HEADER UNKNOWN FUNCTION 09-JUL-14 4TYZ
TITLE CRYSTAL STRUCTURE OF THE C-TERMINAL DOMAIN OF AN UNKNOWN PROTEIN FROM
TITLE 2 LEISHMANIA INFANTUM
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: UNCHARACTERIZED PROTEIN;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: C-TERMINAL DOMAIN (UNP RESIDUES 621-730);
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: LEISHMANIA INFANTUM;
SOURCE 3 ORGANISM_TAXID: 5671;
SOURCE 4 GENE: LINJ_30_2720;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: LEINA.18749.A.B1
KEYWDS SSGCID, LEISHMANIA INFANTUM, STRUCTURAL GENOMICS, SEATTLE STRUCTURAL
KEYWDS 2 GENOMICS CENTER FOR INFECTIOUS DISEASE, UNKNOWN FUNCTION
EXPDTA X-RAY DIFFRACTION
AUTHOR SEATTLE STRUCTURAL GENOMICS CENTER FOR INFECTIOUS DISEASE (SSGCID)
REVDAT 4 27-DEC-23 4TYZ 1 REMARK
REVDAT 3 22-NOV-17 4TYZ 1 SOURCE JRNL REMARK
REVDAT 2 22-OCT-14 4TYZ 1 JRNL
REVDAT 1 06-AUG-14 4TYZ 0
JRNL AUTH E.FISCHER,D.M.DRANOW,J.ABENDROTH,D.LORIMER,T.E.EDWARDS,
JRNL AUTH 2 SEATTLE STRUCTURAL GENOMICS CENTER FOR INFECTIOUS DISEASE
JRNL AUTH 3 (SSGCID)
JRNL TITL CRYSTAL STRUCTURE OF THE C-TERMINAL DOMAIN OF AN UNKNOWN
JRNL TITL 2 PROTEIN FROM LEISHMANIA INFANTUM
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: DEV_1738)
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) : 1.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 33.75
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.360
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 3 NUMBER OF REFLECTIONS : 36479
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.160
REMARK 3 R VALUE (WORKING SET) : 0.159
REMARK 3 FREE R VALUE : 0.186
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.230
REMARK 3 FREE R VALUE TEST SET COUNT : 1909
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 33.7596 - 3.8545 0.97 2590 143 0.1543 0.1699
REMARK 3 2 3.8545 - 3.0601 0.99 2539 120 0.1434 0.1645
REMARK 3 3 3.0601 - 2.6734 0.99 2469 140 0.1640 0.2025
REMARK 3 4 2.6734 - 2.4291 1.00 2480 147 0.1669 0.2169
REMARK 3 5 2.4291 - 2.2550 1.00 2449 161 0.1614 0.1826
REMARK 3 6 2.2550 - 2.1221 1.00 2444 147 0.1561 0.1722
REMARK 3 7 2.1221 - 2.0158 1.00 2468 146 0.1489 0.2078
REMARK 3 8 2.0158 - 1.9281 1.00 2460 121 0.1535 0.1685
REMARK 3 9 1.9281 - 1.8539 1.00 2446 134 0.1541 0.1743
REMARK 3 10 1.8539 - 1.7899 1.00 2455 122 0.1616 0.1780
REMARK 3 11 1.7899 - 1.7339 1.00 2444 121 0.1641 0.1832
REMARK 3 12 1.7339 - 1.6844 1.00 2456 144 0.1768 0.2223
REMARK 3 13 1.6844 - 1.6400 1.00 2420 136 0.1892 0.2322
REMARK 3 14 1.6400 - 1.6000 1.00 2450 127 0.2047 0.2301
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) : 0.130
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 17.170
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 13.71
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 19.87
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 : 0.007 1886
REMARK 3 ANGLE : 1.022 2580
REMARK 3 CHIRALITY : 0.042 291
REMARK 3 PLANARITY : 0.005 326
REMARK 3 DIHEDRAL : 13.559 685
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 9
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 621 THROUGH 673 )
REMARK 3 ORIGIN FOR THE GROUP (A): -38.0208 28.1925 21.3668
REMARK 3 T TENSOR
REMARK 3 T11: 0.1178 T22: 0.1030
REMARK 3 T33: 0.1468 T12: 0.0480
REMARK 3 T13: 0.0508 T23: 0.0331
REMARK 3 L TENSOR
REMARK 3 L11: 0.5553 L22: 0.6812
REMARK 3 L33: 1.6265 L12: 0.0931
REMARK 3 L13: -0.1667 L23: -0.5854
REMARK 3 S TENSOR
REMARK 3 S11: 0.0731 S12: 0.1115 S13: -0.0242
REMARK 3 S21: -0.1415 S22: -0.1002 S23: -0.1698
REMARK 3 S31: 0.0849 S32: 0.1029 S33: -0.0013
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 674 THROUGH 687 )
REMARK 3 ORIGIN FOR THE GROUP (A): -46.0205 35.7389 26.8474
REMARK 3 T TENSOR
REMARK 3 T11: 0.1110 T22: 0.1081
REMARK 3 T33: 0.0900 T12: 0.0458
REMARK 3 T13: 0.0303 T23: 0.0194
REMARK 3 L TENSOR
REMARK 3 L11: 1.3070 L22: 1.8147
REMARK 3 L33: 1.9499 L12: -0.0788
REMARK 3 L13: 0.3478 L23: -1.1733
REMARK 3 S TENSOR
REMARK 3 S11: 0.0481 S12: 0.0501 S13: 0.0220
REMARK 3 S21: -0.0213 S22: -0.0804 S23: -0.0155
REMARK 3 S31: -0.1406 S32: -0.0689 S33: 0.0157
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 688 THROUGH 697 )
REMARK 3 ORIGIN FOR THE GROUP (A): -42.3570 46.2155 8.7329
REMARK 3 T TENSOR
REMARK 3 T11: 0.2048 T22: 0.2745
REMARK 3 T33: 0.2513 T12: 0.1118
REMARK 3 T13: 0.0455 T23: 0.0719
REMARK 3 L TENSOR
REMARK 3 L11: 0.9792 L22: 1.0019
REMARK 3 L33: 3.0971 L12: 0.7846
REMARK 3 L13: -0.7749 L23: 0.3493
REMARK 3 S TENSOR
REMARK 3 S11: 0.1876 S12: 0.1825 S13: -0.1034
REMARK 3 S21: 0.1210 S22: 0.0576 S23: -0.3230
REMARK 3 S31: -0.0047 S32: 0.1927 S33: -0.1090
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 698 THROUGH 715 )
REMARK 3 ORIGIN FOR THE GROUP (A): -42.8186 40.3643 21.2454
REMARK 3 T TENSOR
REMARK 3 T11: 0.1353 T22: 0.1107
REMARK 3 T33: 0.1261 T12: 0.0537
REMARK 3 T13: 0.0463 T23: 0.0421
REMARK 3 L TENSOR
REMARK 3 L11: 1.9435 L22: 1.5826
REMARK 3 L33: 4.9737 L12: 0.1331
REMARK 3 L13: -0.3396 L23: 0.2916
REMARK 3 S TENSOR
REMARK 3 S11: 0.1003 S12: 0.0302 S13: 0.2655
REMARK 3 S21: 0.0331 S22: -0.0995 S23: -0.1346
REMARK 3 S31: -0.2955 S32: -0.0810 S33: -0.0326
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 716 THROUGH 729 )
REMARK 3 ORIGIN FOR THE GROUP (A): -51.8006 33.6645 18.0462
REMARK 3 T TENSOR
REMARK 3 T11: 0.1066 T22: 0.1349
REMARK 3 T33: 0.1731 T12: 0.0591
REMARK 3 T13: -0.0006 T23: -0.0110
REMARK 3 L TENSOR
REMARK 3 L11: 2.8917 L22: 4.4048
REMARK 3 L33: 4.3620 L12: 0.1989
REMARK 3 L13: -0.1555 L23: -0.8175
REMARK 3 S TENSOR
REMARK 3 S11: 0.1962 S12: 0.4519 S13: -0.1922
REMARK 3 S21: -0.1457 S22: -0.0294 S23: 0.2949
REMARK 3 S31: -0.1934 S32: -0.5270 S33: -0.1217
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 621 THROUGH 687 )
REMARK 3 ORIGIN FOR THE GROUP (A): -20.5116 28.9399 0.0366
REMARK 3 T TENSOR
REMARK 3 T11: 0.0773 T22: 0.0974
REMARK 3 T33: 0.0949 T12: 0.0079
REMARK 3 T13: 0.0373 T23: -0.0112
REMARK 3 L TENSOR
REMARK 3 L11: 0.9536 L22: 1.1873
REMARK 3 L33: 1.6199 L12: 0.6860
REMARK 3 L13: 0.0482 L23: 0.2318
REMARK 3 S TENSOR
REMARK 3 S11: -0.0026 S12: -0.0817 S13: 0.0335
REMARK 3 S21: 0.1238 S22: 0.0056 S23: 0.1199
REMARK 3 S31: -0.0068 S32: -0.1597 S33: 0.0009
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 688 THROUGH 697 )
REMARK 3 ORIGIN FOR THE GROUP (A): -15.6020 45.0387 13.8562
REMARK 3 T TENSOR
REMARK 3 T11: 0.2039 T22: 0.2435
REMARK 3 T33: 0.1563 T12: -0.0265
REMARK 3 T13: 0.0586 T23: -0.0655
REMARK 3 L TENSOR
REMARK 3 L11: 0.4118 L22: 1.4376
REMARK 3 L33: 1.9425 L12: -0.7192
REMARK 3 L13: -0.2944 L23: 1.0853
REMARK 3 S TENSOR
REMARK 3 S11: -0.1626 S12: 0.0196 S13: -0.1150
REMARK 3 S21: 0.1726 S22: 0.0511 S23: 0.2585
REMARK 3 S31: 0.1701 S32: -0.2993 S33: 0.1243
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 698 THROUGH 715 )
REMARK 3 ORIGIN FOR THE GROUP (A): -16.4509 39.4064 1.4319
REMARK 3 T TENSOR
REMARK 3 T11: 0.1277 T22: 0.1165
REMARK 3 T33: 0.1076 T12: 0.0019
REMARK 3 T13: 0.0310 T23: -0.0567
REMARK 3 L TENSOR
REMARK 3 L11: 3.6375 L22: 3.0338
REMARK 3 L33: 6.5507 L12: 0.0941
REMARK 3 L13: -1.7276 L23: -0.6643
REMARK 3 S TENSOR
REMARK 3 S11: 0.1500 S12: 0.0405 S13: 0.2707
REMARK 3 S21: -0.0114 S22: 0.0164 S23: 0.2357
REMARK 3 S31: -0.4490 S32: -0.0995 S33: -0.1127
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 716 THROUGH 729 )
REMARK 3 ORIGIN FOR THE GROUP (A): -8.1943 31.3704 4.3779
REMARK 3 T TENSOR
REMARK 3 T11: 0.0811 T22: 0.0993
REMARK 3 T33: 0.1490 T12: -0.0205
REMARK 3 T13: -0.0166 T23: -0.0039
REMARK 3 L TENSOR
REMARK 3 L11: 3.3060 L22: 5.1977
REMARK 3 L33: 3.2379 L12: 0.0346
REMARK 3 L13: 0.1305 L23: 0.4825
REMARK 3 S TENSOR
REMARK 3 S11: 0.0995 S12: -0.3657 S13: -0.3366
REMARK 3 S21: 0.1427 S22: -0.0783 S23: -0.4071
REMARK 3 S31: -0.1884 S32: 0.3625 S33: -0.0774
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 4TYZ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 10-JUL-14.
REMARK 100 THE DEPOSITION ID IS D_1000202549.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 13-JUN-14; NULL
REMARK 200 TEMPERATURE (KELVIN) : 100; 100
REMARK 200 PH : 9.0; 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 2
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y; N
REMARK 200 RADIATION SOURCE : APS; ROTATING ANODE
REMARK 200 BEAMLINE : 21-ID-F; NULL
REMARK 200 X-RAY GENERATOR MODEL : NULL; RIGAKU FR-E+ SUPERBRIGHT
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M; M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97872; 1.5418
REMARK 200 MONOCHROMATOR : DIAMOND [111]; GRAPHITE
REMARK 200 OPTICS : NULL; NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD; NULL
REMARK 200 DETECTOR MANUFACTURER : RAYONIX MX-225; NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XSCALE
REMARK 200 DATA SCALING SOFTWARE : XDS, XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 36500
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.600
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 (%) : 99.4
REMARK 200 DATA REDUNDANCY : 7.300
REMARK 200 R MERGE (I) : 0.04800
REMARK 200 R SYM (I) : 0.04800
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 30.8800
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.64
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 7.29
REMARK 200 R MERGE FOR SHELL (I) : 0.52200
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.730
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH; SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 54.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.68
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: REAGENTS JCSG+ SCEEN B3: 20% PEG 6000,
REMARK 280 100MM BICINE PH 9.0; LEINA.18749.A.B1.PS02018 AT 8.28MG/ML,
REMARK 280 VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 290K. RIGAKUREAGENTS
REMARK 280 JCSG+ SCEEN A9: 20% PEG 3350, 200MM AMMONIUM CHLORIDE;
REMARK 280 LEINA.18749.A.B1.PS02018 AT 8.28MG/ML; THE CRYSTAL WAS SOAKED
REMARK 280 FOR 10SEC EACH IN RESERVOIR SOLUTION WITH 10% EG/500MM NAI, 20%
REMARK 280 EG/1000MM NAI, THIS SAMPLE WAS USED FOR IN-HOUSE PHASING, PH 7.5,
REMARK 280 VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 290K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+2/3
REMARK 290 6555 -X,-X+Y,-Z+1/3
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 45.04000
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 90.08000
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 90.08000
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 45.04000
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 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 A1177 LIES ON A SPECIAL POSITION.
REMARK 375 HOH B 866 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 GLN A 730
REMARK 465 GLN B 730
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 ASN A 621 CG OD1 ND2
REMARK 470 LYS A 729 CG CD CE NZ
REMARK 470 ASN B 621 CG OD1 ND2
REMARK 470 LYS B 628 CG CD CE NZ
REMARK 470 LYS B 692 CG CD CE NZ
REMARK 470 ASN B 705 CG OD1 ND2
REMARK 470 LYS B 729 CG CD CE NZ
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 OH TYR A 720 O HOH A 1101 2.19
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 LEU B 633 37.87 -93.78
REMARK 500 ASN B 696 36.96 -150.85
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 1000
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: SSGCID-LEINA.18749.A RELATED DB: TARGETTRACK
DBREF 4TYZ A 621 730 UNP A4I5U9 A4I5U9_LEIIN 621 730
DBREF 4TYZ B 621 730 UNP A4I5U9 A4I5U9_LEIIN 621 730
SEQRES 1 A 110 ASN ILE GLU GLY VAL PHE ARG LYS SER PHE PRO ASP LEU
SEQRES 2 A 110 ALA GLY GLU THR LEU LEU ASP SER PHE ASN CYS ALA TRP
SEQRES 3 A 110 VAL GLU GLY SER ALA LEU LYS GLN GLY TYR LEU PHE ILE
SEQRES 4 A 110 THR PRO HIS TRP LEU CYS PHE GLN SER THR LEU ALA ALA
SEQRES 5 A 110 ALA HIS PHE SER ILE GLU TYR ASP GLU ILE LYS ASP ILE
SEQRES 6 A 110 ILE LYS SER LYS SER VAL LYS MET PHE GLU ASN ALA ILE
SEQRES 7 A 110 GLU VAL LYS THR HIS LEU ASN ASP THR ILE PHE LEU THR
SEQRES 8 A 110 ASN PHE LEU GLN ARG ASP GLN ALA TYR SER ALA LEU MET
SEQRES 9 A 110 SER GLN TRP LEU LYS GLN
SEQRES 1 B 110 ASN ILE GLU GLY VAL PHE ARG LYS SER PHE PRO ASP LEU
SEQRES 2 B 110 ALA GLY GLU THR LEU LEU ASP SER PHE ASN CYS ALA TRP
SEQRES 3 B 110 VAL GLU GLY SER ALA LEU LYS GLN GLY TYR LEU PHE ILE
SEQRES 4 B 110 THR PRO HIS TRP LEU CYS PHE GLN SER THR LEU ALA ALA
SEQRES 5 B 110 ALA HIS PHE SER ILE GLU TYR ASP GLU ILE LYS ASP ILE
SEQRES 6 B 110 ILE LYS SER LYS SER VAL LYS MET PHE GLU ASN ALA ILE
SEQRES 7 B 110 GLU VAL LYS THR HIS LEU ASN ASP THR ILE PHE LEU THR
SEQRES 8 B 110 ASN PHE LEU GLN ARG ASP GLN ALA TYR SER ALA LEU MET
SEQRES 9 B 110 SER GLN TRP LEU LYS GLN
HET EDO A1000 4
HETNAM EDO 1,2-ETHANEDIOL
HETSYN EDO ETHYLENE GLYCOL
FORMUL 3 EDO C2 H6 O2
FORMUL 4 HOH *296(H2 O)
HELIX 1 AA1 ASN A 621 PHE A 630 1 10
HELIX 2 AA2 PRO A 631 ALA A 634 5 4
HELIX 3 AA3 GLN A 715 LEU A 728 1 14
HELIX 4 AA4 ILE B 622 PHE B 630 1 9
HELIX 5 AA5 GLN B 715 LYS B 729 1 15
SHEET 1 AA1 7 HIS A 674 GLU A 678 0
SHEET 2 AA1 7 TRP A 663 SER A 668 -1 N LEU A 664 O ILE A 677
SHEET 3 AA1 7 ALA A 651 ILE A 659 -1 N PHE A 658 O CYS A 665
SHEET 4 AA1 7 ASP A 640 GLU A 648 -1 N PHE A 642 O LEU A 657
SHEET 5 AA1 7 THR A 707 THR A 711 -1 O THR A 711 N ALA A 645
SHEET 6 AA1 7 ILE A 698 THR A 702 -1 N VAL A 700 O ILE A 708
SHEET 7 AA1 7 ILE A 682 LYS A 687 -1 N ILE A 686 O GLU A 699
SHEET 1 AA2 7 HIS B 674 GLU B 678 0
SHEET 2 AA2 7 TRP B 663 SER B 668 -1 N LEU B 664 O ILE B 677
SHEET 3 AA2 7 ALA B 651 ILE B 659 -1 N PHE B 658 O CYS B 665
SHEET 4 AA2 7 ASP B 640 GLU B 648 -1 N PHE B 642 O LEU B 657
SHEET 5 AA2 7 THR B 707 THR B 711 -1 O THR B 711 N ALA B 645
SHEET 6 AA2 7 ILE B 698 THR B 702 -1 N VAL B 700 O ILE B 708
SHEET 7 AA2 7 ILE B 682 LYS B 687 -1 N ILE B 686 O GLU B 699
SITE 1 AC1 7 ASP A 632 HOH A1127 HOH A1135 HOH A1138
SITE 2 AC1 7 LEU B 633 TRP B 663 SER B 676
CRYST1 58.860 58.860 135.120 90.00 90.00 120.00 P 31 2 1 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 0.016989 0.009809 0.000000 0.00000
SCALE2 0.000000 0.019618 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007401 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
