HEADER STRUCTURAL PROTEIN 21-OCT-09 3KCP
TITLE CRYSTAL STRUCTURE OF INTERACTING CLOSTRIDIUM THERMOCELLUM MULTIMODULAR
TITLE 2 COMPONENTS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CELLULOSOMAL-SCAFFOLDING PROTEIN A;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: COHESIN 9 AND DOCKERIN 1-2 DOMAINS: UNP RESIDUES 1542-1853;
COMPND 5 SYNONYM: CELLULOSOMAL GLYCOPROTEIN S1/SL, CELLULOSE-INTEGRATING
COMPND 6 PROTEIN A, COHESIN;
COMPND 7 ENGINEERED: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: CELLULOSOME ANCHORING PROTEIN, COHESIN REGION;
COMPND 10 CHAIN: B;
COMPND 11 FRAGMENT: UNP RESIDUES 27-200;
COMPND 12 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: CLOSTRIDIUM THERMOCELLUM ATCC 27405;
SOURCE 3 ORGANISM_TAXID: 203119;
SOURCE 4 STRAIN: ATCC 27405 / DSM 1237;
SOURCE 5 GENE: CIPA, CTHE_3077;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 MOL_ID: 2;
SOURCE 9 ORGANISM_SCIENTIFIC: CLOSTRIDIUM THERMOCELLUM ATCC 27405;
SOURCE 10 ORGANISM_TAXID: 203119;
SOURCE 11 STRAIN: ATCC 27405 / DSM 1237;
SOURCE 12 GENE: CTHE_1307, SDBA;
SOURCE 13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 14 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS COHESIN, DOCKERIN, X-MODULE, CELLULOSOME, CARBOHYDRATE METABOLISM,
KEYWDS 2 CELL WALL BIOGENESIS/DEGRADATION, CELLULOSE DEGRADATION,
KEYWDS 3 GLYCOPROTEIN, POLYSACCHARIDE DEGRADATION, SECRETED, STRUCTURAL
KEYWDS 4 PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR J.J.ADAMS,M.A.CURRIE,E.A.BAYER,Z.JIA,S.P.SMITH
REVDAT 3 21-FEB-24 3KCP 1 REMARK SEQADV LINK
REVDAT 2 02-MAR-10 3KCP 1 JRNL
REVDAT 1 09-FEB-10 3KCP 0
JRNL AUTH J.J.ADAMS,M.A.CURRIE,S.ALI,E.A.BAYER,Z.JIA,S.P.SMITH
JRNL TITL INSIGHTS INTO HIGHER-ORDER ORGANIZATION OF THE CELLULOSOME
JRNL TITL 2 REVEALED BY A DISSECT-AND-BUILD APPROACH: CRYSTAL STRUCTURE
JRNL TITL 3 OF INTERACTING CLOSTRIDIUM THERMOCELLUM MULTIMODULAR
JRNL TITL 4 COMPONENTS
JRNL REF J.MOL.BIOL. V. 396 833 2010
JRNL REFN ISSN 0022-2836
JRNL PMID 20070943
JRNL DOI 10.1016/J.JMB.2010.01.015
REMARK 2
REMARK 2 RESOLUTION. 1.94 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0005
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD WITH PHASES
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.94
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 42.49
REMARK 3 DATA CUTOFF (SIGMA(F)) : 1.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.7
REMARK 3 NUMBER OF REFLECTIONS : 39350
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.206
REMARK 3 R VALUE (WORKING SET) : 0.206
REMARK 3 FREE R VALUE : 0.231
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2087
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.94
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.99
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2513
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 88.17
REMARK 3 BIN R VALUE (WORKING SET) : 0.2530
REMARK 3 BIN FREE R VALUE SET COUNT : 149
REMARK 3 BIN FREE R VALUE : 0.2910
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3542
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 3
REMARK 3 SOLVENT ATOMS : 244
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 34.77
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.07000
REMARK 3 B22 (A**2) : -0.04000
REMARK 3 B33 (A**2) : -0.03000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.161
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.142
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.105
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.656
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.954
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.945
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3609 ; 0.019 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4907 ; 1.679 ; 1.967
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 464 ; 6.333 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 152 ;37.213 ;25.724
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 592 ;14.674 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 10 ;17.625 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 571 ; 0.113 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2719 ; 0.007 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1630 ; 0.213 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 2512 ; 0.314 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 263 ; 0.166 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): 7 ; 0.123 ; 0.200
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 58 ; 0.231 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 15 ; 0.150 ; 0.200
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 2366 ; 1.145 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3742 ; 1.792 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1405 ; 2.863 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1165 ; 4.207 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 3KCP COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-OCT-09.
REMARK 100 THE DEPOSITION ID IS D_1000055826.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 26-JUL-05
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : CHESS
REMARK 200 BEAMLINE : F1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9179
REMARK 200 MONOCHROMATOR : HORIZONTAL BENT SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 270
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 41456
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.940
REMARK 200 RESOLUTION RANGE LOW (A) : 42.490
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.7
REMARK 200 DATA REDUNDANCY : 6.800
REMARK 200 R MERGE (I) : 0.06600
REMARK 200 R SYM (I) : 0.06600
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.94
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.05
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.7
REMARK 200 DATA REDUNDANCY IN SHELL : 5.50
REMARK 200 R MERGE FOR SHELL (I) : 0.42400
REMARK 200 R SYM FOR SHELL (I) : 0.42400
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.200
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
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 (%): 50.93
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.51
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM MES, 200 MM AMMONIUM SULFATE,
REMARK 280 30% W/V PEG 3350, PH 6.5, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 294K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -X+1/2,Y+1/2,-Z
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 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 84.98850
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 29.00950
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 84.98850
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 29.00950
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 300 REMARK: THE BIOLOGICAL ASSEMBLY IS THE ASYMMETRIC UNIT
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: 1760 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 21790 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -13.2 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 MET A 1
REMARK 465 PRO A 2
REMARK 465 THR A 3
REMARK 465 ILE A 4
REMARK 465 THR A 5
REMARK 465 PRO A 6
REMARK 465 ASN A 7
REMARK 465 ASP A 311
REMARK 465 ALA A 312
REMARK 465 GLN A 313
REMARK 465 LEU A 314
REMARK 465 GLU A 315
REMARK 465 HIS A 316
REMARK 465 HIS A 317
REMARK 465 HIS A 318
REMARK 465 HIS A 319
REMARK 465 HIS A 320
REMARK 465 HIS A 321
REMARK 465 MET B 423
REMARK 465 ARG B 424
REMARK 465 GLY B 425
REMARK 465 SER B 426
REMARK 465 HIS B 427
REMARK 465 HIS B 428
REMARK 465 HIS B 429
REMARK 465 HIS B 430
REMARK 465 HIS B 431
REMARK 465 HIS B 432
REMARK 465 THR B 433
REMARK 465 ASP B 434
REMARK 465 LEU B 435
REMARK 465 ARG B 436
REMARK 465 ALA B 437
REMARK 465 ASP B 438
REMARK 465 LYS B 439
REMARK 465 ALA B 440
REMARK 465 LEU B 604
REMARK 465 GLY B 605
REMARK 465 ASP B 606
REMARK 465 GLU B 607
REMARK 465 PRO B 608
REMARK 465 TYR B 609
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 TYR A 310 O HOH A 462 1.64
REMARK 500 O HOH A 463 O HOH A 466 2.11
REMARK 500 O HOH B 223 O HOH B 236 2.13
REMARK 500 NH1 ARG B 504 O LEU B 507 2.15
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 GLU A 89 CB GLU A 89 CG 0.164
REMARK 500 CYS A 269 CB CYS A 269 SG -0.117
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ARG B 449 NE - CZ - NH2 ANGL. DEV. = -4.5 DEGREES
REMARK 500 ARG B 504 NE - CZ - NH1 ANGL. DEV. = -4.5 DEGREES
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 THR A 221 -9.69 82.57
REMARK 500 ASP A 255 19.56 -142.31
REMARK 500 ARG A 287 29.99 48.74
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 702 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 251 OD1
REMARK 620 2 VAL A 253 O 74.1
REMARK 620 3 ASP A 255 OD1 87.5 83.9
REMARK 620 4 SER A 257 O 85.8 154.9 80.3
REMARK 620 5 ASP A 262 OD1 104.2 81.7 158.1 118.5
REMARK 620 6 ASP A 262 OD2 126.8 130.0 134.3 74.3 50.9
REMARK 620 7 HOH A 346 O 154.4 83.4 78.0 111.9 84.0 77.3
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 701 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 284 OD1
REMARK 620 2 ASN A 286 OD1 88.2
REMARK 620 3 ASN A 288 OD1 89.9 76.3
REMARK 620 4 ALA A 290 O 84.6 157.3 82.1
REMARK 620 5 ASP A 295 OD1 95.4 76.7 152.3 125.4
REMARK 620 6 ASP A 295 OD2 107.8 127.2 149.7 75.5 52.5
REMARK 620 7 HOH A 345 O 172.0 87.3 82.6 97.1 90.0 80.2
REMARK 620 N 1 2 3 4 5 6
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 702
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 703
DBREF 3KCP A 2 313 UNP Q06851 CIPA_CLOTH 1542 1853
DBREF 3KCP B 436 609 UNP A3DF10 A3DF10_CLOTH 27 200
SEQADV 3KCP MET A 1 UNP Q06851 EXPRESSION TAG
SEQADV 3KCP LEU A 314 UNP Q06851 EXPRESSION TAG
SEQADV 3KCP GLU A 315 UNP Q06851 EXPRESSION TAG
SEQADV 3KCP HIS A 316 UNP Q06851 EXPRESSION TAG
SEQADV 3KCP HIS A 317 UNP Q06851 EXPRESSION TAG
SEQADV 3KCP HIS A 318 UNP Q06851 EXPRESSION TAG
SEQADV 3KCP HIS A 319 UNP Q06851 EXPRESSION TAG
SEQADV 3KCP HIS A 320 UNP Q06851 EXPRESSION TAG
SEQADV 3KCP HIS A 321 UNP Q06851 EXPRESSION TAG
SEQADV 3KCP MET B 423 UNP A3DF10 EXPRESSION TAG
SEQADV 3KCP ARG B 424 UNP A3DF10 EXPRESSION TAG
SEQADV 3KCP GLY B 425 UNP A3DF10 EXPRESSION TAG
SEQADV 3KCP SER B 426 UNP A3DF10 EXPRESSION TAG
SEQADV 3KCP HIS B 427 UNP A3DF10 EXPRESSION TAG
SEQADV 3KCP HIS B 428 UNP A3DF10 EXPRESSION TAG
SEQADV 3KCP HIS B 429 UNP A3DF10 EXPRESSION TAG
SEQADV 3KCP HIS B 430 UNP A3DF10 EXPRESSION TAG
SEQADV 3KCP HIS B 431 UNP A3DF10 EXPRESSION TAG
SEQADV 3KCP HIS B 432 UNP A3DF10 EXPRESSION TAG
SEQADV 3KCP THR B 433 UNP A3DF10 EXPRESSION TAG
SEQADV 3KCP ASP B 434 UNP A3DF10 EXPRESSION TAG
SEQADV 3KCP LEU B 435 UNP A3DF10 EXPRESSION TAG
SEQRES 1 A 321 MET PRO THR ILE THR PRO ASN LYS LEU THR LEU LYS ILE
SEQRES 2 A 321 GLY ARG ALA GLU GLY ARG PRO GLY ASP THR VAL GLU ILE
SEQRES 3 A 321 PRO VAL ASN LEU TYR GLY VAL PRO GLN LYS GLY ILE ALA
SEQRES 4 A 321 SER GLY ASP PHE VAL VAL SER TYR ASP PRO ASN VAL LEU
SEQRES 5 A 321 GLU ILE ILE GLU ILE GLU PRO GLY GLU LEU ILE VAL ASP
SEQRES 6 A 321 PRO ASN PRO THR LYS SER PHE ASP THR ALA VAL TYR PRO
SEQRES 7 A 321 ASP ARG LYS MET ILE VAL PHE LEU PHE ALA GLU ASP SER
SEQRES 8 A 321 GLY THR GLY ALA TYR ALA ILE THR GLU ASP GLY VAL PHE
SEQRES 9 A 321 ALA THR ILE VAL ALA LYS VAL LYS GLU GLY ALA PRO GLU
SEQRES 10 A 321 GLY PHE SER ALA ILE GLU ILE SER GLU PHE GLY ALA PHE
SEQRES 11 A 321 ALA ASP ASN ASP LEU VAL GLU VAL GLU THR ASP LEU ILE
SEQRES 12 A 321 ASN GLY GLY VAL LEU VAL THR ASN LYS PRO VAL ILE GLU
SEQRES 13 A 321 GLY TYR LYS VAL SER GLY TYR ILE LEU PRO ASP PHE SER
SEQRES 14 A 321 PHE ASP ALA THR VAL ALA PRO LEU VAL LYS ALA GLY PHE
SEQRES 15 A 321 LYS VAL GLU ILE VAL GLY THR GLU LEU TYR ALA VAL THR
SEQRES 16 A 321 ASP ALA ASN GLY TYR PHE GLU ILE THR GLY VAL PRO ALA
SEQRES 17 A 321 ASN ALA SER GLY TYR THR LEU LYS ILE SER ARG ALA THR
SEQRES 18 A 321 TYR LEU ASP ARG VAL ILE ALA ASN VAL VAL VAL THR GLY
SEQRES 19 A 321 ASP THR SER VAL SER THR SER GLN ALA PRO ILE MET MET
SEQRES 20 A 321 TRP VAL GLY ASP ILE VAL LYS ASP ASN SER ILE ASN LEU
SEQRES 21 A 321 LEU ASP VAL ALA GLU VAL ILE ARG CYS PHE ASN ALA THR
SEQRES 22 A 321 LYS GLY SER ALA ASN TYR VAL GLU GLU LEU ASP ILE ASN
SEQRES 23 A 321 ARG ASN GLY ALA ILE ASN MET GLN ASP ILE MET ILE VAL
SEQRES 24 A 321 HIS LYS HIS PHE GLY ALA THR SER SER ASP TYR ASP ALA
SEQRES 25 A 321 GLN LEU GLU HIS HIS HIS HIS HIS HIS
SEQRES 1 B 187 MET ARG GLY SER HIS HIS HIS HIS HIS HIS THR ASP LEU
SEQRES 2 B 187 ARG ALA ASP LYS ALA SER SER ILE GLU LEU LYS PHE ASP
SEQRES 3 B 187 ARG ASN LYS GLY GLU VAL GLY ASP ILE LEU ILE GLY THR
SEQRES 4 B 187 VAL ARG ILE ASN ASN ILE LYS ASN PHE ALA GLY PHE GLN
SEQRES 5 B 187 VAL ASN ILE VAL TYR ASP PRO LYS VAL LEU MET ALA VAL
SEQRES 6 B 187 ASP PRO GLU THR GLY LYS GLU PHE THR SER SER THR PHE
SEQRES 7 B 187 PRO PRO GLY ARG THR VAL LEU LYS ASN ASN ALA TYR GLY
SEQRES 8 B 187 PRO ILE GLN ILE ALA ASP ASN ASP PRO GLU LYS GLY ILE
SEQRES 9 B 187 LEU ASN PHE ALA LEU ALA TYR SER TYR ILE ALA GLY TYR
SEQRES 10 B 187 LYS GLU THR GLY VAL ALA GLU GLU SER GLY ILE ILE ALA
SEQRES 11 B 187 LYS ILE GLY PHE LYS ILE LEU GLN LYS LYS SER THR ALA
SEQRES 12 B 187 VAL LYS PHE GLN ASP THR LEU SER MET PRO GLY ALA ILE
SEQRES 13 B 187 SER GLY THR GLN LEU PHE ASP TRP ASP GLY GLU VAL ILE
SEQRES 14 B 187 THR GLY TYR GLU VAL ILE GLN PRO ASP VAL LEU SER LEU
SEQRES 15 B 187 GLY ASP GLU PRO TYR
HET CA A 701 1
HET CA A 702 1
HET CL A 703 1
HETNAM CA CALCIUM ION
HETNAM CL CHLORIDE ION
FORMUL 3 CA 2(CA 2+)
FORMUL 5 CL CL 1-
FORMUL 6 HOH *244(H2 O)
HELIX 1 1 ASN A 67 LYS A 70 5 4
HELIX 2 2 PRO A 78 ARG A 80 5 3
HELIX 3 3 VAL A 174 ALA A 180 1 7
HELIX 4 4 ASN A 259 ARG A 268 1 10
HELIX 5 5 VAL A 280 ASP A 284 5 5
HELIX 6 6 ASN A 292 LYS A 301 1 10
HELIX 7 7 THR A 306 TYR A 310 5 5
HELIX 8 8 ASN B 509 TYR B 512 5 4
HELIX 9 9 ASP B 521 LYS B 524 5 4
HELIX 10 10 TYR B 535 GLY B 543 1 9
SHEET 1 A 5 LEU A 52 PRO A 59 0
SHEET 2 A 5 GLY A 102 VAL A 111 -1 O LYS A 110 N GLU A 53
SHEET 3 A 5 THR A 23 TYR A 31 -1 N VAL A 24 O ALA A 109
SHEET 4 A 5 THR A 10 ILE A 13 -1 N LYS A 12 O ASN A 29
SHEET 5 A 5 ASP A 141 ILE A 143 1 O ILE A 143 N ILE A 13
SHEET 1 B 6 ARG A 15 GLY A 18 0
SHEET 2 B 6 GLY A 145 VAL A 149 1 O LEU A 148 N ALA A 16
SHEET 3 B 6 GLY A 118 ALA A 131 -1 N GLY A 118 O VAL A 149
SHEET 4 B 6 SER A 40 SER A 46 -1 N VAL A 44 O GLU A 126
SHEET 5 B 6 MET A 82 ALA A 88 -1 O PHE A 85 N PHE A 43
SHEET 6 B 6 PHE A 72 TYR A 77 -1 N TYR A 77 O MET A 82
SHEET 1 C 4 ARG A 15 GLY A 18 0
SHEET 2 C 4 GLY A 145 VAL A 149 1 O LEU A 148 N ALA A 16
SHEET 3 C 4 GLY A 118 ALA A 131 -1 N GLY A 118 O VAL A 149
SHEET 4 C 4 GLU A 137 VAL A 138 -1 O VAL A 138 N PHE A 130
SHEET 1 D 3 TYR A 200 VAL A 206 0
SHEET 2 D 3 TYR A 158 PRO A 166 -1 N TYR A 158 O VAL A 206
SHEET 3 D 3 THR A 236 SER A 237 1 O THR A 236 N LYS A 159
SHEET 1 E 3 TYR A 200 VAL A 206 0
SHEET 2 E 3 TYR A 158 PRO A 166 -1 N TYR A 158 O VAL A 206
SHEET 3 E 3 ILE A 245 MET A 247 1 O ILE A 245 N TYR A 163
SHEET 1 F 4 TYR A 192 VAL A 194 0
SHEET 2 F 4 LYS A 183 ILE A 186 -1 N VAL A 184 O ALA A 193
SHEET 3 F 4 ASN A 209 SER A 218 -1 O SER A 218 N LYS A 183
SHEET 4 F 4 ARG A 225 VAL A 232 -1 O ILE A 227 N LEU A 215
SHEET 1 G 2 THR A 221 TYR A 222 0
SHEET 2 G 2 VAL A 249 ASP A 251 -1 O GLY A 250 N THR A 221
SHEET 1 H 5 LEU B 484 VAL B 487 0
SHEET 2 H 5 GLY B 549 ILE B 558 -1 O LYS B 557 N MET B 485
SHEET 3 H 5 ILE B 457 ASN B 465 -1 N GLY B 460 O ILE B 554
SHEET 4 H 5 SER B 442 PHE B 447 -1 N GLU B 444 O ARG B 463
SHEET 5 H 5 GLU B 595 ILE B 597 1 O ILE B 597 N ILE B 443
SHEET 1 I 4 PRO B 514 ALA B 518 0
SHEET 2 I 4 ILE B 526 TYR B 533 -1 O ALA B 530 N ILE B 517
SHEET 3 I 4 PHE B 470 VAL B 478 -1 N ILE B 477 O LEU B 527
SHEET 4 I 4 LYS B 567 PHE B 568 -1 O LYS B 567 N VAL B 478
SHEET 1 J 5 PRO B 514 ALA B 518 0
SHEET 2 J 5 ILE B 526 TYR B 533 -1 O ALA B 530 N ILE B 517
SHEET 3 J 5 PHE B 470 VAL B 478 -1 N ILE B 477 O LEU B 527
SHEET 4 J 5 THR B 581 ASP B 585 -1 O PHE B 584 N ALA B 471
SHEET 5 J 5 VAL B 590 ILE B 591 -1 O ILE B 591 N LEU B 583
LINK OD1 ASP A 251 CA CA A 702 1555 1555 2.37
LINK O VAL A 253 CA CA A 702 1555 1555 2.28
LINK OD1 ASP A 255 CA CA A 702 1555 1555 2.35
LINK O SER A 257 CA CA A 702 1555 1555 2.17
LINK OD1 ASP A 262 CA CA A 702 1555 1555 2.53
LINK OD2 ASP A 262 CA CA A 702 1555 1555 2.47
LINK OD1 ASP A 284 CA CA A 701 1555 1555 2.38
LINK OD1 ASN A 286 CA CA A 701 1555 1555 2.44
LINK OD1 ASN A 288 CA CA A 701 1555 1555 2.40
LINK O ALA A 290 CA CA A 701 1555 1555 2.30
LINK OD1 ASP A 295 CA CA A 701 1555 1555 2.52
LINK OD2 ASP A 295 CA CA A 701 1555 1555 2.55
LINK O HOH A 345 CA CA A 701 1555 1555 2.43
LINK O HOH A 346 CA CA A 702 1555 1555 2.45
SITE 1 AC1 6 ASP A 284 ASN A 286 ASN A 288 ALA A 290
SITE 2 AC1 6 ASP A 295 HOH A 345
SITE 1 AC2 6 ASP A 251 VAL A 253 ASP A 255 SER A 257
SITE 2 AC2 6 ASP A 262 HOH A 346
SITE 1 AC3 2 ARG A 225 MET A 246
CRYST1 169.977 58.019 56.150 90.00 90.00 90.00 P 21 21 2 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 0.005883 0.000000 0.000000 0.00000
SCALE2 0.000000 0.017236 0.000000 0.00000
SCALE3 0.000000 0.000000 0.017809 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
