HEADER HYDROLASE 14-DEC-15 5FBY
TITLE CRYSTAL STRUCTURE OF CTSPD
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SEPARASE;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 1621-2223;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: CLEAVED PEPTIDE;
COMPND 8 CHAIN: B;
COMPND 9 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: CHAETOMIUM THERMOPHILUM (STRAIN DSM 1495 / CBS
SOURCE 3 144.50 / IMI 039719);
SOURCE 4 ORGANISM_TAXID: 759272;
SOURCE 5 STRAIN: DSM 1495 / CBS 144.50 / IMI 039719;
SOURCE 6 GENE: CTHT_0070540;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 9 MOL_ID: 2;
SOURCE 10 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;
SOURCE 11 ORGANISM_TAXID: 32630;
SOURCE 12 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 13 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS COHESIN, COMPLEX, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR Z.LIN,X.LUO,H.YU
REVDAT 6 06-MAR-24 5FBY 1 REMARK
REVDAT 5 27-SEP-17 5FBY 1 REMARK
REVDAT 4 04-MAY-16 5FBY 1 COMPND
REVDAT 3 27-APR-16 5FBY 1 JRNL
REVDAT 2 13-APR-16 5FBY 1 JRNL
REVDAT 1 30-MAR-16 5FBY 0
JRNL AUTH Z.LIN,X.LUO,H.YU
JRNL TITL STRUCTURAL BASIS OF COHESIN CLEAVAGE BY SEPARASE.
JRNL REF NATURE V. 532 131 2016
JRNL REFN ESSN 1476-4687
JRNL PMID 27027290
JRNL DOI 10.1038/NATURE17402
REMARK 2
REMARK 2 RESOLUTION. 1.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX DEV_1839
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) : 1.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.38
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.4
REMARK 3 NUMBER OF REFLECTIONS : 46923
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.172
REMARK 3 R VALUE (WORKING SET) : 0.171
REMARK 3 FREE R VALUE : 0.198
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.280
REMARK 3 FREE R VALUE TEST SET COUNT : 2006
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 49.3973 - 4.5739 1.00 3470 150 0.1833 0.2034
REMARK 3 2 4.5739 - 3.6308 1.00 3325 151 0.1460 0.1784
REMARK 3 3 3.6308 - 3.1719 1.00 3286 146 0.1565 0.1788
REMARK 3 4 3.1719 - 2.8819 1.00 3289 144 0.1729 0.1884
REMARK 3 5 2.8819 - 2.6754 1.00 3254 145 0.1652 0.1835
REMARK 3 6 2.6754 - 2.5177 1.00 3232 146 0.1717 0.1849
REMARK 3 7 2.5177 - 2.3916 1.00 3245 148 0.1625 0.1866
REMARK 3 8 2.3916 - 2.2875 1.00 3244 141 0.1690 0.2096
REMARK 3 9 2.2875 - 2.1994 1.00 3228 140 0.1797 0.2129
REMARK 3 10 2.1994 - 2.1235 1.00 3230 137 0.1763 0.2231
REMARK 3 11 2.1235 - 2.0571 1.00 3189 146 0.1799 0.2018
REMARK 3 12 2.0571 - 1.9983 0.99 3167 154 0.1878 0.2370
REMARK 3 13 1.9983 - 1.9457 0.94 3022 125 0.2005 0.2599
REMARK 3 14 1.9457 - 1.8982 0.85 2736 133 0.2359 0.2586
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) : 0.170
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 18.620
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 : 0.011 4040
REMARK 3 ANGLE : 1.262 5471
REMARK 3 CHIRALITY : 0.052 601
REMARK 3 PLANARITY : 0.009 708
REMARK 3 DIHEDRAL : 13.527 1469
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 6
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 1684 THROUGH 1818 )
REMARK 3 ORIGIN FOR THE GROUP (A): 12.9290 -2.3908 10.5232
REMARK 3 T TENSOR
REMARK 3 T11: 0.1872 T22: 0.0893
REMARK 3 T33: 0.1606 T12: -0.0511
REMARK 3 T13: -0.0439 T23: 0.0334
REMARK 3 L TENSOR
REMARK 3 L11: 0.8403 L22: 0.5340
REMARK 3 L33: 1.5464 L12: 0.0926
REMARK 3 L13: -0.3729 L23: -0.2313
REMARK 3 S TENSOR
REMARK 3 S11: -0.0818 S12: -0.0448 S13: -0.2936
REMARK 3 S21: -0.0618 S22: 0.0662 S23: -0.0690
REMARK 3 S31: 0.4423 S32: -0.0758 S33: 0.1009
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 1819 THROUGH 1945 )
REMARK 3 ORIGIN FOR THE GROUP (A): 36.0060 -9.3784 9.9968
REMARK 3 T TENSOR
REMARK 3 T11: 0.2165 T22: 0.3728
REMARK 3 T33: 0.3740 T12: 0.2208
REMARK 3 T13: 0.0411 T23: 0.2396
REMARK 3 L TENSOR
REMARK 3 L11: 1.4066 L22: 0.3566
REMARK 3 L33: 0.8722 L12: -0.1856
REMARK 3 L13: 0.3573 L23: -0.4203
REMARK 3 S TENSOR
REMARK 3 S11: -0.0084 S12: -0.2075 S13: -0.4005
REMARK 3 S21: -0.1608 S22: -0.2514 S23: -0.2144
REMARK 3 S31: 0.4340 S32: 0.4860 S33: -0.3499
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 1946 THROUGH 2059 )
REMARK 3 ORIGIN FOR THE GROUP (A): 10.7448 17.7994 15.5046
REMARK 3 T TENSOR
REMARK 3 T11: 0.1347 T22: 0.1009
REMARK 3 T33: 0.0898 T12: -0.0181
REMARK 3 T13: -0.0263 T23: 0.0142
REMARK 3 L TENSOR
REMARK 3 L11: 1.0330 L22: 1.3686
REMARK 3 L33: 1.3915 L12: -0.2610
REMARK 3 L13: -0.3240 L23: -0.2140
REMARK 3 S TENSOR
REMARK 3 S11: 0.0220 S12: -0.1607 S13: 0.1097
REMARK 3 S21: 0.1847 S22: 0.0883 S23: -0.0477
REMARK 3 S31: -0.2254 S32: 0.0077 S33: -0.0514
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 2060 THROUGH 2112 )
REMARK 3 ORIGIN FOR THE GROUP (A): -1.5535 22.0101 10.8067
REMARK 3 T TENSOR
REMARK 3 T11: 0.1483 T22: 0.1168
REMARK 3 T33: 0.1194 T12: 0.0450
REMARK 3 T13: 0.0370 T23: 0.0463
REMARK 3 L TENSOR
REMARK 3 L11: 2.8461 L22: 3.4078
REMARK 3 L33: 1.4477 L12: -0.3372
REMARK 3 L13: 1.0472 L23: -0.2097
REMARK 3 S TENSOR
REMARK 3 S11: -0.0317 S12: -0.0620 S13: 0.0180
REMARK 3 S21: -0.0677 S22: 0.1156 S23: 0.1607
REMARK 3 S31: -0.1083 S32: -0.2115 S33: -0.0541
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 2113 THROUGH 2220 )
REMARK 3 ORIGIN FOR THE GROUP (A): 8.8238 13.4554 18.2463
REMARK 3 T TENSOR
REMARK 3 T11: 0.1034 T22: 0.0911
REMARK 3 T33: 0.0823 T12: -0.0072
REMARK 3 T13: -0.0333 T23: 0.0221
REMARK 3 L TENSOR
REMARK 3 L11: 1.5811 L22: 1.5495
REMARK 3 L33: 1.7295 L12: -0.1093
REMARK 3 L13: -0.3365 L23: -0.6547
REMARK 3 S TENSOR
REMARK 3 S11: 0.0377 S12: -0.1076 S13: 0.0479
REMARK 3 S21: 0.1189 S22: 0.0953 S23: 0.0373
REMARK 3 S31: -0.1605 S32: -0.1254 S33: 0.0298
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 10 THROUGH 20 )
REMARK 3 ORIGIN FOR THE GROUP (A): 13.6440 3.5653 -6.0068
REMARK 3 T TENSOR
REMARK 3 T11: 0.1508 T22: 0.2107
REMARK 3 T33: 0.1597 T12: -0.0356
REMARK 3 T13: -0.0589 T23: 0.0027
REMARK 3 L TENSOR
REMARK 3 L11: 4.0944 L22: 3.7407
REMARK 3 L33: 2.4798 L12: -3.2347
REMARK 3 L13: -2.9844 L23: 2.4982
REMARK 3 S TENSOR
REMARK 3 S11: 0.3282 S12: 0.6346 S13: -0.1662
REMARK 3 S21: -0.6062 S22: -0.2123 S23: 0.2531
REMARK 3 S31: -0.0381 S32: -0.4515 S33: 0.1436
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 5FBY COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-DEC-15.
REMARK 100 THE DEPOSITION ID IS D_1000216351.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 27-JAN-15
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 8.2.1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.979
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 47718
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.898
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 (%) : 100.0
REMARK 200 DATA REDUNDANCY : 7.200
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 27.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: HKL-3000
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 45.70
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.27
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG3350, AMMONIUM CITRATE TRIBASIC,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 27.77950
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 53.87350
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 49.44450
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 53.87350
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 27.77950
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 49.44450
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1730 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 21260 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -8.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 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 LYS A 1661
REMARK 465 LYS A 1662
REMARK 465 GLY A 1663
REMARK 465 LEU A 1664
REMARK 465 VAL A 1665
REMARK 465 ASN A 1666
REMARK 465 GLY A 1667
REMARK 465 ASN A 1668
REMARK 465 GLY A 1669
REMARK 465 THR A 1670
REMARK 465 GLU A 1671
REMARK 465 MET A 1672
REMARK 465 THR A 1673
REMARK 465 SER A 1674
REMARK 465 VAL A 1675
REMARK 465 GLN A 1676
REMARK 465 PHE A 1677
REMARK 465 PRO A 1678
REMARK 465 PRO A 1679
REMARK 465 PRO A 1680
REMARK 465 PRO A 1681
REMARK 465 ASN A 1682
REMARK 465 SER A 1750
REMARK 465 SER A 1751
REMARK 465 ARG A 1752
REMARK 465 ASP A 1753
REMARK 465 SER A 1754
REMARK 465 SER A 1755
REMARK 465 VAL A 1756
REMARK 465 ASP A 1757
REMARK 465 GLU A 1758
REMARK 465 THR A 1759
REMARK 465 ASP A 1760
REMARK 465 ARG A 1856
REMARK 465 GLN A 1857
REMARK 465 VAL A 1858
REMARK 465 GLY A 1859
REMARK 465 ARG A 1860
REMARK 465 GLY A 1861
REMARK 465 LYS A 1862
REMARK 465 LYS A 1863
REMARK 465 GLY A 1864
REMARK 465 LYS A 1865
REMARK 465 GLY A 1866
REMARK 465 VAL A 1867
REMARK 465 ALA A 1868
REMARK 465 GLY A 1869
REMARK 465 GLN A 1870
REMARK 465 THR A 1871
REMARK 465 GLU A 1948
REMARK 465 SER A 1949
REMARK 465 ASP A 1950
REMARK 465 GLN A 2001
REMARK 465 ILE A 2002
REMARK 465 GLN A 2003
REMARK 465 GLY A 2004
REMARK 465 GLU A 2005
REMARK 465 ASP A 2006
REMARK 465 SER A 2007
REMARK 465 GLU A 2008
REMARK 465 GLU A 2009
REMARK 465 GLU A 2010
REMARK 465 GLU A 2171
REMARK 465 LYS A 2172
REMARK 465 ASN A 2173
REMARK 465 GLY A 2174
REMARK 465 LYS A 2175
REMARK 465 LYS A 2176
REMARK 465 LYS A 2177
REMARK 465 ALA A 2178
REMARK 465 SER A 2221
REMARK 465 LYS A 2222
REMARK 465 ASP A 2223
REMARK 465 MET B 1
REMARK 465 GLY B 2
REMARK 465 SER B 3
REMARK 465 SER B 4
REMARK 465 HIS B 5
REMARK 465 HIS B 6
REMARK 465 HIS B 7
REMARK 465 HIS B 8
REMARK 465 HIS B 9
REMARK 465 LEU B 21
REMARK 465 GLY B 22
REMARK 465 SER B 23
REMARK 465 GLY B 24
REMARK 465 ARG B 25
REMARK 465 PRO B 26
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 OE2 GLU A 1942 O HOH A 2401 1.93
REMARK 500 OD2 ASP A 1960 O HOH A 2402 1.95
REMARK 500 O HOH A 2753 O HOH A 2764 1.97
REMARK 500 O HOH A 2695 O HOH A 2707 1.99
REMARK 500 O HOH A 2587 O HOH A 2695 2.01
REMARK 500 O HOH A 2652 O HOH A 2730 2.02
REMARK 500 O HOH A 2603 O HOH A 2709 2.03
REMARK 500 O HOH A 2631 O HOH A 2747 2.03
REMARK 500 O HOH A 2510 O HOH A 2673 2.06
REMARK 500 O VAL A 1873 O HOH A 2403 2.13
REMARK 500 OE1 GLU A 1802 O HOH A 2404 2.15
REMARK 500 O HOH A 2611 O HOH A 2697 2.17
REMARK 500 O HOH A 2587 O HOH A 2707 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH A 2728 O HOH A 2780 4555 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 TYR A1706 -53.73 -124.73
REMARK 500 SER A1854 4.64 53.47
REMARK 500 HIS A1914 30.27 -95.20
REMARK 500 SER A2032 -13.63 78.19
REMARK 500 THR A2202 -62.70 -104.22
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5FC2 RELATED DB: PDB
REMARK 900 RELATED ID: 5FC3 RELATED DB: PDB
DBREF 5FBY A 1661 2223 UNP G0SHM3 G0SHM3_CHATD 1661 2223
DBREF 5FBY B 1 26 PDB 5FBY 5FBY 1 26
SEQRES 1 A 563 LYS LYS GLY LEU VAL ASN GLY ASN GLY THR GLU MET THR
SEQRES 2 A 563 SER VAL GLN PHE PRO PRO PRO PRO ASN LEU ALA ALA SER
SEQRES 3 A 563 ALA PRO ARG ARG SER SER LEU GLY PHE THR LEU ASP LEU
SEQRES 4 A 563 HIS ARG ILE GLN ARG ASP TYR ILE ASP LEU VAL PRO LYS
SEQRES 5 A 563 HIS TRP HIS VAL ILE SER LEU SER LEU SER ASP GLY GLY
SEQRES 6 A 563 HIS ASP LEU CYS ILE THR ARG LEU GLN ALA GLY GLN ALA
SEQRES 7 A 563 PRO PHE VAL LEU ARG LEU PRO LEU GLU ARG ALA SER SER
SEQRES 8 A 563 ARG ASP SER SER VAL ASP GLU THR ASP VAL PHE ASP PHE
SEQRES 9 A 563 HIS THR GLY ARG ALA GLU LEU LEU GLU ILE ILE LYS GLU
SEQRES 10 A 563 ILE ASN ARG THR CYS HIS ASP SER ARG ASP MET ALA ALA
SEQRES 11 A 563 LYS GLY GLU ARG GLU LYS TRP TRP ALA GLU ARG GLU ALA
SEQRES 12 A 563 LEU ASP GLN ARG LEU LYS GLU LEU LEU MET ASN ILE GLU
SEQRES 13 A 563 HIS VAL TRP LEU GLY GLY PHE ARG GLY VAL PHE SER GLN
SEQRES 14 A 563 HIS GLY ARG ARG PRO GLU LEU LEU GLU LYS PHE ARG ALA
SEQRES 15 A 563 MET PHE GLU GLY VAL LEU ASP LYS HIS LEU PRO SER ARG
SEQRES 16 A 563 ARG GLN VAL GLY ARG GLY LYS LYS GLY LYS GLY VAL ALA
SEQRES 17 A 563 GLY GLN THR LYS VAL VAL LEU ASP GLY ASN VAL LEU GLU
SEQRES 18 A 563 LEU PHE ILE GLY LEU GLY ASP ALA THR LYS SER GLY ALA
SEQRES 19 A 563 ASP PHE ASP GLU GLU LEU THR ASP LEU LEU TYR PHE VAL
SEQRES 20 A 563 VAL ASP ILE LEU GLN PHE HIS GLY GLU ARG ASN ALA TYR
SEQRES 21 A 563 ASP GLU ILE ASP PHE ASP SER MET VAL VAL GLU THR MET
SEQRES 22 A 563 ASP ALA LEU MET ALA TYR HIS ALA GLU ALA ASN ALA ALA
SEQRES 23 A 563 PRO GLU SER ASP SER HIS ALA HIS THR ILE LEU VAL LEU
SEQRES 24 A 563 ASP LYS GLN LEU HIS VAL PHE PRO TRP GLU SER LEU PRO
SEQRES 25 A 563 CYS LEU GLN GLY LEU ALA VAL SER ARG ILE PRO SER LEU
SEQRES 26 A 563 ALA CYS LEU ARG LYS LEU LEU LEU ASP ARG ARG ARG SER
SEQRES 27 A 563 SER SER GLN ILE GLN GLY GLU ASP SER GLU GLU GLU ASP
SEQRES 28 A 563 PRO ARG SER ALA GLY HIS HIS ALA PRO LEU SER GLY GLY
SEQRES 29 A 563 THR TYR ILE LEU ASN PRO SER SER ASP LEU LEU SER THR
SEQRES 30 A 563 GLN LYS THR PHE GLU SER LEU PHE SER THR HIS LEU HIS
SEQRES 31 A 563 SER PRO ASN SER TRP THR ARG ILE ILE SER ARG PRO PRO
SEQRES 32 A 563 THR GLU PRO GLU PHE LEU SER ALA LEU THR HIS SER PRO
SEQRES 33 A 563 ILE LEU LEU TYR PHE GLY HIS GLY SER GLY ALA GLN TYR
SEQRES 34 A 563 ILE ARG SER ARG ASN ILE ARG HIS LEU ASP HIS CYS ARG
SEQRES 35 A 563 ALA THR VAL LEU LEU MET GLY CYS SER SER ALA ALA LEU
SEQRES 36 A 563 THR ALA LYS GLY GLU PHE GLU PRO SER GLY PRO VAL TRP
SEQRES 37 A 563 ASN TYR MET LEU ALA GLY ALA PRO ALA VAL VAL GLY THR
SEQRES 38 A 563 LEU TRP ASP VAL THR ASP ARG ASP ILE ASP ARG PHE ALA
SEQRES 39 A 563 GLY GLY VAL LEU GLU GLY TRP GLY VAL LEU PRO GLU GLY
SEQRES 40 A 563 CYS MET GLY GLU LYS ASN GLY LYS LYS LYS ALA GLY ARG
SEQRES 41 A 563 ASN GLY LEU SER LEU VAL GLN ALA VAL ALA LYS ALA ARG
SEQRES 42 A 563 ASP ARG CYS ARG PHE ARG TYR VAL THR ALA ALA ALA ALA
SEQRES 43 A 563 VAL VAL TYR GLY ILE PRO VAL TYR VAL ASP VAL ASP GLY
SEQRES 44 A 563 LYS SER LYS ASP
SEQRES 1 B 26 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER GLN LEU
SEQRES 2 B 26 GLU VAL LEU PHE GLN GLY PRO LEU GLY SER GLY ARG PRO
FORMUL 3 HOH *394(H2 O)
HELIX 1 AA1 SER A 1692 TYR A 1706 1 15
HELIX 2 AA2 ILE A 1707 VAL A 1710 5 4
HELIX 3 AA3 ASP A 1763 ASP A 1784 1 22
HELIX 4 AA4 ASP A 1784 LYS A 1791 1 8
HELIX 5 AA5 GLU A 1793 TRP A 1819 1 27
HELIX 6 AA6 LEU A 1820 SER A 1828 5 9
HELIX 7 AA7 ARG A 1833 LEU A 1852 1 20
HELIX 8 AA8 ASP A 1876 GLY A 1885 1 10
HELIX 9 AA9 PHE A 1896 HIS A 1914 1 19
HELIX 10 AB1 ALA A 1919 ILE A 1923 5 5
HELIX 11 AB2 ASP A 1924 ALA A 1946 1 23
HELIX 12 AB3 PRO A 1967 LEU A 1971 5 5
HELIX 13 AB4 SER A 1984 ASP A 1994 1 11
HELIX 14 AB5 ASP A 2011 GLY A 2016 5 6
HELIX 15 AB6 LEU A 2034 LEU A 2049 1 16
HELIX 16 AB7 LEU A 2049 SER A 2054 1 6
HELIX 17 AB8 THR A 2064 SER A 2075 1 12
HELIX 18 AB9 ARG A 2091 HIS A 2097 1 7
HELIX 19 AC1 GLY A 2125 GLY A 2134 1 10
HELIX 20 AC2 THR A 2146 TRP A 2161 1 16
HELIX 21 AC3 SER A 2184 ARG A 2193 1 10
HELIX 22 AC4 ASP A 2194 CYS A 2196 5 3
HELIX 23 AC5 THR A 2202 ALA A 2204 5 3
HELIX 24 AC6 LEU B 13 GLN B 18 5 6
SHEET 1 AA1 5 PHE A1740 PRO A1745 0
SHEET 2 AA1 5 ASP A1727 LEU A1733 -1 N ILE A1730 O LEU A1742
SHEET 3 AA1 5 TRP A1714 LEU A1721 -1 N SER A1720 O CYS A1729
SHEET 4 AA1 5 HIS A1954 LEU A1959 1 O ILE A1956 N HIS A1715
SHEET 5 AA1 5 VAL A1979 ARG A1981 1 O SER A1980 N LEU A1957
SHEET 1 AA2 2 HIS A2017 PRO A2020 0
SHEET 2 AA2 2 VAL A2213 ASP A2216 1 O TYR A2214 N HIS A2017
SHEET 1 AA3 6 THR A2056 ILE A2059 0
SHEET 2 AA3 6 THR A2025 LEU A2028 1 N LEU A2028 O ILE A2058
SHEET 3 AA3 6 ILE A2077 PHE A2081 1 O PHE A2081 N ILE A2027
SHEET 4 AA3 6 THR A2104 LEU A2107 1 O THR A2104 N LEU A2078
SHEET 5 AA3 6 ALA A2137 THR A2141 1 O VAL A2139 N LEU A2107
SHEET 6 AA3 6 ALA A2206 GLY A2210 -1 O TYR A2209 N VAL A2138
CISPEP 1 PRO A 1853 SER A 1854 0 -12.35
CRYST1 55.559 98.889 107.747 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 0.017999 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010112 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009281 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
