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HEADER TRANSFERASE 10-SEP-12 4H18
TITLE THREE DIMENSIONAL STRUCTURE OF CORYNOMYCOLOYL TRANFERASE C
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CMT1;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 SYNONYM: HYPOTHETICAL ESTERASE, PUTATIVE UNCHARACTERIZED PROTEIN
COMPND 5 CGL0343, TREHALOSE CORYNOMYCOLYL TRANSFERASE;
COMPND 6 EC: 2.3.1.122;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: CORYNEBACTERIUM GLUTAMICUM;
SOURCE 3 ORGANISM_TAXID: 196627;
SOURCE 4 STRAIN: ATCC 13032;
SOURCE 5 GENE: CMT1, CMT1, CG0413, CGL0343, WA5_0336;
SOURCE 6 EXPRESSION_SYSTEM: CORYNEBACTERIUM GLUTAMICUM;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 196627;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PCGL482
KEYWDS ALPHA / BETA HYDROLASE, MYCOLOYLTRANSFERASE, TREHALOSE O-
KEYWDS 2 MYCOLYLTRANSFERASE, EXTERNAL MEMBRANE, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR E.HUC,C.DE SOUSA D'AURIA,I.LI DE LA SIERRA-GALLAY,CH.SALMERON,H.VAN
AUTHOR 2 TILBEURGH,N.BAYAN,CH.HOUSSIN,M.DAFFE,M.TROPIS
REVDAT 1 25-SEP-13 4H18 0
JRNL AUTH E.HUC,C.DE SOUSA-D'AURIA,I.L.DE LA SIERRA-GALLAY,C.SALMERON,
JRNL AUTH 2 H.VAN TILBEURGH,N.BAYAN,C.HOUSSIN,M.DAFFE,M.TROPIS
JRNL TITL IDENTIFICATION OF A MYCOLOYL TRANSFERASE SELECTIVELY
JRNL TITL 2 INVOLVED IN O-ACYLATION OF POLYPEPTIDES IN
JRNL TITL 3 CORYNEBACTERIALES.
JRNL REF J.BACTERIOL. V. 195 4121 2013
JRNL REFN ISSN 0021-9193
JRNL PMID 23852866
JRNL DOI 10.1128/JB.00285-13
REMARK 2
REMARK 2 RESOLUTION. 1.75 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) : 1.75
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 37.65
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.990
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 3 NUMBER OF REFLECTIONS : 128479
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.165
REMARK 3 R VALUE (WORKING SET) : 0.163
REMARK 3 FREE R VALUE : 0.203
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 6424
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 37.6549 - 5.4474 0.97 4258 224 0.1701 0.1591
REMARK 3 2 5.4474 - 4.3258 0.99 4164 219 0.1408 0.1669
REMARK 3 3 4.3258 - 3.7796 0.99 4119 217 0.1344 0.1651
REMARK 3 4 3.7796 - 3.4342 0.99 4084 215 0.1500 0.1934
REMARK 3 5 3.4342 - 3.1882 0.99 4129 218 0.1564 0.1858
REMARK 3 6 3.1882 - 3.0003 0.99 4090 215 0.1611 0.1906
REMARK 3 7 3.0003 - 2.8501 0.99 4091 215 0.1644 0.1925
REMARK 3 8 2.8501 - 2.7261 1.00 4082 215 0.1675 0.2123
REMARK 3 9 2.7261 - 2.6212 1.00 4075 214 0.1663 0.2180
REMARK 3 10 2.6212 - 2.5308 1.00 4064 214 0.1645 0.2065
REMARK 3 11 2.5308 - 2.4516 1.00 4074 215 0.1615 0.2125
REMARK 3 12 2.4516 - 2.3816 1.00 4064 214 0.1601 0.2179
REMARK 3 13 2.3816 - 2.3189 1.00 4078 214 0.1593 0.2000
REMARK 3 14 2.3189 - 2.2623 1.00 4067 214 0.1622 0.2013
REMARK 3 15 2.2623 - 2.2109 1.00 4062 214 0.1612 0.2219
REMARK 3 16 2.2109 - 2.1639 1.00 4052 213 0.1590 0.2116
REMARK 3 17 2.1639 - 2.1206 1.00 4044 213 0.1596 0.2112
REMARK 3 18 2.1206 - 2.0806 1.00 4068 214 0.1625 0.2212
REMARK 3 19 2.0806 - 2.0434 1.00 4022 212 0.1606 0.2149
REMARK 3 20 2.0434 - 2.0088 1.00 4034 212 0.1591 0.2210
REMARK 3 21 2.0088 - 1.9764 1.00 4075 215 0.1678 0.2126
REMARK 3 22 1.9764 - 1.9460 1.00 4027 212 0.1727 0.2163
REMARK 3 23 1.9460 - 1.9173 1.00 4056 213 0.1729 0.2444
REMARK 3 24 1.9173 - 1.8903 1.00 4076 215 0.1849 0.2440
REMARK 3 25 1.8903 - 1.8648 1.00 4012 211 0.1896 0.2509
REMARK 3 26 1.8648 - 1.8406 1.00 4059 214 0.1904 0.2430
REMARK 3 27 1.8406 - 1.8176 1.00 4020 211 0.1968 0.2589
REMARK 3 28 1.8176 - 1.7957 1.00 4058 214 0.2085 0.2745
REMARK 3 29 1.7957 - 1.7748 1.00 4049 213 0.2256 0.2637
REMARK 3 30 1.7748 - 1.7550 0.97 3902 205 0.2391 0.2834
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) : 0.180
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 18.420
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 22.82
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 : 0.012 9832
REMARK 3 ANGLE : 1.386 13435
REMARK 3 CHIRALITY : 0.096 1439
REMARK 3 PLANARITY : 0.008 1761
REMARK 3 DIHEDRAL : 14.003 3483
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 4H18 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-SEP-12.
REMARK 100 THE RCSB ID CODE IS RCSB074890.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 08-APR-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 : SOLEIL
REMARK 200 BEAMLINE : PROXIMA 1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9788
REMARK 200 MONOCHROMATOR : CRYSTAL
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 128495
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.755
REMARK 200 RESOLUTION RANGE LOW (A) : 42.811
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 200 DATA REDUNDANCY : 3.890
REMARK 200 R MERGE (I) : 0.15400
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 9.4600
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.75
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.86
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.3
REMARK 200 DATA REDUNDANCY IN SHELL : 3.91
REMARK 200 R MERGE FOR SHELL (I) : 0.64300
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.600
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 1VA5
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 38.15
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.99
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG 4000, 0.2M MAGNESIUM CHLORIDE,
REMARK 280 0.1M MES, PH 6.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
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 42.90200
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 95.34400
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 42.90200
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 95.34400
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5, 6, 7
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 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 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 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C
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: 4
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D
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: 5
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1310 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 23780 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -16.0 KCAL/MOL
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 APPLY THE FOLLOWING TO CHAINS: C
REMARK 350 BIOMT1 2 1.000000 0.000000 0.000000 42.90200
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 95.34400
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 78.49700
REMARK 350
REMARK 350 BIOMOLECULE: 6
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1410 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 23710 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -22.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D
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 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350 BIOMT1 2 1.000000 0.000000 0.000000 42.90200
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 95.34400
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 7
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 5540 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 44680 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -47.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 42.90200
REMARK 350 BIOMT2 1 0.000000 -1.000000 0.000000 95.34400
REMARK 350 BIOMT3 1 0.000000 0.000000 -1.000000 78.49700
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350 BIOMT1 2 1.000000 0.000000 0.000000 42.90200
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 95.34400
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, D
REMARK 350 BIOMT1 3 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 3 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 3 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 B 434 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 LYS A 2
REMARK 465 LEU A 3
REMARK 465 LEU A 4
REMARK 465 ARG A 5
REMARK 465 ARG A 6
REMARK 465 ILE A 7
REMARK 465 ALA A 8
REMARK 465 ALA A 9
REMARK 465 PRO A 10
REMARK 465 ALA A 11
REMARK 465 ILE A 12
REMARK 465 ALA A 13
REMARK 465 LEU A 14
REMARK 465 GLY A 15
REMARK 465 ILE A 16
REMARK 465 ALA A 17
REMARK 465 MET A 18
REMARK 465 SER A 19
REMARK 465 THR A 20
REMARK 465 ILE A 21
REMARK 465 VAL A 22
REMARK 465 THR A 23
REMARK 465 PRO A 24
REMARK 465 SER A 25
REMARK 465 THR A 26
REMARK 465 ALA A 27
REMARK 465 GLY A 28
REMARK 465 ALA A 29
REMARK 465 SER A 281
REMARK 465 VAL A 282
REMARK 465 ASP A 283
REMARK 465 SER A 284
REMARK 465 PRO A 285
REMARK 465 ARG A 286
REMARK 465 PHE A 287
REMARK 465 GLU A 288
REMARK 465 GLY A 289
REMARK 465 LEU A 290
REMARK 465 ASN A 291
REMARK 465 GLN A 292
REMARK 465 GLN A 293
REMARK 465 VAL A 294
REMARK 465 GLN A 295
REMARK 465 SER A 296
REMARK 465 ILE A 297
REMARK 465 ALA A 298
REMARK 465 MET A 299
REMARK 465 ALA A 300
REMARK 465 GLU A 301
REMARK 465 THR A 302
REMARK 465 VAL A 303
REMARK 465 VAL A 304
REMARK 465 ALA A 365
REMARK 465 HIS A 366
REMARK 465 HIS A 367
REMARK 465 HIS A 368
REMARK 465 HIS A 369
REMARK 465 HIS A 370
REMARK 465 HIS A 371
REMARK 465 MET B 1
REMARK 465 LYS B 2
REMARK 465 LEU B 3
REMARK 465 LEU B 4
REMARK 465 ARG B 5
REMARK 465 ARG B 6
REMARK 465 ILE B 7
REMARK 465 ALA B 8
REMARK 465 ALA B 9
REMARK 465 PRO B 10
REMARK 465 ALA B 11
REMARK 465 ILE B 12
REMARK 465 ALA B 13
REMARK 465 LEU B 14
REMARK 465 GLY B 15
REMARK 465 ILE B 16
REMARK 465 ALA B 17
REMARK 465 MET B 18
REMARK 465 SER B 19
REMARK 465 THR B 20
REMARK 465 ILE B 21
REMARK 465 VAL B 22
REMARK 465 THR B 23
REMARK 465 PRO B 24
REMARK 465 SER B 25
REMARK 465 THR B 26
REMARK 465 ALA B 27
REMARK 465 GLY B 28
REMARK 465 ALA B 29
REMARK 465 SER B 281
REMARK 465 VAL B 282
REMARK 465 ASP B 283
REMARK 465 SER B 284
REMARK 465 PRO B 285
REMARK 465 ARG B 286
REMARK 465 PHE B 287
REMARK 465 GLU B 288
REMARK 465 GLY B 289
REMARK 465 LEU B 290
REMARK 465 ASN B 291
REMARK 465 GLN B 292
REMARK 465 GLN B 293
REMARK 465 VAL B 294
REMARK 465 GLN B 295
REMARK 465 SER B 296
REMARK 465 ILE B 297
REMARK 465 ALA B 298
REMARK 465 MET B 299
REMARK 465 ALA B 300
REMARK 465 GLU B 301
REMARK 465 THR B 302
REMARK 465 VAL B 303
REMARK 465 VAL B 304
REMARK 465 GLU B 364
REMARK 465 ALA B 365
REMARK 465 HIS B 366
REMARK 465 HIS B 367
REMARK 465 HIS B 368
REMARK 465 HIS B 369
REMARK 465 HIS B 370
REMARK 465 HIS B 371
REMARK 465 MET C 1
REMARK 465 LYS C 2
REMARK 465 LEU C 3
REMARK 465 LEU C 4
REMARK 465 ARG C 5
REMARK 465 ARG C 6
REMARK 465 ILE C 7
REMARK 465 ALA C 8
REMARK 465 ALA C 9
REMARK 465 PRO C 10
REMARK 465 ALA C 11
REMARK 465 ILE C 12
REMARK 465 ALA C 13
REMARK 465 LEU C 14
REMARK 465 GLY C 15
REMARK 465 ILE C 16
REMARK 465 ALA C 17
REMARK 465 MET C 18
REMARK 465 SER C 19
REMARK 465 THR C 20
REMARK 465 ILE C 21
REMARK 465 VAL C 22
REMARK 465 THR C 23
REMARK 465 PRO C 24
REMARK 465 SER C 25
REMARK 465 THR C 26
REMARK 465 ALA C 27
REMARK 465 GLY C 28
REMARK 465 ALA C 29
REMARK 465 LEU C 275
REMARK 465 ALA C 276
REMARK 465 GLY C 277
REMARK 465 GLU C 278
REMARK 465 TRP C 279
REMARK 465 GLU C 280
REMARK 465 SER C 281
REMARK 465 VAL C 282
REMARK 465 ASP C 283
REMARK 465 SER C 284
REMARK 465 PRO C 285
REMARK 465 ARG C 286
REMARK 465 PHE C 287
REMARK 465 GLU C 288
REMARK 465 GLY C 289
REMARK 465 LEU C 290
REMARK 465 ASN C 291
REMARK 465 GLN C 292
REMARK 465 GLN C 293
REMARK 465 VAL C 294
REMARK 465 GLN C 295
REMARK 465 SER C 296
REMARK 465 ILE C 297
REMARK 465 ALA C 298
REMARK 465 MET C 299
REMARK 465 ALA C 300
REMARK 465 THR C 338
REMARK 465 GLY C 339
REMARK 465 THR C 340
REMARK 465 ALA C 365
REMARK 465 HIS C 366
REMARK 465 HIS C 367
REMARK 465 HIS C 368
REMARK 465 HIS C 369
REMARK 465 HIS C 370
REMARK 465 HIS C 371
REMARK 465 MET D 1
REMARK 465 LYS D 2
REMARK 465 LEU D 3
REMARK 465 LEU D 4
REMARK 465 ARG D 5
REMARK 465 ARG D 6
REMARK 465 ILE D 7
REMARK 465 ALA D 8
REMARK 465 ALA D 9
REMARK 465 PRO D 10
REMARK 465 ALA D 11
REMARK 465 ILE D 12
REMARK 465 ALA D 13
REMARK 465 LEU D 14
REMARK 465 GLY D 15
REMARK 465 ILE D 16
REMARK 465 ALA D 17
REMARK 465 MET D 18
REMARK 465 SER D 19
REMARK 465 THR D 20
REMARK 465 ILE D 21
REMARK 465 VAL D 22
REMARK 465 THR D 23
REMARK 465 PRO D 24
REMARK 465 SER D 25
REMARK 465 THR D 26
REMARK 465 ALA D 27
REMARK 465 GLY D 28
REMARK 465 ALA D 29
REMARK 465 LEU D 275
REMARK 465 ALA D 276
REMARK 465 GLY D 277
REMARK 465 GLU D 278
REMARK 465 TRP D 279
REMARK 465 GLU D 280
REMARK 465 SER D 281
REMARK 465 VAL D 282
REMARK 465 ASP D 283
REMARK 465 SER D 284
REMARK 465 PRO D 285
REMARK 465 ARG D 286
REMARK 465 PHE D 287
REMARK 465 GLU D 288
REMARK 465 GLY D 289
REMARK 465 LEU D 290
REMARK 465 ASN D 291
REMARK 465 GLN D 292
REMARK 465 GLN D 293
REMARK 465 VAL D 294
REMARK 465 GLN D 295
REMARK 465 SER D 296
REMARK 465 ILE D 297
REMARK 465 ALA D 298
REMARK 465 MET D 299
REMARK 465 ALA D 300
REMARK 465 GLY D 339
REMARK 465 THR D 340
REMARK 465 GLU D 364
REMARK 465 ALA D 365
REMARK 465 HIS D 366
REMARK 465 HIS D 367
REMARK 465 HIS D 368
REMARK 465 HIS D 369
REMARK 465 HIS D 370
REMARK 465 HIS D 371
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ARG C 70 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 ARG C 70 NE - CZ - NH2 ANGL. DEV. = -4.5 DEGREES
REMARK 500 ARG C 83 NE - CZ - NH2 ANGL. DEV. = -4.2 DEGREES
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 TYR A 144 14.39 52.39
REMARK 500 SER A 189 -121.82 62.49
REMARK 500 THR A 218 -7.95 -142.84
REMARK 500 SER A 342 -174.78 -66.34
REMARK 500 ALA B 115 76.24 -100.31
REMARK 500 TYR B 144 15.98 54.27
REMARK 500 SER B 189 -120.67 61.32
REMARK 500 THR B 218 -13.43 -143.30
REMARK 500 ASN B 253 37.01 -99.66
REMARK 500 SER B 342 -173.30 -60.34
REMARK 500 TYR C 144 15.50 56.04
REMARK 500 SER C 189 -121.43 51.94
REMARK 500 THR C 218 -6.26 -145.04
REMARK 500 ASN C 271 -158.95 -92.40
REMARK 500 ASP D 122 37.18 -91.83
REMARK 500 ASN D 131 78.28 -101.69
REMARK 500 TYR D 144 13.33 57.26
REMARK 500 SER D 189 -127.04 59.67
REMARK 500 THR D 218 -6.18 -143.97
REMARK 500 ASN D 271 -158.91 -90.52
REMARK 500 SER D 273 111.99 -169.49
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG D 401 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU D 139 OE2
REMARK 620 2 HOH D 721 O 88.6
REMARK 620 3 HOH D 508 O 89.5 90.3
REMARK 620 4 HOH D 585 O 91.7 177.9 91.8
REMARK 620 5 HOH D 686 O 174.4 87.4 86.6 92.4
REMARK 620 6 HOH D 572 O 90.5 91.7 178.0 86.2 93.6
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG D 401
DBREF 4H18 A 1 365 UNP Q8NTG4 Q8NTG4_CORGL 1 365
DBREF 4H18 B 1 365 UNP Q8NTG4 Q8NTG4_CORGL 1 365
DBREF 4H18 C 1 365 UNP Q8NTG4 Q8NTG4_CORGL 1 365
DBREF 4H18 D 1 365 UNP Q8NTG4 Q8NTG4_CORGL 1 365
SEQADV 4H18 HIS A 366 UNP Q8NTG4 EXPRESSION TAG
SEQADV 4H18 HIS A 367 UNP Q8NTG4 EXPRESSION TAG
SEQADV 4H18 HIS A 368 UNP Q8NTG4 EXPRESSION TAG
SEQADV 4H18 HIS A 369 UNP Q8NTG4 EXPRESSION TAG
SEQADV 4H18 HIS A 370 UNP Q8NTG4 EXPRESSION TAG
SEQADV 4H18 HIS A 371 UNP Q8NTG4 EXPRESSION TAG
SEQADV 4H18 HIS B 366 UNP Q8NTG4 EXPRESSION TAG
SEQADV 4H18 HIS B 367 UNP Q8NTG4 EXPRESSION TAG
SEQADV 4H18 HIS B 368 UNP Q8NTG4 EXPRESSION TAG
SEQADV 4H18 HIS B 369 UNP Q8NTG4 EXPRESSION TAG
SEQADV 4H18 HIS B 370 UNP Q8NTG4 EXPRESSION TAG
SEQADV 4H18 HIS B 371 UNP Q8NTG4 EXPRESSION TAG
SEQADV 4H18 HIS C 366 UNP Q8NTG4 EXPRESSION TAG
SEQADV 4H18 HIS C 367 UNP Q8NTG4 EXPRESSION TAG
SEQADV 4H18 HIS C 368 UNP Q8NTG4 EXPRESSION TAG
SEQADV 4H18 HIS C 369 UNP Q8NTG4 EXPRESSION TAG
SEQADV 4H18 HIS C 370 UNP Q8NTG4 EXPRESSION TAG
SEQADV 4H18 HIS C 371 UNP Q8NTG4 EXPRESSION TAG
SEQADV 4H18 HIS D 366 UNP Q8NTG4 EXPRESSION TAG
SEQADV 4H18 HIS D 367 UNP Q8NTG4 EXPRESSION TAG
SEQADV 4H18 HIS D 368 UNP Q8NTG4 EXPRESSION TAG
SEQADV 4H18 HIS D 369 UNP Q8NTG4 EXPRESSION TAG
SEQADV 4H18 HIS D 370 UNP Q8NTG4 EXPRESSION TAG
SEQADV 4H18 HIS D 371 UNP Q8NTG4 EXPRESSION TAG
SEQRES 1 A 371 MET LYS LEU LEU ARG ARG ILE ALA ALA PRO ALA ILE ALA
SEQRES 2 A 371 LEU GLY ILE ALA MET SER THR ILE VAL THR PRO SER THR
SEQRES 3 A 371 ALA GLY ALA ALA GLU VAL THR PRO ALA ASP VAL ALA GLY
SEQRES 4 A 371 ASP THR ALA LEU SER THR ILE SER ASP SER ALA PRO ALA
SEQRES 5 A 371 ASP GLU ALA SER ALA PRO ARG TRP ARG ALA HIS VAL ASN
SEQRES 6 A 371 ALA ALA ASP GLU ARG VAL LYS GLU MET TRP ALA TYR SER
SEQRES 7 A 371 PRO SER MET ASP ARG ASN VAL PRO LEU VAL VAL ILE THR
SEQRES 8 A 371 ALA ASP GLU SER ALA GLY PRO ARG PRO VAL ILE TYR LEU
SEQRES 9 A 371 LEU ASN GLY GLY ASP GLY GLY GLU GLY ALA ALA ASN TRP
SEQRES 10 A 371 VAL MET GLN THR ASP VAL LEU ASP PHE TYR LEU GLU LYS
SEQRES 11 A 371 ASN VAL ASN VAL VAL ILE PRO MET GLU GLY LYS PHE SER
SEQRES 12 A 371 TYR TYR THR ASP TRP VAL GLU GLU ASN ALA SER LEU GLY
SEQRES 13 A 371 GLY LYS GLN MET TRP GLU THR PHE LEU VAL LYS GLU LEU
SEQRES 14 A 371 PRO GLY PRO LEU GLU GLU LYS LEU ASN THR ASP GLY GLN
SEQRES 15 A 371 ARG ALA ILE ALA GLY MET SER MET SER ALA THR THR SER
SEQRES 16 A 371 LEU LEU PHE PRO GLN HIS PHE PRO GLY PHE TYR ASP ALA
SEQRES 17 A 371 ALA ALA SER PHE SER GLY CYS ALA ALA THR SER SER LEU
SEQRES 18 A 371 LEU PRO TRP GLU TYR LEU LYS LEU THR LEU ASP ARG GLY
SEQRES 19 A 371 ASN ALA THR PRO GLU GLN MET TRP GLY PRO ARG GLY GLY
SEQRES 20 A 371 GLU TYR ASN ILE TYR ASN ASP ALA LEU ILE ASN SER ASP
SEQRES 21 A 371 LYS LEU ARG GLY THR GLU LEU TYR VAL SER ASN ALA SER
SEQRES 22 A 371 GLY LEU ALA GLY GLU TRP GLU SER VAL ASP SER PRO ARG
SEQRES 23 A 371 PHE GLU GLY LEU ASN GLN GLN VAL GLN SER ILE ALA MET
SEQRES 24 A 371 ALA GLU THR VAL VAL THR GLY GLY ILE ILE GLU ALA ALA
SEQRES 25 A 371 THR ASN LYS CYS THR HIS ASP LEU LYS ALA LYS LEU ASP
SEQRES 26 A 371 SER ALA GLY ILE PRO ALA ASP TRP ASN LEU ARG PRO THR
SEQRES 27 A 371 GLY THR HIS SER TRP GLY TRP TRP GLN ASP ASP LEU ARG
SEQRES 28 A 371 GLY SER TRP THR THR PHE ALA ARG ALA PHE GLU LEU GLU
SEQRES 29 A 371 ALA HIS HIS HIS HIS HIS HIS
SEQRES 1 B 371 MET LYS LEU LEU ARG ARG ILE ALA ALA PRO ALA ILE ALA
SEQRES 2 B 371 LEU GLY ILE ALA MET SER THR ILE VAL THR PRO SER THR
SEQRES 3 B 371 ALA GLY ALA ALA GLU VAL THR PRO ALA ASP VAL ALA GLY
SEQRES 4 B 371 ASP THR ALA LEU SER THR ILE SER ASP SER ALA PRO ALA
SEQRES 5 B 371 ASP GLU ALA SER ALA PRO ARG TRP ARG ALA HIS VAL ASN
SEQRES 6 B 371 ALA ALA ASP GLU ARG VAL LYS GLU MET TRP ALA TYR SER
SEQRES 7 B 371 PRO SER MET ASP ARG ASN VAL PRO LEU VAL VAL ILE THR
SEQRES 8 B 371 ALA ASP GLU SER ALA GLY PRO ARG PRO VAL ILE TYR LEU
SEQRES 9 B 371 LEU ASN GLY GLY ASP GLY GLY GLU GLY ALA ALA ASN TRP
SEQRES 10 B 371 VAL MET GLN THR ASP VAL LEU ASP PHE TYR LEU GLU LYS
SEQRES 11 B 371 ASN VAL ASN VAL VAL ILE PRO MET GLU GLY LYS PHE SER
SEQRES 12 B 371 TYR TYR THR ASP TRP VAL GLU GLU ASN ALA SER LEU GLY
SEQRES 13 B 371 GLY LYS GLN MET TRP GLU THR PHE LEU VAL LYS GLU LEU
SEQRES 14 B 371 PRO GLY PRO LEU GLU GLU LYS LEU ASN THR ASP GLY GLN
SEQRES 15 B 371 ARG ALA ILE ALA GLY MET SER MET SER ALA THR THR SER
SEQRES 16 B 371 LEU LEU PHE PRO GLN HIS PHE PRO GLY PHE TYR ASP ALA
SEQRES 17 B 371 ALA ALA SER PHE SER GLY CYS ALA ALA THR SER SER LEU
SEQRES 18 B 371 LEU PRO TRP GLU TYR LEU LYS LEU THR LEU ASP ARG GLY
SEQRES 19 B 371 ASN ALA THR PRO GLU GLN MET TRP GLY PRO ARG GLY GLY
SEQRES 20 B 371 GLU TYR ASN ILE TYR ASN ASP ALA LEU ILE ASN SER ASP
SEQRES 21 B 371 LYS LEU ARG GLY THR GLU LEU TYR VAL SER ASN ALA SER
SEQRES 22 B 371 GLY LEU ALA GLY GLU TRP GLU SER VAL ASP SER PRO ARG
SEQRES 23 B 371 PHE GLU GLY LEU ASN GLN GLN VAL GLN SER ILE ALA MET
SEQRES 24 B 371 ALA GLU THR VAL VAL THR GLY GLY ILE ILE GLU ALA ALA
SEQRES 25 B 371 THR ASN LYS CYS THR HIS ASP LEU LYS ALA LYS LEU ASP
SEQRES 26 B 371 SER ALA GLY ILE PRO ALA ASP TRP ASN LEU ARG PRO THR
SEQRES 27 B 371 GLY THR HIS SER TRP GLY TRP TRP GLN ASP ASP LEU ARG
SEQRES 28 B 371 GLY SER TRP THR THR PHE ALA ARG ALA PHE GLU LEU GLU
SEQRES 29 B 371 ALA HIS HIS HIS HIS HIS HIS
SEQRES 1 C 371 MET LYS LEU LEU ARG ARG ILE ALA ALA PRO ALA ILE ALA
SEQRES 2 C 371 LEU GLY ILE ALA MET SER THR ILE VAL THR PRO SER THR
SEQRES 3 C 371 ALA GLY ALA ALA GLU VAL THR PRO ALA ASP VAL ALA GLY
SEQRES 4 C 371 ASP THR ALA LEU SER THR ILE SER ASP SER ALA PRO ALA
SEQRES 5 C 371 ASP GLU ALA SER ALA PRO ARG TRP ARG ALA HIS VAL ASN
SEQRES 6 C 371 ALA ALA ASP GLU ARG VAL LYS GLU MET TRP ALA TYR SER
SEQRES 7 C 371 PRO SER MET ASP ARG ASN VAL PRO LEU VAL VAL ILE THR
SEQRES 8 C 371 ALA ASP GLU SER ALA GLY PRO ARG PRO VAL ILE TYR LEU
SEQRES 9 C 371 LEU ASN GLY GLY ASP GLY GLY GLU GLY ALA ALA ASN TRP
SEQRES 10 C 371 VAL MET GLN THR ASP VAL LEU ASP PHE TYR LEU GLU LYS
SEQRES 11 C 371 ASN VAL ASN VAL VAL ILE PRO MET GLU GLY LYS PHE SER
SEQRES 12 C 371 TYR TYR THR ASP TRP VAL GLU GLU ASN ALA SER LEU GLY
SEQRES 13 C 371 GLY LYS GLN MET TRP GLU THR PHE LEU VAL LYS GLU LEU
SEQRES 14 C 371 PRO GLY PRO LEU GLU GLU LYS LEU ASN THR ASP GLY GLN
SEQRES 15 C 371 ARG ALA ILE ALA GLY MET SER MET SER ALA THR THR SER
SEQRES 16 C 371 LEU LEU PHE PRO GLN HIS PHE PRO GLY PHE TYR ASP ALA
SEQRES 17 C 371 ALA ALA SER PHE SER GLY CYS ALA ALA THR SER SER LEU
SEQRES 18 C 371 LEU PRO TRP GLU TYR LEU LYS LEU THR LEU ASP ARG GLY
SEQRES 19 C 371 ASN ALA THR PRO GLU GLN MET TRP GLY PRO ARG GLY GLY
SEQRES 20 C 371 GLU TYR ASN ILE TYR ASN ASP ALA LEU ILE ASN SER ASP
SEQRES 21 C 371 LYS LEU ARG GLY THR GLU LEU TYR VAL SER ASN ALA SER
SEQRES 22 C 371 GLY LEU ALA GLY GLU TRP GLU SER VAL ASP SER PRO ARG
SEQRES 23 C 371 PHE GLU GLY LEU ASN GLN GLN VAL GLN SER ILE ALA MET
SEQRES 24 C 371 ALA GLU THR VAL VAL THR GLY GLY ILE ILE GLU ALA ALA
SEQRES 25 C 371 THR ASN LYS CYS THR HIS ASP LEU LYS ALA LYS LEU ASP
SEQRES 26 C 371 SER ALA GLY ILE PRO ALA ASP TRP ASN LEU ARG PRO THR
SEQRES 27 C 371 GLY THR HIS SER TRP GLY TRP TRP GLN ASP ASP LEU ARG
SEQRES 28 C 371 GLY SER TRP THR THR PHE ALA ARG ALA PHE GLU LEU GLU
SEQRES 29 C 371 ALA HIS HIS HIS HIS HIS HIS
SEQRES 1 D 371 MET LYS LEU LEU ARG ARG ILE ALA ALA PRO ALA ILE ALA
SEQRES 2 D 371 LEU GLY ILE ALA MET SER THR ILE VAL THR PRO SER THR
SEQRES 3 D 371 ALA GLY ALA ALA GLU VAL THR PRO ALA ASP VAL ALA GLY
SEQRES 4 D 371 ASP THR ALA LEU SER THR ILE SER ASP SER ALA PRO ALA
SEQRES 5 D 371 ASP GLU ALA SER ALA PRO ARG TRP ARG ALA HIS VAL ASN
SEQRES 6 D 371 ALA ALA ASP GLU ARG VAL LYS GLU MET TRP ALA TYR SER
SEQRES 7 D 371 PRO SER MET ASP ARG ASN VAL PRO LEU VAL VAL ILE THR
SEQRES 8 D 371 ALA ASP GLU SER ALA GLY PRO ARG PRO VAL ILE TYR LEU
SEQRES 9 D 371 LEU ASN GLY GLY ASP GLY GLY GLU GLY ALA ALA ASN TRP
SEQRES 10 D 371 VAL MET GLN THR ASP VAL LEU ASP PHE TYR LEU GLU LYS
SEQRES 11 D 371 ASN VAL ASN VAL VAL ILE PRO MET GLU GLY LYS PHE SER
SEQRES 12 D 371 TYR TYR THR ASP TRP VAL GLU GLU ASN ALA SER LEU GLY
SEQRES 13 D 371 GLY LYS GLN MET TRP GLU THR PHE LEU VAL LYS GLU LEU
SEQRES 14 D 371 PRO GLY PRO LEU GLU GLU LYS LEU ASN THR ASP GLY GLN
SEQRES 15 D 371 ARG ALA ILE ALA GLY MET SER MET SER ALA THR THR SER
SEQRES 16 D 371 LEU LEU PHE PRO GLN HIS PHE PRO GLY PHE TYR ASP ALA
SEQRES 17 D 371 ALA ALA SER PHE SER GLY CYS ALA ALA THR SER SER LEU
SEQRES 18 D 371 LEU PRO TRP GLU TYR LEU LYS LEU THR LEU ASP ARG GLY
SEQRES 19 D 371 ASN ALA THR PRO GLU GLN MET TRP GLY PRO ARG GLY GLY
SEQRES 20 D 371 GLU TYR ASN ILE TYR ASN ASP ALA LEU ILE ASN SER ASP
SEQRES 21 D 371 LYS LEU ARG GLY THR GLU LEU TYR VAL SER ASN ALA SER
SEQRES 22 D 371 GLY LEU ALA GLY GLU TRP GLU SER VAL ASP SER PRO ARG
SEQRES 23 D 371 PHE GLU GLY LEU ASN GLN GLN VAL GLN SER ILE ALA MET
SEQRES 24 D 371 ALA GLU THR VAL VAL THR GLY GLY ILE ILE GLU ALA ALA
SEQRES 25 D 371 THR ASN LYS CYS THR HIS ASP LEU LYS ALA LYS LEU ASP
SEQRES 26 D 371 SER ALA GLY ILE PRO ALA ASP TRP ASN LEU ARG PRO THR
SEQRES 27 D 371 GLY THR HIS SER TRP GLY TRP TRP GLN ASP ASP LEU ARG
SEQRES 28 D 371 GLY SER TRP THR THR PHE ALA ARG ALA PHE GLU LEU GLU
SEQRES 29 D 371 ALA HIS HIS HIS HIS HIS HIS
HET MG D 401 1
HETNAM MG MAGNESIUM ION
FORMUL 5 MG MG 2+
FORMUL 6 HOH *978(H2 O)
HELIX 1 1 THR A 33 GLY A 39 1 7
HELIX 2 2 TRP A 60 ALA A 66 1 7
HELIX 3 3 ASN A 116 THR A 121 1 6
HELIX 4 4 ASP A 122 ASN A 131 1 10
HELIX 5 5 ASN A 152 GLY A 156 5 5
HELIX 6 6 MET A 160 LYS A 167 1 8
HELIX 7 7 LEU A 169 LEU A 177 1 9
HELIX 8 8 MET A 190 PHE A 202 1 13
HELIX 9 9 SER A 220 ARG A 233 1 14
HELIX 10 10 THR A 237 GLY A 243 1 7
HELIX 11 11 GLY A 247 ASN A 253 1 7
HELIX 12 12 ASN A 258 ARG A 263 5 6
HELIX 13 13 ALA A 272 TRP A 279 5 8
HELIX 14 14 GLY A 306 GLY A 328 1 23
HELIX 15 15 SER A 342 GLU A 362 1 21
HELIX 16 16 THR B 33 GLY B 39 1 7
HELIX 17 17 TRP B 60 ALA B 66 1 7
HELIX 18 18 ASN B 116 THR B 121 1 6
HELIX 19 19 ASP B 122 ASN B 131 1 10
HELIX 20 20 ASN B 152 GLY B 156 5 5
HELIX 21 21 MET B 160 LYS B 167 1 8
HELIX 22 22 LEU B 169 ASN B 178 1 10
HELIX 23 23 MET B 190 PHE B 202 1 13
HELIX 24 24 SER B 220 ARG B 233 1 14
HELIX 25 25 THR B 237 GLY B 243 1 7
HELIX 26 26 GLY B 247 ASN B 253 1 7
HELIX 27 27 ASN B 258 ARG B 263 5 6
HELIX 28 28 ALA B 272 GLU B 280 5 9
HELIX 29 29 GLY B 306 GLY B 328 1 23
HELIX 30 30 SER B 342 GLU B 362 1 21
HELIX 31 31 THR C 33 GLY C 39 1 7
HELIX 32 32 TRP C 60 ALA C 67 1 8
HELIX 33 33 ASP C 93 GLY C 97 5 5
HELIX 34 34 ASN C 116 THR C 121 1 6
HELIX 35 35 ASP C 122 GLU C 129 1 8
HELIX 36 36 ASN C 152 GLY C 156 5 5
HELIX 37 37 MET C 160 LYS C 167 1 8
HELIX 38 38 LEU C 169 ASN C 178 1 10
HELIX 39 39 SER C 189 PHE C 202 1 14
HELIX 40 40 SER C 220 ASP C 232 1 13
HELIX 41 41 ARG C 233 ASN C 235 5 3
HELIX 42 42 THR C 237 GLY C 243 1 7
HELIX 43 43 GLY C 247 ASN C 253 1 7
HELIX 44 44 ASN C 258 ARG C 263 5 6
HELIX 45 45 THR C 302 GLY C 328 1 27
HELIX 46 46 SER C 342 PHE C 361 1 20
HELIX 47 47 THR D 33 GLY D 39 1 7
HELIX 48 48 TRP D 60 ALA D 67 1 8
HELIX 49 49 ASP D 93 GLY D 97 5 5
HELIX 50 50 ASN D 116 THR D 121 1 6
HELIX 51 51 ASP D 122 GLU D 129 1 8
HELIX 52 52 ASN D 152 GLY D 156 5 5
HELIX 53 53 MET D 160 LYS D 167 1 8
HELIX 54 54 LEU D 169 ASN D 178 1 10
HELIX 55 55 SER D 189 PHE D 202 1 14
HELIX 56 56 SER D 220 ASP D 232 1 13
HELIX 57 57 ARG D 233 ASN D 235 5 3
HELIX 58 58 THR D 237 GLY D 243 1 7
HELIX 59 59 GLY D 247 ASN D 253 1 7
HELIX 60 60 ASN D 258 ARG D 263 5 6
HELIX 61 61 THR D 302 GLY D 328 1 27
HELIX 62 62 SER D 342 PHE D 361 1 20
SHEET 1 A 9 THR A 45 SER A 47 0
SHEET 2 A 9 VAL A 71 SER A 78 -1 O TRP A 75 N SER A 47
SHEET 3 A 9 ARG A 83 ILE A 90 -1 O ARG A 83 N SER A 78
SHEET 4 A 9 ASN A 133 PRO A 137 -1 O ILE A 136 N VAL A 88
SHEET 5 A 9 VAL A 101 LEU A 105 1 N ILE A 102 O VAL A 135
SHEET 6 A 9 ARG A 183 MET A 188 1 O ALA A 186 N LEU A 105
SHEET 7 A 9 ALA A 208 PHE A 212 1 O PHE A 212 N GLY A 187
SHEET 8 A 9 GLU A 266 SER A 270 1 O TYR A 268 N SER A 211
SHEET 9 A 9 ASP A 332 ASN A 334 1 O ASP A 332 N LEU A 267
SHEET 1 B 9 THR B 45 SER B 47 0
SHEET 2 B 9 VAL B 71 SER B 78 -1 O TRP B 75 N SER B 47
SHEET 3 B 9 ARG B 83 ILE B 90 -1 O VAL B 85 N ALA B 76
SHEET 4 B 9 ASN B 133 PRO B 137 -1 O ILE B 136 N VAL B 88
SHEET 5 B 9 ARG B 99 LEU B 105 1 N PRO B 100 O ASN B 133
SHEET 6 B 9 THR B 179 MET B 188 1 O ALA B 186 N LEU B 105
SHEET 7 B 9 ALA B 208 PHE B 212 1 O PHE B 212 N GLY B 187
SHEET 8 B 9 GLU B 266 SER B 270 1 O TYR B 268 N SER B 211
SHEET 9 B 9 ASP B 332 ASN B 334 1 O ASP B 332 N LEU B 267
SHEET 1 C 9 THR C 45 SER C 47 0
SHEET 2 C 9 VAL C 71 SER C 78 -1 O TRP C 75 N SER C 47
SHEET 3 C 9 ARG C 83 ILE C 90 -1 O LEU C 87 N MET C 74
SHEET 4 C 9 ASN C 133 PRO C 137 -1 O ILE C 136 N VAL C 88
SHEET 5 C 9 VAL C 101 LEU C 105 1 N ILE C 102 O VAL C 135
SHEET 6 C 9 ARG C 183 MET C 188 1 O ALA C 184 N TYR C 103
SHEET 7 C 9 ALA C 208 PHE C 212 1 O PHE C 212 N GLY C 187
SHEET 8 C 9 GLU C 266 SER C 270 1 O GLU C 266 N ALA C 209
SHEET 9 C 9 ASP C 332 ASN C 334 1 O ASP C 332 N VAL C 269
SHEET 1 D 9 THR D 45 SER D 47 0
SHEET 2 D 9 VAL D 71 SER D 78 -1 O TRP D 75 N SER D 47
SHEET 3 D 9 ARG D 83 ILE D 90 -1 O LEU D 87 N MET D 74
SHEET 4 D 9 ASN D 133 PRO D 137 -1 O VAL D 134 N ILE D 90
SHEET 5 D 9 VAL D 101 LEU D 105 1 N ILE D 102 O VAL D 135
SHEET 6 D 9 ARG D 183 MET D 188 1 O ALA D 186 N LEU D 105
SHEET 7 D 9 ALA D 208 PHE D 212 1 O PHE D 212 N GLY D 187
SHEET 8 D 9 GLU D 266 SER D 270 1 O GLU D 266 N ALA D 209
SHEET 9 D 9 ASP D 332 ASN D 334 1 O ASP D 332 N LEU D 267
SSBOND 1 CYS A 215 CYS A 316 1555 1555 2.06
SSBOND 2 CYS B 215 CYS B 316 1555 1555 2.05
SSBOND 3 CYS C 215 CYS C 316 1555 1555 2.05
SSBOND 4 CYS D 215 CYS D 316 1555 1555 2.05
LINK OE2 GLU D 139 MG MG D 401 1555 1555 2.13
LINK MG MG D 401 O HOH D 721 1555 1555 2.00
LINK MG MG D 401 O HOH D 508 1555 1555 2.05
LINK MG MG D 401 O HOH D 585 1555 1555 2.10
LINK MG MG D 401 O HOH D 686 1555 1555 2.16
LINK MG MG D 401 O HOH D 572 1555 1555 2.19
SITE 1 AC1 6 GLU D 139 HOH D 508 HOH D 572 HOH D 585
SITE 2 AC1 6 HOH D 686 HOH D 721
CRYST1 85.804 190.688 78.497 90.00 90.00 90.00 P 21 21 2 16
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 0.011654 0.000000 0.000000 0.00000
SCALE2 0.000000 0.005244 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012739 0.00000
TER 2417 GLU A 364
TER 4812 LEU B 363
TER 7199 GLU C 364
TER 9565 LEU D 363
MASTER 632 0 1 62 36 0 2 610474 4 16 116
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