HEADER CELL CYCLE 05-FEB-18 6CC2
TITLE CRYSTAL STRUCTURE OF CDC45 FROM ENTAMOEBA HISTOLYTICA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CELL DIVISION CONTROL PROTEIN 45 CDC45 PUTATIVE;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ENTAMOEBA HISTOLYTICA;
SOURCE 3 ORGANISM_TAXID: 5759;
SOURCE 4 GENE: CL6EHI_049900;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS CELL DIVISION CONTROL PROTEIN, CELL CYCLE
EXPDTA X-RAY DIFFRACTION
AUTHOR K.SHI,F.KURNIAWAN,K.KURAHASHI,A.BIELINSKY,H.AIHARA
REVDAT 2 01-JAN-20 6CC2 1 REMARK
REVDAT 1 27-JUN-18 6CC2 0
JRNL AUTH F.KURNIAWAN,K.SHI,K.KURAHASHI,A.K.BIELINSKY,H.AIHARA
JRNL TITL CRYSTAL STRUCTURE OFENTAMOEBA HISTOLYTICACDC45 SUGGESTS A
JRNL TITL 2 CONFORMATIONAL SWITCH THAT MAY REGULATE DNA REPLICATION.
JRNL REF ISCIENCE V. 3 102 2018
JRNL REFN ESSN 2589-0042
JRNL PMID 29901028
JRNL DOI 10.1016/J.ISCI.2018.04.011
REMARK 2
REMARK 2 RESOLUTION. 1.66 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (DEV_3063: ???)
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) : 1.66
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 37.09
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 94.6
REMARK 3 NUMBER OF REFLECTIONS : 107361
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.159
REMARK 3 R VALUE (WORKING SET) : 0.157
REMARK 3 FREE R VALUE : 0.191
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.060
REMARK 3 FREE R VALUE TEST SET COUNT : 5435
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 37.0994 - 5.1536 0.93 3373 157 0.1698 0.2168
REMARK 3 2 5.1536 - 4.0923 0.94 3361 190 0.1223 0.1415
REMARK 3 3 4.0923 - 3.5755 0.96 3425 175 0.1258 0.1628
REMARK 3 4 3.5755 - 3.2488 0.96 3441 179 0.1389 0.1926
REMARK 3 5 3.2488 - 3.0160 0.97 3461 197 0.1513 0.1796
REMARK 3 6 3.0160 - 2.8383 0.94 3358 185 0.1522 0.1846
REMARK 3 7 2.8383 - 2.6962 0.95 3414 203 0.1482 0.1751
REMARK 3 8 2.6962 - 2.5788 0.96 3465 172 0.1426 0.1789
REMARK 3 9 2.5788 - 2.4796 0.98 3485 190 0.1463 0.1844
REMARK 3 10 2.4796 - 2.3940 0.96 3469 178 0.1474 0.2012
REMARK 3 11 2.3940 - 2.3192 0.97 3469 186 0.1460 0.1851
REMARK 3 12 2.3192 - 2.2529 0.92 3341 180 0.1518 0.1812
REMARK 3 13 2.2529 - 2.1936 0.97 3453 188 0.1474 0.1682
REMARK 3 14 2.1936 - 2.1401 0.95 3390 200 0.1508 0.2022
REMARK 3 15 2.1401 - 2.0914 0.98 3510 206 0.1621 0.1928
REMARK 3 16 2.0914 - 2.0469 0.97 3474 166 0.1592 0.1771
REMARK 3 17 2.0469 - 2.0060 0.93 3349 185 0.1580 0.1766
REMARK 3 18 2.0060 - 1.9681 0.96 3437 172 0.1656 0.1772
REMARK 3 19 1.9681 - 1.9330 0.93 3365 167 0.1768 0.2469
REMARK 3 20 1.9330 - 1.9002 0.90 3246 160 0.2026 0.2229
REMARK 3 21 1.9002 - 1.8696 0.95 3372 199 0.2165 0.2651
REMARK 3 22 1.8696 - 1.8408 0.92 3324 178 0.2279 0.2847
REMARK 3 23 1.8408 - 1.8137 0.94 3387 166 0.2285 0.2249
REMARK 3 24 1.8137 - 1.7882 0.96 3458 180 0.2301 0.2687
REMARK 3 25 1.7882 - 1.7640 0.95 3379 180 0.2334 0.2544
REMARK 3 26 1.7640 - 1.7411 0.94 3441 185 0.2520 0.2393
REMARK 3 27 1.7411 - 1.7194 0.95 3419 155 0.2592 0.2941
REMARK 3 28 1.7194 - 1.6986 0.94 3316 180 0.2710 0.2840
REMARK 3 29 1.6986 - 1.6789 0.92 3312 208 0.2866 0.3196
REMARK 3 30 1.6789 - 1.6600 0.89 3232 168 0.2975 0.3083
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) : 19.110
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 : 0.008 4220
REMARK 3 ANGLE : 0.748 5677
REMARK 3 CHIRALITY : 0.051 630
REMARK 3 PLANARITY : 0.006 708
REMARK 3 DIHEDRAL : 11.793 2510
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 4
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 1 THROUGH 123 )
REMARK 3 ORIGIN FOR THE GROUP (A): 35.4157 -21.0860 155.5166
REMARK 3 T TENSOR
REMARK 3 T11: 0.1870 T22: 0.1459
REMARK 3 T33: 0.2625 T12: -0.0000
REMARK 3 T13: 0.0436 T23: -0.0124
REMARK 3 L TENSOR
REMARK 3 L11: 1.8245 L22: 2.4613
REMARK 3 L33: 3.0530 L12: -0.2252
REMARK 3 L13: -0.0740 L23: -0.1956
REMARK 3 S TENSOR
REMARK 3 S11: -0.0654 S12: -0.0062 S13: -0.3641
REMARK 3 S21: -0.0012 S22: -0.0122 S23: 0.0661
REMARK 3 S31: 0.4812 S32: 0.0332 S33: 0.0359
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 124 THROUGH 213 )
REMARK 3 ORIGIN FOR THE GROUP (A): 41.8727 -10.5609 147.2512
REMARK 3 T TENSOR
REMARK 3 T11: 0.1101 T22: 0.2101
REMARK 3 T33: 0.1867 T12: -0.0142
REMARK 3 T13: 0.0416 T23: -0.0211
REMARK 3 L TENSOR
REMARK 3 L11: 1.1758 L22: 2.9101
REMARK 3 L33: 3.5846 L12: -0.0722
REMARK 3 L13: 0.2696 L23: 0.3886
REMARK 3 S TENSOR
REMARK 3 S11: 0.0260 S12: -0.0232 S13: -0.1694
REMARK 3 S21: -0.0636 S22: -0.0234 S23: -0.2073
REMARK 3 S31: 0.2832 S32: 0.1750 S33: 0.0627
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 214 THROUGH 417 )
REMARK 3 ORIGIN FOR THE GROUP (A): 32.1610 9.2739 141.4502
REMARK 3 T TENSOR
REMARK 3 T11: 0.1512 T22: 0.2119
REMARK 3 T33: 0.1210 T12: -0.0213
REMARK 3 T13: 0.0070 T23: -0.0158
REMARK 3 L TENSOR
REMARK 3 L11: 0.8925 L22: 1.6527
REMARK 3 L33: 1.0367 L12: -0.1557
REMARK 3 L13: -0.1246 L23: -0.3769
REMARK 3 S TENSOR
REMARK 3 S11: 0.0361 S12: 0.1493 S13: 0.0746
REMARK 3 S21: -0.1155 S22: 0.0214 S23: -0.0335
REMARK 3 S31: -0.1478 S32: -0.0035 S33: -0.0614
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 418 THROUGH 542 )
REMARK 3 ORIGIN FOR THE GROUP (A): 26.3024 7.2188 169.9778
REMARK 3 T TENSOR
REMARK 3 T11: 0.1483 T22: 0.1492
REMARK 3 T33: 0.1499 T12: 0.0055
REMARK 3 T13: 0.0226 T23: -0.0154
REMARK 3 L TENSOR
REMARK 3 L11: 2.6019 L22: 2.0911
REMARK 3 L33: 2.3575 L12: 0.3995
REMARK 3 L13: -0.7723 L23: 0.2053
REMARK 3 S TENSOR
REMARK 3 S11: -0.0730 S12: -0.0840 S13: -0.1946
REMARK 3 S21: 0.1881 S22: -0.0384 S23: 0.1234
REMARK 3 S31: 0.0626 S32: -0.0203 S33: 0.1090
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 6CC2 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-FEB-18.
REMARK 100 THE DEPOSITION ID IS D_1000232521.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-JUL-16
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 24-ID-C
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97880
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M-F
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 57872
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.660
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.7
REMARK 200 DATA REDUNDANCY : 5.100
REMARK 200 R MERGE (I) : 0.06800
REMARK 200 R SYM (I) : 0.06800
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 10.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.66
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.69
REMARK 200 COMPLETENESS FOR SHELL (%) : 92.1
REMARK 200 DATA REDUNDANCY IN SHELL : 5.10
REMARK 200 R MERGE FOR SHELL (I) : 0.90500
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.600
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: AUTOSOL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 37.27
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.96
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: SODIUM THIOCYANATE (PH 6.9),
REMARK 280 POLYETHYLENEGLYCOL 3,350, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 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 19.56000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 85.80000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 36.90500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 85.80000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 19.56000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 36.90500
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 GLN A 131
REMARK 465 GLN A 132
REMARK 465 PHE A 133
REMARK 465 ILE A 134
REMARK 465 GLU A 135
REMARK 465 GLN A 136
REMARK 465 GLU A 137
REMARK 465 THR A 138
REMARK 465 GLN A 139
REMARK 465 LEU A 140
REMARK 465 GLU A 141
REMARK 465 LYS A 142
REMARK 465 SER A 143
REMARK 465 ASP A 144
REMARK 465 LEU A 145
REMARK 465 LEU A 146
REMARK 465 GLU A 147
REMARK 465 VAL A 148
REMARK 465 ASP A 149
REMARK 465 ASP A 150
REMARK 465 ASP A 151
REMARK 465 LEU A 152
REMARK 465 ILE A 153
REMARK 465 GLY A 154
REMARK 465 LEU A 155
REMARK 465 ASN A 156
REMARK 465 LYS A 157
REMARK 465 SER A 158
REMARK 465 GLN A 159
REMARK 465 SER A 160
REMARK 465 PHE A 161
REMARK 465 ASN A 162
REMARK 465 ASN A 163
REMARK 465 CYS A 164
REMARK 465 GLU A 165
REMARK 465 TYR A 166
REMARK 465 ILE A 167
REMARK 465 ARG A 168
REMARK 465 LYS A 169
REMARK 465 MSE A 170
REMARK 465 ILE A 543
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 C LYS A 538 H CME A 539 1.60
REMARK 500 OE2 GLU A 476 O HOH A 701 1.93
REMARK 500 O HOH A 865 O HOH A 1043 1.95
REMARK 500 O HOH A 763 O HOH A 1030 2.01
REMARK 500 O HOH A 1043 O HOH A 1065 2.05
REMARK 500 O HOH A 935 O HOH A 1076 2.06
REMARK 500 O HOH A 1016 O HOH A 1064 2.07
REMARK 500 NZ LYS A 320 O HOH A 702 2.09
REMARK 500 OD1 ASP A 76 O HOH A 703 2.09
REMARK 500 O HOH A 808 O HOH A 1077 2.10
REMARK 500 O2 EDO A 601 O HOH A 704 2.12
REMARK 500 O HOH A 1071 O HOH A 1075 2.12
REMARK 500 O HOH A 977 O HOH A 1039 2.12
REMARK 500 O HOH A 883 O HOH A 939 2.14
REMARK 500 O HOH A 1002 O HOH A 1093 2.14
REMARK 500 O HOH A 976 O HOH A 994 2.14
REMARK 500 O HOH A 976 O HOH A 990 2.16
REMARK 500 O HOH A 1064 O HOH A 1097 2.16
REMARK 500 O HOH A 915 O HOH A 976 2.17
REMARK 500 O HOH A 870 O HOH A 1043 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 ALA A 86 -22.29 83.29
REMARK 500 ASP A 97 104.56 -55.05
REMARK 500 SER A 179 -144.75 -112.62
REMARK 500 TRP A 265 -144.29 -143.50
REMARK 500 ASN A 336 1.14 -69.20
REMARK 500 SER A 516 -167.68 -119.00
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A1101 DISTANCE = 6.24 ANGSTROMS
REMARK 525 HOH A1102 DISTANCE = 6.63 ANGSTROMS
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 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 603
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 604
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 605
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 606
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 607
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 608
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 609
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 610
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 611
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 612
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 614
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 615
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG A 616
DBREF1 6CC2 A 1 543 UNP A0A175JFA5_ENTHI
DBREF2 6CC2 A A0A175JFA5 1 543
SEQRES 1 A 543 MSE ILE ILE ASN GLY THR SER PHE GLU GLU LEU TYR ASN
SEQRES 2 A 543 GLY LEU ARG ASN ARG GLY LYS ASP LYS LYS THR ILE GLN
SEQRES 3 A 543 LEU TYR VAL SER PRO THR VAL ASP ALA ILE VAL CYS TYR
SEQRES 4 A 543 LYS ILE LEU SER MSE MSE PHE GLU LYS ASP GLY LEU LEU
SEQRES 5 A 543 HIS SER ALA VAL PRO VAL ASN ASN TYR GLU THR LEU SER
SEQRES 6 A 543 ARG VAL PHE LYS GLU THR ILE GLY HIS THR ASP VAL HIS
SEQRES 7 A 543 THR VAL PHE PHE ILE ASP CYS ALA GLY SER ILE ASP VAL
SEQRES 8 A 543 SER GLU LEU LEU GLY ASP ILE GLU ASN ILE PHE VAL TYR
SEQRES 9 A 543 ILE ILE ASP SER HIS ARG PRO PHE ASN LYS LEU ASN VAL
SEQRES 10 A 543 THR ASN THR ASN ILE GLY LEU ILE THR SER ASN GLU TYR
SEQRES 11 A 543 GLN GLN PHE ILE GLU GLN GLU THR GLN LEU GLU LYS SER
SEQRES 12 A 543 ASP LEU LEU GLU VAL ASP ASP ASP LEU ILE GLY LEU ASN
SEQRES 13 A 543 LYS SER GLN SER PHE ASN ASN CYS GLU TYR ILE ARG LYS
SEQRES 14 A 543 MSE VAL ASP SER ASP GLY GLU PHE TYR SER GLU SER VAL
SEQRES 15 A 543 GLY ARG VAL ALA LEU ALA ILE ALA LYS LYS LEU ASN LYS
SEQRES 16 A 543 VAL GLU ASN ASP MSE TYR TRP TYR ALA ALA ILE GLY VAL
SEQRES 17 A 543 CYS ASP GLN TYR ILE SER LEU LYS ILE ASN ALA LYS THR
SEQRES 18 A 543 TYR VAL HIS ALA ILE GLN TYR PHE ILE ASP ASN LEU GLN
SEQRES 19 A 543 LEU GLU THR LEU GLU ILE THR ASP LEU LEU GLN THR VAL
SEQRES 20 A 543 LYS THR PRO MSE CYS VAL LYS MSE ASP CYS GLN LEU MSE
SEQRES 21 A 543 LEU LEU ARG HIS TRP THR LEU TYR ASP SER LEU PHE HIS
SEQRES 22 A 543 THR ARG GLU ILE ALA SER LYS LEU GLY ILE TRP THR SER
SEQRES 23 A 543 ARG GLY LYS GLU LYS PHE ASP VAL LEU ILE ALA ASP MSE
SEQRES 24 A 543 GLY ILE PRO LEU SER GLN ALA GLN GLN SER TYR LYS THR
SEQRES 25 A 543 MSE SER LEU GLU MSE LYS ASN LYS PHE LEU LEU LYS MSE
SEQRES 26 A 543 GLU GLY TYR SER LYS PHE TYR HIS PHE GLU ASN LEU PHE
SEQRES 27 A 543 LEU PRO SER PHE PHE LYS LYS PHE GLY MSE ASP TYR SER
SEQRES 28 A 543 ILE SER ALA PHE ASP ALA ALA HIS ALA ILE GLY SER ILE
SEQRES 29 A 543 ILE THR ASN ASP GLU PRO ASP GLN ASN TRP GLN GLN GLN
SEQRES 30 A 543 PHE TRP GLU GLY PHE LYS LEU LEU SER SER THR THR ALA
SEQRES 31 A 543 GLU PRO TYR ASP PHE GLY PHE ALA LYS CYS ILE GLU SER
SEQRES 32 A 543 ASN LYS ASN LEU VAL GLU THR GLY ILE ILE LEU LEU LEU
SEQRES 33 A 543 SER GLY SER CYS PHE ASN GLU ALA ASN LYS TYR ARG PHE
SEQRES 34 A 543 CYS SER VAL SER ASP GLU LEU LEU SER ILE ARG PHE LYS
SEQRES 35 A 543 THR PRO TYR LYS ALA LEU GLN LEU ALA GLN PHE LEU ALA
SEQRES 36 A 543 GLU ALA SER SER ARG ARG TYR LYS LYS TRP LEU PRO PHE
SEQRES 37 A 543 ILE LEU ALA VAL LEU ASP ALA GLU LYS LYS THR PHE VAL
SEQRES 38 A 543 ILE VAL GLY TYR SER SER PRO ILE SER VAL LYS THR LEU
SEQRES 39 A 543 ASN TYR PHE GLY ALA LYS PHE THR GLN THR ALA GLN ASN
SEQRES 40 A 543 MSE LYS ILE SER ILE LEU GLN LYS SER PHE ASP SER PHE
SEQRES 41 A 543 VAL THR GLU ILE HIS ARG GLU ASN LEU VAL LYS TYR LYS
SEQRES 42 A 543 LYS ALA LEU HIS LYS CME PHE THR SER ILE
MODRES 6CC2 MSE A 1 MET MODIFIED RESIDUE
MODRES 6CC2 MSE A 44 MET MODIFIED RESIDUE
MODRES 6CC2 MSE A 45 MET MODIFIED RESIDUE
MODRES 6CC2 MSE A 200 MET MODIFIED RESIDUE
MODRES 6CC2 MSE A 251 MET MODIFIED RESIDUE
MODRES 6CC2 MSE A 255 MET MODIFIED RESIDUE
MODRES 6CC2 MSE A 260 MET MODIFIED RESIDUE
MODRES 6CC2 MSE A 299 MET MODIFIED RESIDUE
MODRES 6CC2 MSE A 313 MET MODIFIED RESIDUE
MODRES 6CC2 MSE A 317 MET MODIFIED RESIDUE
MODRES 6CC2 MSE A 325 MET MODIFIED RESIDUE
MODRES 6CC2 MSE A 348 MET MODIFIED RESIDUE
MODRES 6CC2 MSE A 508 MET MODIFIED RESIDUE
MODRES 6CC2 CME A 539 CYS MODIFIED RESIDUE
HET MSE A 1 9
HET MSE A 44 10
HET MSE A 45 10
HET MSE A 200 17
HET MSE A 251 17
HET MSE A 255 17
HET MSE A 260 17
HET MSE A 299 17
HET MSE A 313 17
HET MSE A 317 17
HET MSE A 325 10
HET MSE A 348 17
HET MSE A 508 17
HET CME A 539 19
HET EDO A 601 10
HET EDO A 602 10
HET EDO A 603 10
HET EDO A 604 10
HET EDO A 605 10
HET EDO A 606 10
HET EDO A 607 10
HET EDO A 608 10
HET EDO A 609 10
HET EDO A 610 10
HET EDO A 611 10
HET EDO A 612 10
HET CL A 613 1
HET CL A 614 1
HET CL A 615 1
HET PEG A 616 17
HETNAM MSE SELENOMETHIONINE
HETNAM CME S,S-(2-HYDROXYETHYL)THIOCYSTEINE
HETNAM EDO 1,2-ETHANEDIOL
HETNAM CL CHLORIDE ION
HETNAM PEG DI(HYDROXYETHYL)ETHER
HETSYN EDO ETHYLENE GLYCOL
FORMUL 1 MSE 13(C5 H11 N O2 SE)
FORMUL 1 CME C5 H11 N O3 S2
FORMUL 2 EDO 12(C2 H6 O2)
FORMUL 14 CL 3(CL 1-)
FORMUL 17 PEG C4 H10 O3
FORMUL 18 HOH *402(H2 O)
HELIX 1 AA1 ASN A 4 THR A 6 5 3
HELIX 2 AA2 SER A 7 ASP A 21 1 15
HELIX 3 AA3 THR A 32 ASP A 49 1 18
HELIX 4 AA4 ASN A 60 ILE A 72 1 13
HELIX 5 AA5 ASP A 90 GLY A 96 1 7
HELIX 6 AA6 ASN A 113 ASN A 119 1 7
HELIX 7 AA7 SER A 181 LEU A 193 1 13
HELIX 8 AA8 ASN A 198 SER A 214 1 17
HELIX 9 AA9 ASN A 218 GLN A 234 1 17
HELIX 10 AB1 LEU A 261 TRP A 265 5 5
HELIX 11 AB2 THR A 266 THR A 274 1 9
HELIX 12 AB3 THR A 274 GLY A 282 1 9
HELIX 13 AB4 ARG A 287 MSE A 299 1 13
HELIX 14 AB5 PRO A 302 GLN A 307 1 6
HELIX 15 AB6 SER A 314 TYR A 332 1 19
HELIX 16 AB7 PHE A 334 ASN A 336 5 3
HELIX 17 AB8 SER A 353 ILE A 365 1 13
HELIX 18 AB9 ASN A 373 SER A 386 1 14
HELIX 19 AC1 PRO A 392 GLY A 418 1 27
HELIX 20 AC2 ASP A 434 LYS A 442 1 9
HELIX 21 AC3 THR A 443 LYS A 463 1 21
HELIX 22 AC4 SER A 487 LYS A 492 5 6
HELIX 23 AC5 THR A 493 LYS A 509 1 17
HELIX 24 AC6 ASN A 528 PHE A 540 1 13
SHEET 1 AA1 6 ILE A 2 ILE A 3 0
SHEET 2 AA1 6 ILE A 122 ILE A 125 1 O LEU A 124 N ILE A 3
SHEET 3 AA1 6 PHE A 102 ILE A 106 1 N ILE A 105 O GLY A 123
SHEET 4 AA1 6 VAL A 77 ILE A 83 1 N VAL A 80 O PHE A 102
SHEET 5 AA1 6 THR A 24 VAL A 29 1 N TYR A 28 O PHE A 81
SHEET 6 AA1 6 HIS A 53 PRO A 57 1 O VAL A 56 N LEU A 27
SHEET 1 AA2 2 HIS A 109 ARG A 110 0
SHEET 2 AA2 2 PHE A 177 TYR A 178 -1 O PHE A 177 N ARG A 110
SHEET 1 AA3 3 THR A 237 LEU A 238 0
SHEET 2 AA3 3 MSE A 251 CYS A 257 1 O VAL A 253 N LEU A 238
SHEET 3 AA3 3 PHE A 338 LYS A 344 -1 O PHE A 343 N CYS A 252
SHEET 1 AA4 6 SER A 419 GLU A 423 0
SHEET 2 AA4 6 TYR A 427 VAL A 432 -1 O PHE A 429 N PHE A 421
SHEET 3 AA4 6 PHE A 468 ASP A 474 1 O ILE A 469 N ARG A 428
SHEET 4 AA4 6 THR A 479 TYR A 485 -1 O THR A 479 N ASP A 474
SHEET 5 AA4 6 SER A 519 HIS A 525 -1 O THR A 522 N ILE A 482
SHEET 6 AA4 6 GLN A 514 LYS A 515 -1 N GLN A 514 O VAL A 521
SSBOND 1 CYS A 420 CYS A 430 1555 1555 2.59
LINK C MSE A 1 N ILE A 2 1555 1555 1.32
LINK C SER A 43 N MSE A 44 1555 1555 1.32
LINK C MSE A 44 N MSE A 45 1555 1555 1.33
LINK C MSE A 45 N PHE A 46 1555 1555 1.34
LINK C ASP A 199 N MSE A 200 1555 1555 1.33
LINK C MSE A 200 N TYR A 201 1555 1555 1.33
LINK C PRO A 250 N MSE A 251 1555 1555 1.33
LINK C MSE A 251 N CYS A 252 1555 1555 1.33
LINK C LYS A 254 N MSE A 255 1555 1555 1.33
LINK C MSE A 255 N ASP A 256 1555 1555 1.33
LINK C LEU A 259 N MSE A 260 1555 1555 1.32
LINK C MSE A 260 N LEU A 261 1555 1555 1.34
LINK C ASP A 298 N MSE A 299 1555 1555 1.33
LINK C MSE A 299 N GLY A 300 1555 1555 1.33
LINK C THR A 312 N MSE A 313 1555 1555 1.33
LINK C MSE A 313 N SER A 314 1555 1555 1.33
LINK C GLU A 316 N MSE A 317 1555 1555 1.33
LINK C MSE A 317 N LYS A 318 1555 1555 1.34
LINK C LYS A 324 N MSE A 325 1555 1555 1.34
LINK C MSE A 325 N GLU A 326 1555 1555 1.33
LINK C GLY A 347 N MSE A 348 1555 1555 1.33
LINK C MSE A 348 N ASP A 349 1555 1555 1.32
LINK C ASN A 507 N MSE A 508 1555 1555 1.33
LINK C MSE A 508 N LYS A 509 1555 1555 1.33
LINK C LYS A 538 N CME A 539 1555 1555 1.32
LINK C CME A 539 N PHE A 540 1555 1555 1.31
CISPEP 1 ARG A 110 PRO A 111 0 -6.43
SITE 1 AC1 5 ASN A 198 PRO A 250 MSE A 251 LYS A 320
SITE 2 AC1 5 HOH A 704
SITE 1 AC2 7 CYS A 420 PHE A 421 ASN A 422 ARG A 428
SITE 2 AC2 7 TYR A 462 ARG A 526 HOH A 912
SITE 1 AC3 4 MSE A 508 ILE A 524 HIS A 525 ASN A 528
SITE 1 AC4 8 TYR A 178 ILE A 217 THR A 221 GLU A 369
SITE 2 AC4 8 PRO A 370 ASP A 371 HOH A 923 HOH A 925
SITE 1 AC5 4 GLN A 375 EDO A 608 HOH A 706 HOH A 968
SITE 1 AC6 4 THR A 479 GLU A 523 HIS A 525 HOH A 890
SITE 1 AC7 3 LEU A 243 ARG A 263 TYR A 310
SITE 1 AC8 4 TYR A 130 GLN A 375 EDO A 605 HOH A 714
SITE 1 AC9 4 TYR A 39 GLU A 47 HIS A 53 PHE A 382
SITE 1 AD1 2 ASP A 256 ARG A 263
SITE 1 AD2 3 LYS A 311 MSE A 313 LYS A 318
SITE 1 AD3 3 ARG A 460 LYS A 463 TRP A 465
SITE 1 AD4 1 ASN A 406
SITE 1 AD5 2 ASN A 336 HOH A 993
SITE 1 AD6 8 ILE A 413 SER A 417 GLY A 418 ASN A 422
SITE 2 AD6 8 ALA A 424 ASN A 425 SER A 433 ASP A 434
CRYST1 39.120 73.810 171.600 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 0.025562 0.000000 0.000000 0.00000
SCALE2 0.000000 0.013548 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005828 0.00000
HETATM 1 N MSE A 1 46.825 -21.985 161.080 1.00 26.57 N
ANISOU 1 N MSE A 1 2715 3476 3904 1095 59 474 N
HETATM 2 CA MSE A 1 48.019 -21.962 160.236 1.00 35.85 C
ANISOU 2 CA MSE A 1 3707 4766 5148 1190 78 454 C
HETATM 3 C MSE A 1 47.820 -21.044 159.040 1.00 29.24 C
ANISOU 3 C MSE A 1 2800 3975 4333 1051 150 355 C
HETATM 4 O MSE A 1 46.689 -20.734 158.671 1.00 28.97 O
ANISOU 4 O MSE A 1 2884 3847 4276 922 196 297 O
HETATM 5 CB MSE A 1 48.368 -23.369 159.756 1.00 59.93 C
ANISOU 5 CB MSE A 1 6817 7697 8256 1397 158 474 C
HETATM 6 CG MSE A 1 47.291 -24.042 158.930 1.00 84.27 C
ANISOU 6 CG MSE A 1 10093 10570 11356 1358 277 403 C
HETATM 7 SE MSE A 1 47.852 -25.808 158.309 1.00110.51 SE
ANISOU 7 SE MSE A 1 13523 13716 14751 1631 377 409 SE
HETATM 8 CE MSE A 1 46.181 -26.372 157.472 1.00120.37 C
ANISOU 8 CE MSE A 1 15037 14700 15998 1474 482 300 C
HETATM 9 HA MSE A 1 48.766 -21.638 160.764 1.00 43.02 H
(ATOM LINES ARE NOT SHOWN.)
END