HEADER TRANSFERASE 03-DEC-10 3PTY
TITLE CRYSTAL STRUCTURE OF THE C-TERMINAL EXTRACELLULAR DOMAIN OF
TITLE 2 MYCOBACTERIUM TUBERCULOSIS EMBC
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ARABINOSYLTRANSFERASE C;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: C-TERMINAL DOMAIN (UNP RESIDUES 719-1094);
COMPND 5 SYNONYM: ARABINOSYLTRANSFERASE EMBC;
COMPND 6 EC: 2.4.2.-;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM TUBERCULOSIS;
SOURCE 3 ORGANISM_TAXID: 1773;
SOURCE 4 GENE: EMBC, MT3900, MTCY13D12.27, RV3793;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: C41(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET23B
KEYWDS BETA-SANDWICH, CARBOHYDRATE BINDING, CARBOHYDRATE, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR L.J.ALDERWICK,G.S.BESRA,K.FUTTERER
REVDAT 3 29-JUL-20 3PTY 1 REMARK SEQADV LINK SITE
REVDAT 2 23-MAR-11 3PTY 1 JRNL
REVDAT 1 15-DEC-10 3PTY 0
JRNL AUTH L.J.ALDERWICK,G.S.LLOYD,H.GHADBANE,J.W.MAY,A.BHATT,
JRNL AUTH 2 L.EGGELING,K.FUTTERER,G.S.BESRA
JRNL TITL THE C-TERMINAL DOMAIN OF THE ARABINOSYLTRANSFERASE
JRNL TITL 2 MYCOBACTERIUM TUBERCULOSIS EMBC IS A LECTIN-LIKE
JRNL TITL 3 CARBOHYDRATE BINDING MODULE.
JRNL REF PLOS PATHOG. V. 7 01299 2011
JRNL REFN ISSN 1553-7366
JRNL PMID 21383969
JRNL DOI 10.1371/JOURNAL.PPAT.1001299
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE)
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) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 43.28
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.380
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 43081
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.188
REMARK 3 R VALUE (WORKING SET) : 0.187
REMARK 3 FREE R VALUE : 0.207
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.050
REMARK 3 FREE R VALUE TEST SET COUNT : 4348
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 43.2921 - 6.2086 1.00 2750 126 0.1937 0.1951
REMARK 3 2 6.2086 - 4.9302 1.00 2719 171 0.1759 0.1801
REMARK 3 3 4.9302 - 4.3076 1.00 2711 151 0.1460 0.1629
REMARK 3 4 4.3076 - 3.9140 1.00 2707 144 0.1641 0.1697
REMARK 3 5 3.9140 - 3.6337 1.00 2751 160 0.1782 0.1745
REMARK 3 6 3.6337 - 3.4195 1.00 2715 138 0.1876 0.2430
REMARK 3 7 3.4195 - 3.2483 1.00 2728 150 0.1914 0.2099
REMARK 3 8 3.2483 - 3.1070 1.00 2752 133 0.1943 0.2317
REMARK 3 9 3.1070 - 2.9874 1.00 2696 163 0.2036 0.2302
REMARK 3 10 2.9874 - 2.8843 1.00 2725 148 0.2008 0.2226
REMARK 3 11 2.8843 - 2.7941 1.00 2731 149 0.1809 0.2058
REMARK 3 12 2.7941 - 2.7143 1.00 2755 132 0.1816 0.2040
REMARK 3 13 2.7143 - 2.6428 1.00 2734 126 0.1845 0.2297
REMARK 3 14 2.6428 - 2.5784 1.00 2704 152 0.1812 0.1940
REMARK 3 15 2.5784 - 2.5198 1.00 2702 168 0.1943 0.2290
REMARK 3 16 2.5198 - 2.4661 1.00 2760 169 0.1984 0.2220
REMARK 3 17 2.4661 - 2.4168 1.00 2703 134 0.1883 0.2105
REMARK 3 18 2.4168 - 2.3712 1.00 2725 157 0.1769 0.1556
REMARK 3 19 2.3712 - 2.3289 1.00 2745 111 0.1714 0.1933
REMARK 3 20 2.3289 - 2.2894 1.00 2748 136 0.1737 0.1736
REMARK 3 21 2.2894 - 2.2525 1.00 2742 146 0.1762 0.2008
REMARK 3 22 2.2525 - 2.2178 1.00 2732 115 0.1741 0.2195
REMARK 3 23 2.2178 - 2.1852 1.00 2666 170 0.1745 0.2167
REMARK 3 24 2.1852 - 2.1544 1.00 2737 160 0.1828 0.1870
REMARK 3 25 2.1544 - 2.1253 1.00 2744 149 0.1875 0.2295
REMARK 3 26 2.1253 - 2.0977 1.00 2708 161 0.1971 0.2368
REMARK 3 27 2.0977 - 2.0715 1.00 2761 104 0.2075 0.2451
REMARK 3 28 2.0715 - 2.0465 1.00 2697 149 0.2116 0.2501
REMARK 3 29 2.0465 - 2.0227 1.00 2746 142 0.2163 0.2784
REMARK 3 30 2.0227 - 2.0000 1.00 2721 134 0.2266 0.2681
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 : 0.37
REMARK 3 B_SOL : 51.79
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.250
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : NULL
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 27.90
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.07580
REMARK 3 B22 (A**2) : -1.07580
REMARK 3 B33 (A**2) : 2.15170
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
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 : 1.052 3013
REMARK 3 CHIRALITY : 0.074 341
REMARK 3 PLANARITY : 0.005 395
REMARK 3 DIHEDRAL : 17.683 780
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 1
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN A
REMARK 3 ORIGIN FOR THE GROUP (A): 80.7989 5.1276 20.1224
REMARK 3 T TENSOR
REMARK 3 T11: 0.1643 T22: 0.1556
REMARK 3 T33: 0.1717 T12: -0.0117
REMARK 3 T13: 0.0128 T23: -0.0171
REMARK 3 L TENSOR
REMARK 3 L11: 0.4919 L22: 0.5821
REMARK 3 L33: 0.8765 L12: -0.2945
REMARK 3 L13: -0.6492 L23: 0.3292
REMARK 3 S TENSOR
REMARK 3 S11: -0.0239 S12: -0.0248 S13: -0.0436
REMARK 3 S21: 0.0213 S22: -0.0174 S23: 0.0812
REMARK 3 S31: 0.0420 S32: 0.0690 S33: 0.0000
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 3PTY COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-DEC-10.
REMARK 100 THE DEPOSITION ID IS D_1000062807.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-MAY-06
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 4.4
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID23-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9763,0.9797,0.9799
REMARK 200 MONOCHROMATOR : SILICON(111)
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 : 45942
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 46.900
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 14.40
REMARK 200 R MERGE (I) : 0.07300
REMARK 200 R SYM (I) : 0.07300
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 27.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.11
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 14.50
REMARK 200 R MERGE FOR SHELL (I) : 0.56400
REMARK 200 R SYM FOR SHELL (I) : 0.56400
REMARK 200 <I/SIGMA(I)> FOR SHELL : 5.300
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: MAD
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD
REMARK 200 SOFTWARE USED: SHELXDE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 67.42
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.78
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M SODIUM ACETATE, 0.08 M AMMONIUM
REMARK 280 PHOSPHATE, PH 4.4, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE
REMARK 280 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 65 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+1/6
REMARK 290 6555 X-Y,X,Z+5/6
REMARK 290 7555 Y,X,-Z+2/3
REMARK 290 8555 X-Y,-Y,-Z
REMARK 290 9555 -X,-X+Y,-Z+1/3
REMARK 290 10555 -Y,-X,-Z+1/6
REMARK 290 11555 -X+Y,Y,-Z+1/2
REMARK 290 12555 X,X-Y,-Z+5/6
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 91.15333
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 45.57667
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 68.36500
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 22.78833
REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 113.94167
REMARK 290 SMTRY1 7 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 7 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 91.15333
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 9 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 9 0.000000 0.000000 -1.000000 45.57667
REMARK 290 SMTRY1 10 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 10 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 22.78833
REMARK 290 SMTRY1 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 11 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 68.36500
REMARK 290 SMTRY1 12 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 12 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 113.94167
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 300 REMARK: DIMERIZATION MAY NOT OCCUR IN THE CONTEXT OF THE FULL
REMARK 300 LENGTH PROTEIN
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3230 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 24620 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -56.0 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 BIOMT1 2 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 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 GLU A 719
REMARK 465 VAL A 720
REMARK 465 VAL A 721
REMARK 465 SER A 722
REMARK 465 LEU A 723
REMARK 465 THR A 724
REMARK 465 GLN A 725
REMARK 465 ALA A 726
REMARK 465 MET A 727
REMARK 465 ILE A 728
REMARK 465 SER A 729
REMARK 465 GLN A 730
REMARK 465 TYR A 731
REMARK 465 PRO A 732
REMARK 465 ALA A 733
REMARK 465 TRP A 734
REMARK 465 THR A 795
REMARK 465 ALA A 796
REMARK 465 ASP A 797
REMARK 465 PRO A 798
REMARK 465 VAL A 799
REMARK 465 MET A 800
REMARK 465 GLU A 801
REMARK 465 ARG A 802
REMARK 465 PRO A 803
REMARK 465 GLY A 804
REMARK 465 ASP A 805
REMARK 465 ARG A 806
REMARK 465 SER A 807
REMARK 465 PHE A 808
REMARK 465 LEU A 809
REMARK 465 ASN A 810
REMARK 465 ASP A 811
REMARK 465 ASP A 812
REMARK 465 GLY A 813
REMARK 465 LEU A 814
REMARK 465 ILE A 815
REMARK 465 THR A 816
REMARK 465 GLY A 817
REMARK 465 SER A 818
REMARK 465 GLU A 819
REMARK 465 PRO A 820
REMARK 465 GLY A 821
REMARK 465 THR A 822
REMARK 465 GLU A 823
REMARK 465 GLY A 824
REMARK 465 PHE A 1016
REMARK 465 GLY A 1017
REMARK 465 ALA A 1018
REMARK 465 GLU A 1019
REMARK 465 ALA A 1020
REMARK 465 ASN A 1021
REMARK 465 SER A 1022
REMARK 465 PRO A 1023
REMARK 465 VAL A 1024
REMARK 465 MET A 1025
REMARK 465 ASP A 1026
REMARK 465 HIS A 1027
REMARK 465 ASN A 1028
REMARK 465 GLY A 1029
REMARK 465 GLY A 1030
REMARK 465 GLY A 1031
REMARK 465 PRO A 1032
REMARK 465 LEU A 1033
REMARK 465 GLY A 1034
REMARK 465 PRO A 1068
REMARK 465 ASP A 1069
REMARK 465 ALA A 1070
REMARK 465 GLN A 1071
REMARK 465 PRO A 1072
REMARK 465 ALA A 1073
REMARK 465 ASP A 1074
REMARK 465 LEU A 1075
REMARK 465 ASN A 1076
REMARK 465 LEU A 1077
REMARK 465 GLY A 1078
REMARK 465 THR A 1079
REMARK 465 VAL A 1080
REMARK 465 THR A 1081
REMARK 465 ARG A 1082
REMARK 465 SER A 1083
REMARK 465 GLY A 1084
REMARK 465 LEU A 1085
REMARK 465 TRP A 1086
REMARK 465 SER A 1087
REMARK 465 PRO A 1088
REMARK 465 ALA A 1089
REMARK 465 PRO A 1090
REMARK 465 LEU A 1091
REMARK 465 ARG A 1092
REMARK 465 ARG A 1093
REMARK 465 GLY A 1094
REMARK 465 ALA A 1095
REMARK 465 PRO A 1096
REMARK 465 PRO A 1097
REMARK 465 PRO A 1098
REMARK 465 PRO A 1099
REMARK 465 PRO A 1100
REMARK 465 LEU A 1101
REMARK 465 GLY A 1102
REMARK 465 ARG A 1103
REMARK 465 ASP A 1104
REMARK 465 PRO A 1105
REMARK 465 ASN A 1106
REMARK 465 SER A 1107
REMARK 465 SER A 1108
REMARK 465 SER A 1109
REMARK 465 VAL A 1110
REMARK 465 ASP A 1111
REMARK 465 LYS A 1112
REMARK 465 LEU A 1113
REMARK 465 ALA A 1114
REMARK 465 ALA A 1115
REMARK 465 ALA A 1116
REMARK 465 LEU A 1117
REMARK 465 GLU A 1118
REMARK 465 HIS A 1119
REMARK 465 HIS A 1120
REMARK 465 HIS A 1121
REMARK 465 HIS A 1122
REMARK 465 HIS A 1123
REMARK 465 HIS A 1124
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 738 CD NE CZ NH1 NH2
REMARK 470 ASP A 793 CG OD1 OD2
REMARK 470 ASN A 874 CG OD1 ND2
REMARK 470 GLU A 875 CG CD OE1 OE2
REMARK 470 ARG A 877 CG CD NE CZ NH1 NH2
REMARK 470 GLN A 955 CG CD OE1 NE2
REMARK 470 LYS A1008 NZ
REMARK 470 ARG A1015 CG CD NE CZ NH1 NH2
REMARK 470 LEU A1038 CG CD1 CD2
REMARK 470 LEU A1039 CG CD1 CD2
REMARK 470 TYR A1066 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 TYR A1067 CG CD1 CD2 CE1 CE2 CZ OH
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 881 48.76 -83.24
REMARK 500 LEU A1038 3.50 137.16
REMARK 500 LEU A1039 69.99 65.79
REMARK 500 ASP A1052 98.71 -160.48
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 CA A1125 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A 33 O
REMARK 620 2 HOH A 39 O 102.3
REMARK 620 3 HOH A 67 O 91.6 74.8
REMARK 620 4 ASP A 949 OD2 81.8 152.3 77.8
REMARK 620 5 ASP A 949 OD1 79.6 157.8 127.4 49.7
REMARK 620 6 ASP A 951 O 87.9 76.6 150.6 131.0 81.3
REMARK 620 7 HIS A 956 O 168.4 89.0 89.2 87.1 90.7 97.0
REMARK 620 N 1 2 3 4 5 6
DBREF 3PTY A 719 1094 UNP P72059 EMBC_MYCTU 719 1094
SEQADV 3PTY ALA A 1095 UNP P72059 EXPRESSION TAG
SEQADV 3PTY PRO A 1096 UNP P72059 EXPRESSION TAG
SEQADV 3PTY PRO A 1097 UNP P72059 EXPRESSION TAG
SEQADV 3PTY PRO A 1098 UNP P72059 EXPRESSION TAG
SEQADV 3PTY PRO A 1099 UNP P72059 EXPRESSION TAG
SEQADV 3PTY PRO A 1100 UNP P72059 EXPRESSION TAG
SEQADV 3PTY LEU A 1101 UNP P72059 EXPRESSION TAG
SEQADV 3PTY GLY A 1102 UNP P72059 EXPRESSION TAG
SEQADV 3PTY ARG A 1103 UNP P72059 EXPRESSION TAG
SEQADV 3PTY ASP A 1104 UNP P72059 EXPRESSION TAG
SEQADV 3PTY PRO A 1105 UNP P72059 EXPRESSION TAG
SEQADV 3PTY ASN A 1106 UNP P72059 EXPRESSION TAG
SEQADV 3PTY SER A 1107 UNP P72059 EXPRESSION TAG
SEQADV 3PTY SER A 1108 UNP P72059 EXPRESSION TAG
SEQADV 3PTY SER A 1109 UNP P72059 EXPRESSION TAG
SEQADV 3PTY VAL A 1110 UNP P72059 EXPRESSION TAG
SEQADV 3PTY ASP A 1111 UNP P72059 EXPRESSION TAG
SEQADV 3PTY LYS A 1112 UNP P72059 EXPRESSION TAG
SEQADV 3PTY LEU A 1113 UNP P72059 EXPRESSION TAG
SEQADV 3PTY ALA A 1114 UNP P72059 EXPRESSION TAG
SEQADV 3PTY ALA A 1115 UNP P72059 EXPRESSION TAG
SEQADV 3PTY ALA A 1116 UNP P72059 EXPRESSION TAG
SEQADV 3PTY LEU A 1117 UNP P72059 EXPRESSION TAG
SEQADV 3PTY GLU A 1118 UNP P72059 EXPRESSION TAG
SEQADV 3PTY HIS A 1119 UNP P72059 EXPRESSION TAG
SEQADV 3PTY HIS A 1120 UNP P72059 EXPRESSION TAG
SEQADV 3PTY HIS A 1121 UNP P72059 EXPRESSION TAG
SEQADV 3PTY HIS A 1122 UNP P72059 EXPRESSION TAG
SEQADV 3PTY HIS A 1123 UNP P72059 EXPRESSION TAG
SEQADV 3PTY HIS A 1124 UNP P72059 EXPRESSION TAG
SEQRES 1 A 406 GLU VAL VAL SER LEU THR GLN ALA MET ILE SER GLN TYR
SEQRES 2 A 406 PRO ALA TRP SER VAL GLY ARG SER ASN LEU GLN ALA LEU
SEQRES 3 A 406 ALA GLY LYS THR CYS GLY LEU ALA GLU ASP VAL LEU VAL
SEQRES 4 A 406 GLU LEU ASP PRO ASN ALA GLY MET LEU ALA PRO VAL THR
SEQRES 5 A 406 ALA PRO LEU ALA ASP ALA LEU GLY ALA GLY LEU SER GLU
SEQRES 6 A 406 ALA PHE THR PRO ASN GLY ILE PRO ALA ASP VAL THR ALA
SEQRES 7 A 406 ASP PRO VAL MET GLU ARG PRO GLY ASP ARG SER PHE LEU
SEQRES 8 A 406 ASN ASP ASP GLY LEU ILE THR GLY SER GLU PRO GLY THR
SEQRES 9 A 406 GLU GLY GLY THR THR ALA ALA PRO GLY ILE ASN GLY SER
SEQRES 10 A 406 ARG ALA ARG LEU PRO TYR ASN LEU ASP PRO ALA ARG THR
SEQRES 11 A 406 PRO VAL LEU GLY SER TRP ARG ALA GLY VAL GLN VAL PRO
SEQRES 12 A 406 ALA MET LEU ARG SER GLY TRP TYR ARG LEU PRO THR ASN
SEQRES 13 A 406 GLU GLN ARG ASP ARG ALA PRO LEU LEU VAL VAL THR ALA
SEQRES 14 A 406 ALA GLY ARG PHE ASP SER ARG GLU VAL ARG LEU GLN TRP
SEQRES 15 A 406 ALA THR ASP GLU GLN ALA ALA ALA GLY HIS HIS GLY GLY
SEQRES 16 A 406 SER MET GLU PHE ALA ASP VAL GLY ALA ALA PRO ALA TRP
SEQRES 17 A 406 ARG ASN LEU ARG ALA PRO LEU SER ALA ILE PRO SER THR
SEQRES 18 A 406 ALA THR GLN VAL ARG LEU VAL ALA ASP ASP GLN ASP LEU
SEQRES 19 A 406 ALA PRO GLN HIS TRP ILE ALA LEU THR PRO PRO ARG ILE
SEQRES 20 A 406 PRO ARG VAL ARG THR LEU GLN ASN VAL VAL GLY ALA ALA
SEQRES 21 A 406 ASP PRO VAL PHE LEU ASP TRP LEU VAL GLY LEU ALA PHE
SEQRES 22 A 406 PRO CYS GLN ARG PRO PHE GLY HIS GLN TYR GLY VAL ASP
SEQRES 23 A 406 GLU THR PRO LYS TRP ARG ILE LEU PRO ASP ARG PHE GLY
SEQRES 24 A 406 ALA GLU ALA ASN SER PRO VAL MET ASP HIS ASN GLY GLY
SEQRES 25 A 406 GLY PRO LEU GLY ILE THR GLU LEU LEU MET ARG ALA THR
SEQRES 26 A 406 THR VAL ALA SER TYR LEU LYS ASP ASP TRP PHE ARG ASP
SEQRES 27 A 406 TRP GLY ALA LEU GLN ARG LEU THR PRO TYR TYR PRO ASP
SEQRES 28 A 406 ALA GLN PRO ALA ASP LEU ASN LEU GLY THR VAL THR ARG
SEQRES 29 A 406 SER GLY LEU TRP SER PRO ALA PRO LEU ARG ARG GLY ALA
SEQRES 30 A 406 PRO PRO PRO PRO PRO LEU GLY ARG ASP PRO ASN SER SER
SEQRES 31 A 406 SER VAL ASP LYS LEU ALA ALA ALA LEU GLU HIS HIS HIS
SEQRES 32 A 406 HIS HIS HIS
HET AFO A 1 18
HET CA A1125 1
HET PO4 A 2 5
HETNAM AFO OCTYL ALPHA-D-ARABINOFURANOSIDE
HETNAM CA CALCIUM ION
HETNAM PO4 PHOSPHATE ION
FORMUL 2 AFO C13 H26 O5
FORMUL 3 CA CA 2+
FORMUL 4 PO4 O4 P 3-
FORMUL 5 HOH *113(H2 O)
HELIX 1 1 SER A 735 LYS A 747 1 13
HELIX 2 2 CYS A 749 GLU A 753 5 5
HELIX 3 3 ASP A 760 MET A 765 5 6
HELIX 4 4 PRO A 772 LEU A 777 1 6
HELIX 5 5 ASP A 844 THR A 848 5 5
HELIX 6 6 ASP A 892 ARG A 894 5 3
HELIX 7 7 THR A 902 ALA A 908 1 7
HELIX 8 8 SER A 934 ILE A 936 5 3
HELIX 9 9 LEU A 971 GLY A 976 1 6
HELIX 10 10 ASP A 984 LEU A 989 1 6
HELIX 11 11 HIS A 999 VAL A 1003 5 5
SHEET 1 A 7 ARG A 969 THR A 970 0
SHEET 2 A 7 VAL A 755 GLU A 758 -1 N VAL A 757 O ARG A 969
SHEET 3 A 7 MET A1040 LEU A1049 -1 O TYR A1048 N LEU A 756
SHEET 4 A 7 ALA A1059 PRO A1065 -1 O THR A1064 N ARG A1041
SHEET 5 A 7 TRP A1009 LEU A1012 -1 N ARG A1010 O GLN A1061
SHEET 6 A 7 PRO A 980 PHE A 982 1 N PHE A 982 O TRP A1009
SHEET 7 A 7 ARG A 995 PRO A 996 1 O ARG A 995 N VAL A 981
SHEET 1 B 4 LEU A 781 GLU A 783 0
SHEET 2 B 4 ALA A 862 ARG A 865 -1 O MET A 863 N GLU A 783
SHEET 3 B 4 GLN A 942 ASP A 949 -1 O ASP A 949 N ALA A 862
SHEET 4 B 4 TYR A 869 ARG A 870 -1 N TYR A 869 O VAL A 943
SHEET 1 C 5 LEU A 781 GLU A 783 0
SHEET 2 C 5 ALA A 862 ARG A 865 -1 O MET A 863 N GLU A 783
SHEET 3 C 5 GLN A 942 ASP A 949 -1 O ASP A 949 N ALA A 862
SHEET 4 C 5 VAL A 896 ALA A 901 -1 N ARG A 897 O VAL A 946
SHEET 5 C 5 GLY A 913 GLU A 916 -1 O MET A 915 N LEU A 898
SHEET 1 D 5 LEU A 851 GLY A 852 0
SHEET 2 D 5 ILE A 958 LEU A 960 -1 O LEU A 960 N LEU A 851
SHEET 3 D 5 LEU A 882 GLY A 889 -1 N ALA A 888 O ALA A 959
SHEET 4 D 5 ARG A 927 PRO A 932 -1 O ALA A 931 N LEU A 883
SHEET 5 D 5 ALA A 918 VAL A 920 -1 N ALA A 918 O ARG A 930
SSBOND 1 CYS A 749 CYS A 993 1555 1555 2.07
LINK O HOH A 33 CA CA A1125 1555 1555 2.50
LINK O HOH A 39 CA CA A1125 1555 1555 2.56
LINK O HOH A 67 CA CA A1125 1555 1555 2.63
LINK OD2 ASP A 949 CA CA A1125 1555 1555 2.61
LINK OD1 ASP A 949 CA CA A1125 1555 1555 2.63
LINK O ASP A 951 CA CA A1125 1555 1555 2.49
LINK O HIS A 956 CA CA A1125 1555 1555 2.40
CISPEP 1 ALA A 923 PRO A 924 0 4.61
CISPEP 2 ILE A 1035 THR A 1036 0 -19.35
CRYST1 129.130 129.130 136.730 90.00 90.00 120.00 P 65 2 2 12
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 0.007744 0.004471 0.000000 0.00000
SCALE2 0.000000 0.008942 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007314 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
