.000000 0.014680 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013315 0.00000
TER 2106 GLY A 282
MASTER 310 0 0 12 8 0 0 6 2258 1 0 24
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