LinkDB: 3FHI
Original site: 3FHI
Chemical substance (4) PDB-CCD (4) Chemical reaction (1) KEGG ENZYME (1) Protein sequence (6) UniProt (2) SWISS-PROT (2) PDBSTR (2) Protein domain (13) InterPro (11) Pfam (2) Literature (1) PubMed (1) All databases (25)
Download RDF
HEADER TRANSFERASE 09-DEC-08 3FHI
TITLE CRYSTAL STRUCTURE OF A COMPLEX BETWEEN THE CATALYTIC AND REGULATORY
TITLE 2 (RI{ALPHA}) SUBUNITS OF PKA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CAMP-DEPENDENT PROTEIN KINASE CATALYTIC SUBUNIT ALPHA;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: PKA C-ALPHA;
COMPND 5 EC: 2.7.11.11;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: CAMP-DEPENDENT PROTEIN KINASE TYPE I-ALPHA REGULATORY
COMPND 10 SUBUNIT;
COMPND 11 CHAIN: B;
COMPND 12 FRAGMENT: UNP RESIDUES 92-245;
COMPND 13 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: MOUSE;
SOURCE 4 ORGANISM_TAXID: 10090;
SOURCE 5 GENE: PRKACA, PKACA;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 MOL_ID: 2;
SOURCE 9 ORGANISM_SCIENTIFIC: BOS TAURUS;
SOURCE 10 ORGANISM_COMMON: BOVINE,COW,DOMESTIC CATTLE,DOMESTIC COW;
SOURCE 11 ORGANISM_TAXID: 9913;
SOURCE 12 GENE: PRKAR1A;
SOURCE 13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 14 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS CAMP, CAMP DEPENDENT PROTEIN KINASE, PROTEIN-PROTEIN COMPLEX, AMP-
KEYWDS 2 PNP, PROTEIN KINASE REGULATION, NUCLEOTIDE BINDING, PROTEIN KINASE
KEYWDS 3 ACTIVITY, PROTEIN SERINE/THREONINE KINASE ACTIVITY, CAMP-DEPENDENT
KEYWDS 4 PROTEIN KINASE ACTIVITY, PROTEIN BINDING, ATP BINDING, KINASE
KEYWDS 5 ACTIVITY, TRANSFERASE ACTIVITY, ATP-BINDING, KINASE, LIPOPROTEIN,
KEYWDS 6 MYRISTATE, NUCLEOTIDE-BINDING, NUCLEUS, PHOSPHOPROTEIN,
KEYWDS 7 SERINE/THREONINE-PROTEIN KINASE, TRANSFERASE, CAMP-BINDING
EXPDTA X-RAY DIFFRACTION
AUTHOR C.KIM
REVDAT 3 01-NOV-17 3FHI 1 REMARK
REVDAT 2 13-JUL-11 3FHI 1 VERSN
REVDAT 1 14-APR-09 3FHI 0
SPRSDE 14-APR-09 3FHI 1U7E
JRNL AUTH C.KIM,N.H.XUONG,S.S.TAYLOR
JRNL TITL CRYSTAL STRUCTURE OF A COMPLEX BETWEEN THE CATALYTIC AND
JRNL TITL 2 REGULATORY (RIALPHA) SUBUNITS OF PKA.
JRNL REF SCIENCE V. 307 690 2005
JRNL REFN ISSN 0036-8075
JRNL PMID 15692043
JRNL DOI 10.1126/SCIENCE.1104607
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.2
REMARK 3 NUMBER OF REFLECTIONS : 42244
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) : 0.199
REMARK 3 R VALUE (WORKING SET) : 0.198
REMARK 3 FREE R VALUE : 0.226
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2136
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) : 2.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.05
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2870
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.34
REMARK 3 BIN R VALUE (WORKING SET) : 0.2640
REMARK 3 BIN FREE R VALUE SET COUNT : 144
REMARK 3 BIN FREE R VALUE : 0.2700
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3842
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 33
REMARK 3 SOLVENT ATOMS : 159
REMARK 3
REMARK 3 B VALUES.
REMARK 3 B VALUE TYPE : LIKELY RESIDUAL
REMARK 3 FROM WILSON PLOT (A**2) : 34.90
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 44.57
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.17000
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) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.166
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.146
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.117
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 8.427
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.959
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.949
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3966 ; 0.012 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 2661 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 5381 ; 1.406 ; 1.957
REMARK 3 BOND ANGLES OTHERS (DEGREES): 6453 ; 0.884 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 486 ; 6.161 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 180 ;35.744 ;23.667
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 645 ;14.052 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 23 ;17.701 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 585 ; 0.084 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4422 ; 0.005 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 861 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 806 ; 0.223 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 2789 ; 0.196 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 1956 ; 0.182 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): 2041 ; 0.087 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 176 ; 0.128 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 4 ; 0.178 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 25 ; 0.228 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 8 ; 0.145 ; 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): 2597 ; 0.740 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 990 ; 0.157 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3867 ; 1.095 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1735 ; 1.735 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1514 ; 2.505 ; 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 : 4
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 11 A 128
REMARK 3 ORIGIN FOR THE GROUP (A): 19.7240 3.1540 29.6710
REMARK 3 T TENSOR
REMARK 3 T11: 0.1812 T22: 0.1740
REMARK 3 T33: -0.0887 T12: -0.0864
REMARK 3 T13: 0.0218 T23: -0.0500
REMARK 3 L TENSOR
REMARK 3 L11: 0.4533 L22: 2.4387
REMARK 3 L33: 1.8748 L12: 0.3267
REMARK 3 L13: 0.1466 L23: 1.2075
REMARK 3 S TENSOR
REMARK 3 S11: -0.1127 S12: 0.3550 S13: 0.0602
REMARK 3 S21: -0.9870 S22: 0.1329 S23: -0.0605
REMARK 3 S31: -0.3178 S32: 0.1779 S33: -0.0203
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 92 B 240
REMARK 3 ORIGIN FOR THE GROUP (A): 19.4670 35.2720 48.5000
REMARK 3 T TENSOR
REMARK 3 T11: -0.1200 T22: 0.0316
REMARK 3 T33: -0.2640 T12: -0.0518
REMARK 3 T13: -0.0110 T23: 0.0271
REMARK 3 L TENSOR
REMARK 3 L11: 1.5522 L22: 1.0946
REMARK 3 L33: 1.0342 L12: 0.0055
REMARK 3 L13: -0.1544 L23: -0.1823
REMARK 3 S TENSOR
REMARK 3 S11: -0.0541 S12: 0.1922 S13: 0.0973
REMARK 3 S21: -0.1134 S22: 0.0324 S23: -0.0838
REMARK 3 S31: 0.0455 S32: -0.0364 S33: 0.0217
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 400 A 403
REMARK 3 ORIGIN FOR THE GROUP (A): 12.4130 6.0400 36.5500
REMARK 3 T TENSOR
REMARK 3 T11: 0.2356 T22: 0.3072
REMARK 3 T33: 0.0823 T12: -0.1240
REMARK 3 T13: -0.0484 T23: -0.0445
REMARK 3 L TENSOR
REMARK 3 L11: 15.1568 L22: 6.1915
REMARK 3 L33: 14.5148 L12: 9.0039
REMARK 3 L13: 8.7154 L23: 2.3476
REMARK 3 S TENSOR
REMARK 3 S11: -0.2099 S12: -0.1288 S13: -0.3546
REMARK 3 S21: -0.7638 S22: 0.7170 S23: -0.4087
REMARK 3 S31: 0.3891 S32: -0.9316 S33: -0.5072
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 129 A 350
REMARK 3 ORIGIN FOR THE GROUP (A): 19.1380 4.5860 48.5950
REMARK 3 T TENSOR
REMARK 3 T11: -0.1612 T22: -0.0445
REMARK 3 T33: -0.2646 T12: -0.0308
REMARK 3 T13: 0.0263 T23: -0.0296
REMARK 3 L TENSOR
REMARK 3 L11: 1.1831 L22: 1.9908
REMARK 3 L33: 1.2963 L12: 0.2697
REMARK 3 L13: -0.2287 L23: 0.2555
REMARK 3 S TENSOR
REMARK 3 S11: -0.1032 S12: 0.1519 S13: -0.1666
REMARK 3 S21: -0.3173 S22: 0.0998 S23: 0.0369
REMARK 3 S31: -0.0027 S32: 0.0247 S33: 0.0033
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 3FHI COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 10-DEC-08.
REMARK 100 THE DEPOSITION ID IS D_1000050597.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 12-OCT-03
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
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) : 1.000
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL, SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO, HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK, HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 42244
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.2
REMARK 200 DATA REDUNDANCY : 23.50
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.07600
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 28.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.06
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.7
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.25300
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.800
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER, DM
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 53.86
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.67
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20 % PEG 2000, 0.1 M TRIS-HCL, 4 % 1,3
REMARK 280 -PROPANEDIOL, 2.0 MM CYCLOHEXYL-PENTYL-D-MALTOSIDE, PH 7.0,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K
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 27.22650
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 61.02150
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 46.50850
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 61.02150
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 27.22650
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 46.50850
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3010 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 21180 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -13.0 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 GLY A 1
REMARK 465 ASN A 2
REMARK 465 ALA A 3
REMARK 465 ALA A 4
REMARK 465 ALA A 5
REMARK 465 ALA A 6
REMARK 465 LYS A 7
REMARK 465 LYS A 8
REMARK 465 GLY A 9
REMARK 465 SER A 10
REMARK 465 GLU A 11
REMARK 465 GLN A 12
REMARK 465 GLY B 91
REMARK 465 LYS B 242
REMARK 465 MET B 243
REMARK 465 TYR B 244
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 GLU A 13 CG CD OE1 OE2
REMARK 470 SER A 14 OG
REMARK 470 LYS A 16 CG CD CE NZ
REMARK 470 GLU A 17 CG CD OE1 OE2
REMARK 470 LYS A 21 CG CD CE NZ
REMARK 470 LYS A 28 CG CD CE NZ
REMARK 470 GLU A 31 CG CD OE1 OE2
REMARK 470 GLN A 35 CG CD OE1 NE2
REMARK 470 GLN A 39 CG CD OE1 NE2
REMARK 470 ASP A 41 CG OD1 OD2
REMARK 470 ASP A 44 CG OD1 OD2
REMARK 470 GLU A 64 CG CD OE1 OE2
REMARK 470 GLN A 176 CG CD OE1 NE2
REMARK 470 LYS A 192 CG CD CE NZ
REMARK 470 LYS A 317 CG CD CE NZ
REMARK 470 PHE A 318 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LYS A 319 CG CD CE NZ
REMARK 470 GLU A 331 CG CD OE1 OE2
REMARK 470 GLU A 333 CG CD OE1 OE2
REMARK 470 GLU A 334 CG CD OE1 OE2
REMARK 470 ILE A 335 CG1 CG2 CD1
REMARK 470 ARG A 336 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 345 CG CD CE NZ
REMARK 470 GLU A 349 CG CD OE1 OE2
REMARK 470 PHE A 350 O
REMARK 470 ARG B 92 CG CD NE CZ NH1 NH2
REMARK 470 ARG B 93 CG CD NE CZ NH1 NH2
REMARK 470 GLU B 106 CG CD OE1 OE2
REMARK 470 ASP B 107 CG OD1 OD2
REMARK 470 SER B 110 OG
REMARK 470 LYS B 114 CG CD CE NZ
REMARK 470 LYS B 121 CG CD CE NZ
REMARK 470 GLU B 168 CG CD OE1 OE2
REMARK 470 ARG B 241 CG CD NE CZ NH1 NH2
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 A 137 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES
REMARK 500 ARG A 144 NE - CZ - NH1 ANGL. DEV. = 4.2 DEGREES
REMARK 500 ARG A 144 NE - CZ - NH2 ANGL. DEV. = -3.5 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 ASP A 112 -158.30 -130.88
REMARK 500 ASP A 166 46.35 -143.44
REMARK 500 ASP A 184 75.70 64.04
REMARK 500 LEU A 273 41.75 -88.22
REMARK 500 LYS A 319 54.68 -109.88
REMARK 500 ILE A 335 85.94 -41.43
REMARK 500 ASN B 186 16.30 59.82
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 TYR B 205 GLY B 206 43.12
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 MN A 401 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN A 171 OD1
REMARK 620 2 ASP A 184 OD1 88.6
REMARK 620 3 ANP A 400 O2G 118.0 86.4
REMARK 620 4 ANP A 400 O2A 93.7 91.0 148.0
REMARK 620 5 HOH A 416 O 96.3 173.2 87.1 93.4
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN A 402 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 184 OD2
REMARK 620 2 ANP A 400 O1G 143.8
REMARK 620 3 ANP A 400 O2B 88.3 85.6
REMARK 620 4 HOH A 372 O 103.5 111.7 86.3
REMARK 620 5 HOH A 356 O 94.4 96.6 171.8 85.5
REMARK 620 N 1 2 3 4
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ANP A 400
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN A 402
DBREF 3FHI A 1 350 UNP P05132 KAPCA_MOUSE 2 351
DBREF 3FHI B 91 244 UNP P00514 KAP0_BOVIN 92 245
SEQADV 3FHI ALA A 199 UNP P05132 CYS 200 ENGINEERED
SEQRES 1 A 350 GLY ASN ALA ALA ALA ALA LYS LYS GLY SER GLU GLN GLU
SEQRES 2 A 350 SER VAL LYS GLU PHE LEU ALA LYS ALA LYS GLU ASP PHE
SEQRES 3 A 350 LEU LYS LYS TRP GLU THR PRO SER GLN ASN THR ALA GLN
SEQRES 4 A 350 LEU ASP GLN PHE ASP ARG ILE LYS THR LEU GLY THR GLY
SEQRES 5 A 350 SER PHE GLY ARG VAL MET LEU VAL LYS HIS LYS GLU SER
SEQRES 6 A 350 GLY ASN HIS TYR ALA MET LYS ILE LEU ASP LYS GLN LYS
SEQRES 7 A 350 VAL VAL LYS LEU LYS GLN ILE GLU HIS THR LEU ASN GLU
SEQRES 8 A 350 LYS ARG ILE LEU GLN ALA VAL ASN PHE PRO PHE LEU VAL
SEQRES 9 A 350 LYS LEU GLU PHE SER PHE LYS ASP ASN SER ASN LEU TYR
SEQRES 10 A 350 MET VAL MET GLU TYR VAL ALA GLY GLY GLU MET PHE SER
SEQRES 11 A 350 HIS LEU ARG ARG ILE GLY ARG PHE SER GLU PRO HIS ALA
SEQRES 12 A 350 ARG PHE TYR ALA ALA GLN ILE VAL LEU THR PHE GLU TYR
SEQRES 13 A 350 LEU HIS SER LEU ASP LEU ILE TYR ARG ASP LEU LYS PRO
SEQRES 14 A 350 GLU ASN LEU LEU ILE ASP GLN GLN GLY TYR ILE GLN VAL
SEQRES 15 A 350 THR ASP PHE GLY PHE ALA LYS ARG VAL LYS GLY ARG THR
SEQRES 16 A 350 TRP TPO LEU ALA GLY THR PRO GLU TYR LEU ALA PRO GLU
SEQRES 17 A 350 ILE ILE LEU SER LYS GLY TYR ASN LYS ALA VAL ASP TRP
SEQRES 18 A 350 TRP ALA LEU GLY VAL LEU ILE TYR GLU MET ALA ALA GLY
SEQRES 19 A 350 TYR PRO PRO PHE PHE ALA ASP GLN PRO ILE GLN ILE TYR
SEQRES 20 A 350 GLU LYS ILE VAL SER GLY LYS VAL ARG PHE PRO SER HIS
SEQRES 21 A 350 PHE SER SER ASP LEU LYS ASP LEU LEU ARG ASN LEU LEU
SEQRES 22 A 350 GLN VAL ASP LEU THR LYS ARG PHE GLY ASN LEU LYS ASN
SEQRES 23 A 350 GLY VAL ASN ASP ILE LYS ASN HIS LYS TRP PHE ALA THR
SEQRES 24 A 350 THR ASP TRP ILE ALA ILE TYR GLN ARG LYS VAL GLU ALA
SEQRES 25 A 350 PRO PHE ILE PRO LYS PHE LYS GLY PRO GLY ASP THR SER
SEQRES 26 A 350 ASN PHE ASP ASP TYR GLU GLU GLU GLU ILE ARG VAL SEP
SEQRES 27 A 350 ILE ASN GLU LYS CYS GLY LYS GLU PHE THR GLU PHE
SEQRES 1 B 154 GLY ARG ARG ARG ARG GLY ALA ILE SER ALA GLU VAL TYR
SEQRES 2 B 154 THR GLU GLU ASP ALA ALA SER TYR VAL ARG LYS VAL ILE
SEQRES 3 B 154 PRO LYS ASP TYR LYS THR MET ALA ALA LEU ALA LYS ALA
SEQRES 4 B 154 ILE GLU LYS ASN VAL LEU PHE SER HIS LEU ASP ASP ASN
SEQRES 5 B 154 GLU ARG SER ASP ILE PHE ASP ALA MET PHE PRO VAL SER
SEQRES 6 B 154 PHE ILE ALA GLY GLU THR VAL ILE GLN GLN GLY ASP GLU
SEQRES 7 B 154 GLY ASP ASN PHE TYR VAL ILE ASP GLN GLY GLU MET ASP
SEQRES 8 B 154 VAL TYR VAL ASN ASN GLU TRP ALA THR SER VAL GLY GLU
SEQRES 9 B 154 GLY GLY SER PHE GLY GLU LEU ALA LEU ILE TYR GLY THR
SEQRES 10 B 154 PRO ARG ALA ALA THR VAL LYS ALA LYS THR ASN VAL LYS
SEQRES 11 B 154 LEU TRP GLY ILE ASP ARG ASP SER TYR ARG ARG ILE LEU
SEQRES 12 B 154 MET GLY SER THR LEU ARG LYS ARG LYS MET TYR
MODRES 3FHI TPO A 197 THR PHOSPHOTHREONINE
MODRES 3FHI SEP A 338 SER PHOSPHOSERINE
HET TPO A 197 11
HET SEP A 338 10
HET ANP A 400 31
HET MN A 401 1
HET MN A 402 1
HETNAM TPO PHOSPHOTHREONINE
HETNAM SEP PHOSPHOSERINE
HETNAM ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER
HETNAM MN MANGANESE (II) ION
HETSYN TPO PHOSPHONOTHREONINE
HETSYN SEP PHOSPHONOSERINE
FORMUL 1 TPO C4 H10 N O6 P
FORMUL 1 SEP C3 H8 N O6 P
FORMUL 3 ANP C10 H17 N6 O12 P3
FORMUL 4 MN 2(MN 2+)
FORMUL 6 HOH *159(H2 O)
HELIX 1 1 GLU A 13 THR A 32 1 20
HELIX 2 2 GLN A 39 ASP A 41 5 3
HELIX 3 3 LYS A 76 LEU A 82 1 7
HELIX 4 4 GLN A 84 VAL A 98 1 15
HELIX 5 5 GLU A 127 GLY A 136 1 10
HELIX 6 6 SER A 139 LEU A 160 1 22
HELIX 7 7 LYS A 168 GLU A 170 5 3
HELIX 8 8 THR A 201 LEU A 205 5 5
HELIX 9 9 ALA A 206 LEU A 211 1 6
HELIX 10 10 ALA A 218 GLY A 234 1 17
HELIX 11 11 GLN A 242 GLY A 253 1 12
HELIX 12 12 SER A 262 LEU A 273 1 12
HELIX 13 13 ASP A 276 ARG A 280 5 5
HELIX 14 14 VAL A 288 ASN A 293 1 6
HELIX 15 15 HIS A 294 ALA A 298 5 5
HELIX 16 16 ASP A 301 GLN A 307 1 7
HELIX 17 17 THR B 104 ALA B 109 5 6
HELIX 18 18 ASP B 119 ILE B 130 1 12
HELIX 19 19 ASP B 140 MET B 151 1 12
HELIX 20 20 GLY B 199 ILE B 204 5 6
HELIX 21 21 ARG B 226 LYS B 240 1 15
SHEET 1 A 5 PHE A 43 THR A 51 0
SHEET 2 A 5 ARG A 56 HIS A 62 -1 O LEU A 59 N LYS A 47
SHEET 3 A 5 HIS A 68 ASP A 75 -1 O ILE A 73 N ARG A 56
SHEET 4 A 5 ASN A 115 GLU A 121 -1 O MET A 118 N LYS A 72
SHEET 5 A 5 LEU A 106 LYS A 111 -1 N PHE A 108 O VAL A 119
SHEET 1 B 2 LEU A 162 ILE A 163 0
SHEET 2 B 2 LYS A 189 ARG A 190 -1 O LYS A 189 N ILE A 163
SHEET 1 C 2 LEU A 172 ILE A 174 0
SHEET 2 C 2 ILE A 180 VAL A 182 -1 O GLN A 181 N LEU A 173
SHEET 1 D 2 ALA A 199 GLY A 200 0
SHEET 2 D 2 ILE B 98 SER B 99 -1 O ILE B 98 N GLY A 200
SHEET 1 E 4 PHE B 152 PHE B 156 0
SHEET 2 E 4 VAL B 219 ASP B 225 -1 O LEU B 221 N VAL B 154
SHEET 3 E 4 ASN B 171 GLN B 177 -1 N PHE B 172 O ILE B 224
SHEET 4 E 4 SER B 197 PHE B 198 -1 O PHE B 198 N TYR B 173
SHEET 1 F 4 THR B 161 ILE B 163 0
SHEET 2 F 4 THR B 212 ALA B 215 -1 O VAL B 213 N ILE B 163
SHEET 3 F 4 MET B 180 VAL B 184 -1 N ASP B 181 O LYS B 214
SHEET 4 F 4 GLU B 187 VAL B 192 -1 O ALA B 189 N VAL B 182
LINK C TRP A 196 N TPO A 197 1555 1555 1.33
LINK C TPO A 197 N LEU A 198 1555 1555 1.32
LINK C VAL A 337 N SEP A 338 1555 1555 1.34
LINK C SEP A 338 N ILE A 339 1555 1555 1.33
LINK OD1 ASN A 171 MN MN A 401 1555 1555 2.01
LINK OD1 ASP A 184 MN MN A 401 1555 1555 1.78
LINK OD2 ASP A 184 MN MN A 402 1555 1555 2.06
LINK O1G ANP A 400 MN MN A 402 1555 1555 1.89
LINK O2G ANP A 400 MN MN A 401 1555 1555 2.24
LINK O2B ANP A 400 MN MN A 402 1555 1555 2.24
LINK O2A ANP A 400 MN MN A 401 1555 1555 2.13
LINK MN MN A 401 O HOH A 416 1555 1555 1.91
LINK MN MN A 402 O HOH A 372 1555 1555 2.21
LINK MN MN A 402 O HOH A 356 1555 1555 2.26
SITE 1 AC1 31 GLY A 50 THR A 51 GLY A 52 SER A 53
SITE 2 AC1 31 PHE A 54 GLY A 55 VAL A 57 ALA A 70
SITE 3 AC1 31 LYS A 72 VAL A 104 MET A 120 GLU A 121
SITE 4 AC1 31 VAL A 123 GLU A 127 ASP A 166 LYS A 168
SITE 5 AC1 31 GLU A 170 ASN A 171 LEU A 173 THR A 183
SITE 6 AC1 31 ASP A 184 PHE A 327 HOH A 372 MN A 401
SITE 7 AC1 31 MN A 402 HOH A 416 HOH A 497 HOH A 505
SITE 8 AC1 31 ARG B 94 GLY B 96 ALA B 97
SITE 1 AC2 4 ASN A 171 ASP A 184 ANP A 400 HOH A 416
SITE 1 AC3 4 ASP A 184 HOH A 356 HOH A 372 ANP A 400
CRYST1 54.453 93.017 122.043 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 0.018364 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010751 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008194 0.00000
(ATOM LINES ARE NOT SHOWN.)
END