HEADER IMMUNE SYSTEM 16-MAR-12 4AN8
TITLE STRUCTURE OF THERMUS THERMOPHILUS CASA (CSE1)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CSE1;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES;
COMPND 5 OTHER_DETAILS: TEV PROTEASE SCAR AT N-TERMINUS (GAGS)
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS;
SOURCE 3 ORGANISM_TAXID: 300852;
SOURCE 4 STRAIN: HB8;
SOURCE 5 ATCC: 27634;
SOURCE 6 GENE: TTHB188;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PSV272 (PET VECTOR WITH ADDED TEV
SOURCE 11 PROTEASE SITE)
KEYWDS IMMUNE SYSTEM, CRISPR, CASCADE, CASA
EXPDTA X-RAY DIFFRACTION
AUTHOR D.G.SASHITAL,B.WIEDENHEFT,J.A.DOUDNA
REVDAT 2 20-JUN-12 4AN8 1 JRNL
REVDAT 1 02-MAY-12 4AN8 0
JRNL AUTH D.G.SASHITAL,B.WIEDENHEFT,J.A.DOUDNA
JRNL TITL MECHANISM OF FOREIGN DNA SELECTION IN A BACTERIAL ADAPTIVE
JRNL TITL 2 IMMUNE SYSTEM.
JRNL REF MOL.CELL V. 46 606 2012
JRNL REFN ISSN 1097-2765
JRNL PMID 22521690
JRNL DOI 10.1016/J.MOLCEL.2012.03.020
REMARK 2
REMARK 2 RESOLUTION. 2.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VICENT 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) : 2.300
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 46.825
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.99
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.59
REMARK 3 NUMBER OF REFLECTIONS : 51896
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.1984
REMARK 3 R VALUE (WORKING SET) : 0.1959
REMARK 3 FREE R VALUE : 0.2472
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.0
REMARK 3 FREE R VALUE TEST SET COUNT : 2594
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 46.8348 - 6.1329 0.99 2739 144 0.2038 0.2350
REMARK 3 2 6.1329 - 4.8695 1.00 2643 139 0.1901 0.2493
REMARK 3 3 4.8695 - 4.2545 1.00 2641 139 0.1604 0.2051
REMARK 3 4 4.2545 - 3.8657 1.00 2618 138 0.1701 0.2264
REMARK 3 5 3.8657 - 3.5887 1.00 2611 137 0.1755 0.2159
REMARK 3 6 3.5887 - 3.3772 1.00 2588 136 0.1893 0.2386
REMARK 3 7 3.3772 - 3.2081 1.00 2582 136 0.1821 0.2249
REMARK 3 8 3.2081 - 3.0685 1.00 2630 139 0.1895 0.2214
REMARK 3 9 3.0685 - 2.9504 1.00 2565 135 0.2006 0.2544
REMARK 3 10 2.9504 - 2.8486 1.00 2594 136 0.2147 0.3041
REMARK 3 11 2.8486 - 2.7595 1.00 2607 137 0.2198 0.2902
REMARK 3 12 2.7595 - 2.6806 1.00 2557 135 0.2219 0.2997
REMARK 3 13 2.6806 - 2.6101 1.00 2607 137 0.2279 0.3013
REMARK 3 14 2.6101 - 2.5464 1.00 2552 135 0.2301 0.2764
REMARK 3 15 2.5464 - 2.4885 1.00 2595 136 0.2294 0.3019
REMARK 3 16 2.4885 - 2.4356 1.00 2587 136 0.2312 0.2667
REMARK 3 17 2.4356 - 2.3868 1.00 2571 136 0.2374 0.2821
REMARK 3 18 2.3868 - 2.3418 1.00 2582 135 0.2426 0.3089
REMARK 3 19 2.3418 - 2.3000 0.96 2433 128 0.2538 0.3107
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.30
REMARK 3 SHRINKAGE RADIUS : 1.06
REMARK 3 K_SOL : 0.372
REMARK 3 B_SOL : 48.448
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.67
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 23.33
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 36.16
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 44.40
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.2968
REMARK 3 B22 (A**2) : 0.7999
REMARK 3 B33 (A**2) : -1.0967
REMARK 3 B12 (A**2) : 0.0000
REMARK 3 B13 (A**2) : 1.0220
REMARK 3 B23 (A**2) : 0.0000
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 : 0.009 7517
REMARK 3 ANGLE : 1.119 10206
REMARK 3 CHIRALITY : 0.075 1102
REMARK 3 PLANARITY : 0.006 1346
REMARK 3 DIHEDRAL : 14.186 2842
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: CHAIN A RESIDUES 1-3, 130-143,
REMARK 3 401-411 AND 497-502 ARE DISORDERED. CHAIN B RESIDUES 1-4,
REMARK 3 129-143, 401-423 AND 494-502 ARE DISORDERED
REMARK 4
REMARK 4 4AN8 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 16-MAR-12.
REMARK 100 THE PDBE ID CODE IS EBI-51708.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 27-MAR-11
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 8.3.1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.11587
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 51896
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.30
REMARK 200 RESOLUTION RANGE LOW (A) : 46.83
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.5
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 200 DATA REDUNDANCY : 3.9
REMARK 200 R MERGE (I) : 0.06
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 18.90
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.36
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.8
REMARK 200 DATA REDUNDANCY IN SHELL : 3.6
REMARK 200 R MERGE FOR SHELL (I) : 0.46
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.90
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD
REMARK 200 SOFTWARE USED: AUTOSHARP
REMARK 200 STARTING MODEL: NONE
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 53
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.6
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 2.1M NAAC, MES PH 6.5
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 24.05500
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
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 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 GLY A -3
REMARK 465 ALA A -2
REMARK 465 GLY A -1
REMARK 465 SER A 0
REMARK 465 MET A 1
REMARK 465 GLY A 2
REMARK 465 SER A 3
REMARK 465 SER A 130
REMARK 465 GLY A 131
REMARK 465 ASN A 132
REMARK 465 ASN A 133
REMARK 465 PRO A 134
REMARK 465 THR A 135
REMARK 465 LEU A 136
REMARK 465 PHE A 137
REMARK 465 ASP A 138
REMARK 465 HIS A 139
REMARK 465 THR A 140
REMARK 465 THR A 141
REMARK 465 GLU A 142
REMARK 465 GLU A 143
REMARK 465 GLY A 401
REMARK 465 GLU A 402
REMARK 465 ARG A 403
REMARK 465 ASP A 404
REMARK 465 ARG A 405
REMARK 465 GLY A 406
REMARK 465 HIS A 407
REMARK 465 GLY A 408
REMARK 465 ARG A 409
REMARK 465 SER A 410
REMARK 465 PRO A 411
REMARK 465 GLY A 497
REMARK 465 GLU A 498
REMARK 465 GLU A 499
REMARK 465 VAL A 500
REMARK 465 ARG A 501
REMARK 465 THR A 502
REMARK 465 GLY B -3
REMARK 465 ALA B -2
REMARK 465 GLY B -1
REMARK 465 SER B 0
REMARK 465 MET B 1
REMARK 465 GLY B 2
REMARK 465 SER B 3
REMARK 465 LEU B 4
REMARK 465 ALA B 129
REMARK 465 SER B 130
REMARK 465 GLY B 131
REMARK 465 ASN B 132
REMARK 465 ASN B 133
REMARK 465 PRO B 134
REMARK 465 THR B 135
REMARK 465 LEU B 136
REMARK 465 PHE B 137
REMARK 465 ASP B 138
REMARK 465 HIS B 139
REMARK 465 THR B 140
REMARK 465 THR B 141
REMARK 465 GLU B 142
REMARK 465 GLU B 143
REMARK 465 GLY B 401
REMARK 465 GLU B 402
REMARK 465 ARG B 403
REMARK 465 ASP B 404
REMARK 465 ARG B 405
REMARK 465 GLY B 406
REMARK 465 HIS B 407
REMARK 465 GLY B 408
REMARK 465 ARG B 409
REMARK 465 SER B 410
REMARK 465 PRO B 411
REMARK 465 TYR B 412
REMARK 465 LEU B 413
REMARK 465 GLU B 414
REMARK 465 GLU B 415
REMARK 465 LEU B 416
REMARK 465 THR B 417
REMARK 465 LYS B 418
REMARK 465 LEU B 419
REMARK 465 ALA B 420
REMARK 465 ASN B 421
REMARK 465 SER B 422
REMARK 465 LEU B 423
REMARK 465 GLY B 494
REMARK 465 GLU B 495
REMARK 465 LEU B 496
REMARK 465 GLY B 497
REMARK 465 GLU B 498
REMARK 465 GLU B 499
REMARK 465 VAL B 500
REMARK 465 ARG B 501
REMARK 465 THR B 502
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 OD2 ASP A 11 NH1A ARG A 95 2.11
REMARK 500 OE1 GLU A 25 O HOH A 2017 2.16
REMARK 500 OE1 GLU A 49 NH1 ARG A 356 2.00
REMARK 500 OE1 GLN A 84 O HOH A 2062 2.18
REMARK 500 NE ARG A 88 O HOH A 2063 2.16
REMARK 500 OE2 GLU A 115 O HOH A 2090 1.84
REMARK 500 N LEU A 128 O HOH A 2097 2.04
REMARK 500 O ASP A 210 O HOH A 2125 2.19
REMARK 500 OD1 ASP A 353 O HOH A 2196 2.18
REMARK 500 O GLU A 414 OG1 THR A 417 2.10
REMARK 500 NH1 ARG A 439 O HOH A 2208 2.13
REMARK 500 OD2 ASP B 11 NH1 ARG B 95 2.18
REMARK 500 N GLY B 364 O HOH B 2123 2.14
REMARK 500 O GLU B 446 OG SER B 449 2.13
REMARK 500 O HOH A 2003 O HOH A 2004 1.94
REMARK 500 O HOH A 2008 O HOH A 2015 2.16
REMARK 500 O HOH A 2011 O HOH A 2030 1.99
REMARK 500 O HOH A 2055 O HOH A 2123 1.90
REMARK 500 O HOH A 2064 O HOH A 2133 1.99
REMARK 500 O HOH A 2073 O HOH A 2077 1.92
REMARK 500 O HOH A 2092 O HOH A 2093 2.08
REMARK 500 O HOH A 2125 O HOH A 2138 2.13
REMARK 500 O HOH A 2162 O HOH A 2167 2.08
REMARK 500 O HOH A 2174 O HOH A 2197 2.07
REMARK 500 O HOH B 2011 O HOH B 2012 2.06
REMARK 500 O HOH B 2018 O HOH B 2019 1.92
REMARK 500 O HOH B 2027 O HOH B 2065 1.99
REMARK 500 O HOH B 2034 O HOH B 2036 2.08
REMARK 500 O HOH B 2052 O HOH B 2114 1.91
REMARK 500 O HOH B 2064 O HOH B 2128 2.05
REMARK 500 O HOH B 2088 O HOH B 2097 2.04
REMARK 500 O HOH B 2100 O HOH B 2101 2.07
REMARK 500 O HOH B 2121 O HOH B 2122 2.08
REMARK 500 O HOH B 2124 O HOH B 2134 2.15
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 PHE A 7 75.27 63.63
REMARK 500 TRP A 14 -13.99 -150.77
REMARK 500 ALA A 105 55.93 -142.54
REMARK 500 LEU A 169 -56.04 -131.55
REMARK 500 ASP A 255 22.54 -142.10
REMARK 500 GLN A 348 -133.77 50.98
REMARK 500 LEU A 413 -16.88 -47.47
REMARK 500 PHE B 7 78.96 66.31
REMARK 500 TRP B 14 -7.82 -154.77
REMARK 500 SER B 65 50.15 39.68
REMARK 500 ALA B 105 51.55 -144.77
REMARK 500 TYR B 172 47.19 38.48
REMARK 500 ALA B 212 133.03 -173.30
REMARK 500 HIS B 273 121.46 -23.74
REMARK 500 GLN B 348 -126.57 47.09
REMARK 500 GLU B 445 24.57 -78.35
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 ACT A1497
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A1498
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT B1494
DBREF 4AN8 A 1 502 UNP Q53VY1 Q53VY1_THET8 1 502
DBREF 4AN8 B 1 502 UNP Q53VY1 Q53VY1_THET8 1 502
SEQADV 4AN8 GLY A -3 UNP Q53VY1 EXPRESSION TAG
SEQADV 4AN8 ALA A -2 UNP Q53VY1 EXPRESSION TAG
SEQADV 4AN8 GLY A -1 UNP Q53VY1 EXPRESSION TAG
SEQADV 4AN8 SER A 0 UNP Q53VY1 EXPRESSION TAG
SEQADV 4AN8 GLY B -3 UNP Q53VY1 EXPRESSION TAG
SEQADV 4AN8 ALA B -2 UNP Q53VY1 EXPRESSION TAG
SEQADV 4AN8 GLY B -1 UNP Q53VY1 EXPRESSION TAG
SEQADV 4AN8 SER B 0 UNP Q53VY1 EXPRESSION TAG
SEQRES 1 A 506 GLY ALA GLY SER MET GLY SER LEU GLU LYS PHE ASN LEU
SEQRES 2 A 506 ILE ASP GLU PRO TRP ILE PRO VAL LEU LYS GLY GLY ARG
SEQRES 3 A 506 VAL VAL GLU VAL GLY ILE GLY GLU ALA LEU LEU ARG ALA
SEQRES 4 A 506 HIS GLU PHE ALA ARG ILE GLU THR PRO SER PRO LEU GLU
SEQRES 5 A 506 GLU ALA VAL LEU HIS ARG LEU LEU LEU ALA VAL LEU HIS
SEQRES 6 A 506 ARG ALA LEU SER GLY PRO ARG CYS PRO GLU ASP VAL LEU
SEQRES 7 A 506 ASP TRP TRP ARG LYS GLY GLY PHE PRO GLN ASP PRO ILE
SEQRES 8 A 506 ARG ASP TYR LEU ASN ARG PHE ARG ASP ARG PHE PHE LEU
SEQRES 9 A 506 PHE HIS PRO GLU ALA PRO PHE LEU GLN VAL ALA ASP LEU
SEQRES 10 A 506 PRO GLU GLU ASN PRO LEU PRO TRP SER LYS LEU LEU PRO
SEQRES 11 A 506 GLU LEU ALA SER GLY ASN ASN PRO THR LEU PHE ASP HIS
SEQRES 12 A 506 THR THR GLU GLU ASN LEU PRO LYS ALA THR TYR ALA GLN
SEQRES 13 A 506 ALA ALA ARG ALA LEU LEU VAL HIS GLN ALA PHE ALA PRO
SEQRES 14 A 506 GLY GLY LEU LEU ARG ARG TYR GLY VAL GLY SER ALA LYS
SEQRES 15 A 506 ASP ALA PRO VAL ALA ARG PRO ALA LEU PHE LEU PRO THR
SEQRES 16 A 506 GLY GLN ASN LEU LEU GLU THR LEU LEU LEU ASN LEU VAL
SEQRES 17 A 506 PRO TYR THR PRO GLU ASP ASP ALA PRO ILE TRP GLU VAL
SEQRES 18 A 506 PRO PRO LEU ARG LEU GLY ASP LEU GLU GLY ALA ARG THR
SEQRES 19 A 506 LYS TRP PRO LEU THR GLY ARG THR ARG VAL TYR THR TRP
SEQRES 20 A 506 PRO ALA ARG GLY VAL ARG LEU LEU ASP GLU GLY ASP GLY
SEQRES 21 A 506 VAL ARG PHE MET GLY TYR GLY PRO GLY VAL GLU PRO LEU
SEQRES 22 A 506 GLU ALA THR HIS ARG ASP PRO MET VAL ALA GLN ARG LEU
SEQRES 23 A 506 ASP ALA LYS GLY ASN LEU LEU VAL LEU ARG LEU SER GLU
SEQRES 24 A 506 GLU ARG SER PHE TRP ARG ASP PHE SER ALA MET LEU PRO
SEQRES 25 A 506 ARG GLN GLY GLY LYS VAL ALA ALA THR LEU GLU HIS ALA
SEQRES 26 A 506 GLU ASN LEU GLN GLY GLU LEU GLU ASP GLU GLY LEU GLU
SEQRES 27 A 506 GLY ARG ILE THR LEU ARG VAL LEU GLY GLN VAL SER ASP
SEQRES 28 A 506 GLN ALA LYS VAL LEU ASP ILE ARG ARG GLU VAL TYR PRO
SEQRES 29 A 506 LEU PRO SER GLY LEU LEU THR PRO LYS ALA GLU GLU ASN
SEQRES 30 A 506 LEU GLU LYS ALA LEU LYS MET ALA GLU GLU LEU GLY GLN
SEQRES 31 A 506 GLY LEU LYS HIS LEU ALA GLN GLU VAL ALA LYS ALA VAL
SEQRES 32 A 506 VAL GLY GLU ARG ASP ARG GLY HIS GLY ARG SER PRO TYR
SEQRES 33 A 506 LEU GLU GLU LEU THR LYS LEU ALA ASN SER LEU PRO LEU
SEQRES 34 A 506 GLU ARG LEU TYR TRP HIS ALA LEU ASP GLY ALA PHE PRO
SEQRES 35 A 506 ARG PHE PHE ALA ARG VAL GLU GLU GLU ALA SER LEU ASP
SEQRES 36 A 506 LEU TRP ARG GLU ALA LEU ARG GLY ALA ALA LEU GLU ALA
SEQRES 37 A 506 TRP LYS ALA THR ARG ARG PHE LEU GLY THR GLY ALA ARG
SEQRES 38 A 506 HIS LEU LYS ALA LEU ALA GLN GLY GLU GLN GLU PHE GLY
SEQRES 39 A 506 ARG LEU LEU GLY GLU LEU GLY GLU GLU VAL ARG THR
SEQRES 1 B 506 GLY ALA GLY SER MET GLY SER LEU GLU LYS PHE ASN LEU
SEQRES 2 B 506 ILE ASP GLU PRO TRP ILE PRO VAL LEU LYS GLY GLY ARG
SEQRES 3 B 506 VAL VAL GLU VAL GLY ILE GLY GLU ALA LEU LEU ARG ALA
SEQRES 4 B 506 HIS GLU PHE ALA ARG ILE GLU THR PRO SER PRO LEU GLU
SEQRES 5 B 506 GLU ALA VAL LEU HIS ARG LEU LEU LEU ALA VAL LEU HIS
SEQRES 6 B 506 ARG ALA LEU SER GLY PRO ARG CYS PRO GLU ASP VAL LEU
SEQRES 7 B 506 ASP TRP TRP ARG LYS GLY GLY PHE PRO GLN ASP PRO ILE
SEQRES 8 B 506 ARG ASP TYR LEU ASN ARG PHE ARG ASP ARG PHE PHE LEU
SEQRES 9 B 506 PHE HIS PRO GLU ALA PRO PHE LEU GLN VAL ALA ASP LEU
SEQRES 10 B 506 PRO GLU GLU ASN PRO LEU PRO TRP SER LYS LEU LEU PRO
SEQRES 11 B 506 GLU LEU ALA SER GLY ASN ASN PRO THR LEU PHE ASP HIS
SEQRES 12 B 506 THR THR GLU GLU ASN LEU PRO LYS ALA THR TYR ALA GLN
SEQRES 13 B 506 ALA ALA ARG ALA LEU LEU VAL HIS GLN ALA PHE ALA PRO
SEQRES 14 B 506 GLY GLY LEU LEU ARG ARG TYR GLY VAL GLY SER ALA LYS
SEQRES 15 B 506 ASP ALA PRO VAL ALA ARG PRO ALA LEU PHE LEU PRO THR
SEQRES 16 B 506 GLY GLN ASN LEU LEU GLU THR LEU LEU LEU ASN LEU VAL
SEQRES 17 B 506 PRO TYR THR PRO GLU ASP ASP ALA PRO ILE TRP GLU VAL
SEQRES 18 B 506 PRO PRO LEU ARG LEU GLY ASP LEU GLU GLY ALA ARG THR
SEQRES 19 B 506 LYS TRP PRO LEU THR GLY ARG THR ARG VAL TYR THR TRP
SEQRES 20 B 506 PRO ALA ARG GLY VAL ARG LEU LEU ASP GLU GLY ASP GLY
SEQRES 21 B 506 VAL ARG PHE MET GLY TYR GLY PRO GLY VAL GLU PRO LEU
SEQRES 22 B 506 GLU ALA THR HIS ARG ASP PRO MET VAL ALA GLN ARG LEU
SEQRES 23 B 506 ASP ALA LYS GLY ASN LEU LEU VAL LEU ARG LEU SER GLU
SEQRES 24 B 506 GLU ARG SER PHE TRP ARG ASP PHE SER ALA MET LEU PRO
SEQRES 25 B 506 ARG GLN GLY GLY LYS VAL ALA ALA THR LEU GLU HIS ALA
SEQRES 26 B 506 GLU ASN LEU GLN GLY GLU LEU GLU ASP GLU GLY LEU GLU
SEQRES 27 B 506 GLY ARG ILE THR LEU ARG VAL LEU GLY GLN VAL SER ASP
SEQRES 28 B 506 GLN ALA LYS VAL LEU ASP ILE ARG ARG GLU VAL TYR PRO
SEQRES 29 B 506 LEU PRO SER GLY LEU LEU THR PRO LYS ALA GLU GLU ASN
SEQRES 30 B 506 LEU GLU LYS ALA LEU LYS MET ALA GLU GLU LEU GLY GLN
SEQRES 31 B 506 GLY LEU LYS HIS LEU ALA GLN GLU VAL ALA LYS ALA VAL
SEQRES 32 B 506 VAL GLY GLU ARG ASP ARG GLY HIS GLY ARG SER PRO TYR
SEQRES 33 B 506 LEU GLU GLU LEU THR LYS LEU ALA ASN SER LEU PRO LEU
SEQRES 34 B 506 GLU ARG LEU TYR TRP HIS ALA LEU ASP GLY ALA PHE PRO
SEQRES 35 B 506 ARG PHE PHE ALA ARG VAL GLU GLU GLU ALA SER LEU ASP
SEQRES 36 B 506 LEU TRP ARG GLU ALA LEU ARG GLY ALA ALA LEU GLU ALA
SEQRES 37 B 506 TRP LYS ALA THR ARG ARG PHE LEU GLY THR GLY ALA ARG
SEQRES 38 B 506 HIS LEU LYS ALA LEU ALA GLN GLY GLU GLN GLU PHE GLY
SEQRES 39 B 506 ARG LEU LEU GLY GLU LEU GLY GLU GLU VAL ARG THR
HET ACT A1497 4
HET ACT A1498 4
HET ACT B1494 4
HETNAM ACT ACETATE ION
FORMUL 3 ACT 3(C2 H3 O2 1-)
FORMUL 4 HOH *348(H2 O)
HELIX 1 1 GLY A 27 ARG A 34 1 8
HELIX 2 2 ALA A 35 PHE A 38 5 4
HELIX 3 3 SER A 45 LEU A 64 1 20
HELIX 4 4 CYS A 69 GLY A 80 1 12
HELIX 5 5 PRO A 83 ARG A 95 1 13
HELIX 6 6 SER A 122 LEU A 125 5 4
HELIX 7 7 THR A 149 ALA A 164 1 16
HELIX 8 8 ASN A 194 LEU A 203 1 10
HELIX 9 9 PRO A 213 VAL A 217 5 5
HELIX 10 10 ARG A 221 GLU A 226 1 6
HELIX 11 11 GLY A 227 ARG A 229 5 3
HELIX 12 12 GLY A 236 THR A 242 1 7
HELIX 13 13 SER A 298 PHE A 303 5 6
HELIX 14 14 LEU A 307 GLY A 311 5 5
HELIX 15 15 ALA A 315 ASP A 330 1 16
HELIX 16 16 THR A 367 VAL A 400 1 34
HELIX 17 17 TYR A 412 LEU A 423 1 12
HELIX 18 18 PRO A 424 ARG A 443 1 20
HELIX 19 19 ALA A 448 GLY A 473 1 26
HELIX 20 20 HIS A 478 LEU A 496 1 19
HELIX 21 21 GLY B 27 ARG B 34 1 8
HELIX 22 22 ALA B 35 PHE B 38 5 4
HELIX 23 23 SER B 45 LEU B 64 1 20
HELIX 24 24 CYS B 69 GLY B 80 1 12
HELIX 25 25 PRO B 83 ARG B 95 1 13
HELIX 26 26 SER B 122 LEU B 124 5 3
HELIX 27 27 THR B 149 ALA B 164 1 16
HELIX 28 28 ASN B 194 LEU B 203 1 10
HELIX 29 29 PRO B 213 VAL B 217 5 5
HELIX 30 30 ARG B 221 GLU B 226 1 6
HELIX 31 31 GLY B 227 ARG B 229 5 3
HELIX 32 32 GLY B 236 THR B 242 1 7
HELIX 33 33 SER B 298 PHE B 303 5 6
HELIX 34 34 LEU B 307 GLY B 311 5 5
HELIX 35 35 ALA B 315 GLU B 331 1 17
HELIX 36 36 THR B 367 VAL B 400 1 34
HELIX 37 37 PRO B 424 ALA B 442 1 19
HELIX 38 38 GLU B 447 GLY B 473 1 27
HELIX 39 39 THR B 474 ARG B 477 5 4
HELIX 40 40 HIS B 478 LEU B 493 1 16
SHEET 1 AA 2 LYS A 6 ASN A 8 0
SHEET 2 AA 2 PHE A 99 PHE A 101 -1 N LEU A 100 O PHE A 7
SHEET 1 AB 3 ARG A 22 VAL A 26 0
SHEET 2 AB 3 ILE A 15 LYS A 19 -1 O ILE A 15 N VAL A 26
SHEET 3 AB 3 ARG A 40 ILE A 41 -1 O ARG A 40 N LEU A 18
SHEET 1 AC 3 LEU A 119 PRO A 120 0
SHEET 2 AC 3 VAL A 257 PRO A 264 -1 O MET A 260 N LEU A 119
SHEET 3 AC 3 ARG A 246 ASP A 252 -1 O GLY A 247 N GLY A 263
SHEET 1 AD 2 GLY A 167 ARG A 171 0
SHEET 2 AD 2 VAL A 174 ALA A 177 -1 O VAL A 174 N ARG A 171
SHEET 1 AE 3 LEU A 187 THR A 191 0
SHEET 2 AE 3 THR A 338 ASP A 347 -1 O THR A 338 N THR A 191
SHEET 3 AE 3 LYS A 350 PRO A 360 -1 O LYS A 350 N ASP A 347
SHEET 1 AF 2 LYS A 231 PRO A 233 0
SHEET 2 AF 2 GLU A 267 LEU A 269 1 O GLU A 267 N TRP A 232
SHEET 1 AG 2 GLN A 280 LEU A 282 0
SHEET 2 AG 2 LEU A 288 VAL A 290 -1 O LEU A 289 N ARG A 281
SHEET 1 BA 2 LYS B 6 ASN B 8 0
SHEET 2 BA 2 PHE B 99 PHE B 101 -1 N LEU B 100 O PHE B 7
SHEET 1 BB 3 ARG B 22 VAL B 26 0
SHEET 2 BB 3 ILE B 15 LYS B 19 -1 O ILE B 15 N VAL B 26
SHEET 3 BB 3 ARG B 40 ILE B 41 -1 O ARG B 40 N LEU B 18
SHEET 1 BC 3 LEU B 119 PRO B 120 0
SHEET 2 BC 3 VAL B 257 PRO B 264 -1 O MET B 260 N LEU B 119
SHEET 3 BC 3 ARG B 246 ASP B 252 -1 O GLY B 247 N GLY B 263
SHEET 1 BD 2 GLY B 167 ARG B 171 0
SHEET 2 BD 2 VAL B 174 ALA B 177 -1 O VAL B 174 N ARG B 171
SHEET 1 BE 3 LEU B 187 THR B 191 0
SHEET 2 BE 3 THR B 338 ASP B 347 -1 O THR B 338 N THR B 191
SHEET 3 BE 3 LYS B 350 PRO B 360 -1 O LYS B 350 N ASP B 347
SHEET 1 BF 2 LYS B 231 PRO B 233 0
SHEET 2 BF 2 GLU B 267 LEU B 269 1 O GLU B 267 N TRP B 232
SHEET 1 BG 2 GLN B 280 LEU B 282 0
SHEET 2 BG 2 LEU B 288 VAL B 290 -1 O LEU B 289 N ARG B 281
SSBOND 1 CYS A 69 CYS B 69 1555 1565 2.04
CISPEP 1 GLY A 66 PRO A 67 0 2.35
CISPEP 2 PRO A 264 GLY A 265 0 16.35
CISPEP 3 GLY B 66 PRO B 67 0 4.14
CISPEP 4 GLU B 334 GLY B 335 0 -4.03
SITE 1 AC1 4 LEU A 124 PRO A 126 HIS A 160 GLN A 344
SITE 1 AC2 7 LYS A 123 PRO A 165 GLY A 167 LEU A 168
SITE 2 AC2 7 ARG A 246 TYR A 262 HOH A2105
SITE 1 AC3 5 LYS B 123 PRO B 165 GLY B 167 ARG B 246
SITE 2 AC3 5 TYR B 262
CRYST1 94.360 48.110 129.780 90.00 97.03 90.00 P 1 21 1 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 0.010598 0.000000 0.001307 0.00000
SCALE2 0.000000 0.020786 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007764 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
