HEADER TRANSFERASE 02-DEC-13 4NTT
TITLE STRUCTURE OF THE CATALYTIC SUBUNIT OF CAMP-DEPENDENT PROTEIN KINASE
TITLE 2 BOUND TO ADP AND ONE MAGNESIUM ION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CAMP-DEPENDENT PROTEIN KINASE CATALYTIC SUBUNIT ALPHA;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: PKA C-ALPHA;
COMPND 5 EC: 2.7.11.11;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: 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
KEYWDS PROTEIN KINASE FOLD, KINASE, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.C.BASTIDAS,J.WU,S.S.TAYLOR
REVDAT 2 28-JAN-15 4NTT 1 JRNL
REVDAT 1 15-OCT-14 4NTT 0
JRNL AUTH A.C.BASTIDAS,J.WU,S.S.TAYLOR
JRNL TITL MOLECULAR FEATURES OF PRODUCT RELEASE FOR THE PKA CATALYTIC
JRNL TITL 2 CYCLE.
JRNL REF BIOCHEMISTRY V. 54 2 2015
JRNL REFN ISSN 0006-2960
JRNL PMID 25077557
JRNL DOI 10.1021/BI500684C
REMARK 2
REMARK 2 RESOLUTION. 3.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0110
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) : 3.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 71.58
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.1
REMARK 3 NUMBER OF REFLECTIONS : 10114
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) : 0.230
REMARK 3 R VALUE (WORKING SET) : 0.227
REMARK 3 FREE R VALUE : 0.284
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT : 516
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) : 3.50
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.59
REMARK 3 REFLECTION IN BIN (WORKING SET) : 767
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.41
REMARK 3 BIN R VALUE (WORKING SET) : 0.2970
REMARK 3 BIN FREE R VALUE SET COUNT : 38
REMARK 3 BIN FREE R VALUE : 0.4930
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5206
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 56
REMARK 3 SOLVENT ATOMS : 0
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 93.10
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 8.48000
REMARK 3 B22 (A**2) : -4.63000
REMARK 3 B33 (A**2) : -2.11000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 3.68000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.735
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.643
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 92.329
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.927
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.893
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 5400 ; 0.007 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 7370 ; 1.114 ; 1.958
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 680 ; 5.766 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 239 ;38.907 ;23.891
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 767 ;19.256 ;15.039
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 22 ;20.999 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 804 ; 0.073 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4169 ; 0.004 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
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): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
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): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
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 : 2
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
REMARK 3 CHAIN NAMES : A B
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 2
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 10 A 126 4
REMARK 3 1 B 10 B 126 4
REMARK 3 2 A 327 A 350 4
REMARK 3 2 B 327 B 350 4
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 1 A (A): 1002 ; 0.540 ; 0.500
REMARK 3
REMARK 3 NCS GROUP NUMBER : 2
REMARK 3 CHAIN NAMES : A B
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 127 A 326 4
REMARK 3 1 B 127 B 326 4
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 2 A (A): 1571 ; 0.510 ; 0.500
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 6
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 4
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 10 A 126
REMARK 3 RESIDUE RANGE : A 127 A 300
REMARK 3 RESIDUE RANGE : A 301 A 326
REMARK 3 RESIDUE RANGE : A 327 A 350
REMARK 3 ORIGIN FOR THE GROUP (A): 28.5402 49.5433 18.4871
REMARK 3 T TENSOR
REMARK 3 T11: 0.7153 T22: 0.7978
REMARK 3 T33: 0.8516 T12: -0.0634
REMARK 3 T13: 0.0124 T23: 0.0703
REMARK 3 L TENSOR
REMARK 3 L11: 2.2560 L22: 3.3724
REMARK 3 L33: 3.8608 L12: -0.5111
REMARK 3 L13: -0.0327 L23: 1.0201
REMARK 3 S TENSOR
REMARK 3 S11: -0.0106 S12: -0.1699 S13: -0.1015
REMARK 3 S21: 0.1739 S22: 0.0118 S23: -0.0346
REMARK 3 S31: 0.2769 S32: -0.2515 S33: -0.0012
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 4
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 10 B 126
REMARK 3 RESIDUE RANGE : B 127 B 300
REMARK 3 RESIDUE RANGE : B 301 B 326
REMARK 3 RESIDUE RANGE : B 327 B 350
REMARK 3 ORIGIN FOR THE GROUP (A): 9.2262 19.4777 -20.0632
REMARK 3 T TENSOR
REMARK 3 T11: 0.7124 T22: 0.7437
REMARK 3 T33: 0.8124 T12: -0.0515
REMARK 3 T13: -0.0156 T23: -0.0732
REMARK 3 L TENSOR
REMARK 3 L11: 1.4180 L22: 3.8565
REMARK 3 L33: 4.3193 L12: -0.7734
REMARK 3 L13: 0.1621 L23: -2.0669
REMARK 3 S TENSOR
REMARK 3 S11: -0.0189 S12: -0.3315 S13: 0.0576
REMARK 3 S21: 0.2259 S22: 0.0628 S23: 0.2501
REMARK 3 S31: -0.1590 S32: -0.2047 S33: -0.0438
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 401 A 401
REMARK 3 ORIGIN FOR THE GROUP (A): 30.3727 46.1927 28.5532
REMARK 3 T TENSOR
REMARK 3 T11: 1.4199 T22: 1.8281
REMARK 3 T33: 1.6881 T12: 0.5143
REMARK 3 T13: 0.5233 T23: 0.0078
REMARK 3 L TENSOR
REMARK 3 L11: 59.4528 L22: 6.9773
REMARK 3 L33: 53.7699 L12: 20.3540
REMARK 3 L13: 56.5302 L23: 19.3603
REMARK 3 S TENSOR
REMARK 3 S11: -0.2458 S12: -3.3969 S13: 1.2720
REMARK 3 S21: -0.0874 S22: -1.0417 S23: 0.3440
REMARK 3 S31: -0.1950 S32: -3.0604 S33: 1.2875
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 402 A 402
REMARK 3 ORIGIN FOR THE GROUP (A): 34.5510 46.7001 24.3552
REMARK 3 T TENSOR
REMARK 3 T11: 0.7689 T22: 0.8279
REMARK 3 T33: 0.0073 T12: 0.1476
REMARK 3 T13: 0.0412 T23: 0.0718
REMARK 3 L TENSOR
REMARK 3 L11: 0.0000 L22: 0.0000
REMARK 3 L33: 0.0000 L12: 0.0000
REMARK 3 L13: 0.0000 L23: 0.0000
REMARK 3 S TENSOR
REMARK 3 S11: 0.0000 S12: 0.0000 S13: 0.0000
REMARK 3 S21: 0.0000 S22: 0.0000 S23: 0.0000
REMARK 3 S31: 0.0000 S32: 0.0000 S33: 0.0000
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 401 B 401
REMARK 3 ORIGIN FOR THE GROUP (A): 2.1474 20.1646 -12.1457
REMARK 3 T TENSOR
REMARK 3 T11: 1.5412 T22: 1.2350
REMARK 3 T33: 0.9454 T12: -0.0936
REMARK 3 T13: -0.2196 T23: 0.2457
REMARK 3 L TENSOR
REMARK 3 L11: 34.2789 L22: 1.1389
REMARK 3 L33: 12.7603 L12: -6.2241
REMARK 3 L13: -20.9116 L23: 3.7986
REMARK 3 S TENSOR
REMARK 3 S11: 0.8598 S12: 2.1324 S13: 0.5335
REMARK 3 S21: -0.0580 S22: -0.4448 S23: -0.0795
REMARK 3 S31: -0.5055 S32: -1.3241 S33: -0.4150
REMARK 3
REMARK 3 TLS GROUP : 6
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 402 B 402
REMARK 3 ORIGIN FOR THE GROUP (A): 0.7422 17.6528 -17.9002
REMARK 3 T TENSOR
REMARK 3 T11: 0.7157 T22: 0.7779
REMARK 3 T33: 0.7415 T12: 0.5716
REMARK 3 T13: -0.5425 T23: -0.1074
REMARK 3 L TENSOR
REMARK 3 L11: 0.0000 L22: 0.0000
REMARK 3 L33: 0.0000 L12: 0.0000
REMARK 3 L13: 0.0000 L23: 0.0000
REMARK 3 S TENSOR
REMARK 3 S11: 0.0000 S12: 0.0000 S13: 0.0000
REMARK 3 S21: 0.0000 S22: 0.0000 S23: 0.0000
REMARK 3 S31: 0.0000 S32: 0.0000 S33: 0.0000
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
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 4NTT COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-DEC-13.
REMARK 100 THE RCSB ID CODE IS RCSB083647.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 07-MAR-12
REMARK 200 TEMPERATURE (KELVIN) : NULL
REMARK 200 PH : 8.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 8.2.1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : NULL
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 : 10660
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.500
REMARK 200 RESOLUTION RANGE LOW (A) : 32.150
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.5
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
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: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: PDB ENTRY 4NTS
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 54.51
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.70
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 8% MPD, 0.1 M BICINE, 150 MM AMMONIUM
REMARK 280 ACETATE, 10 MM DTT, 9% METHANOL ADDED TO THE WELL, PH 8.0, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 277.15K
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 71.57500
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 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 CYS A 7
REMARK 465 LYS A 8
REMARK 465 GLY A 9
REMARK 465 GLY B 1
REMARK 465 ASN B 2
REMARK 465 ALA B 3
REMARK 465 ALA B 4
REMARK 465 ALA B 5
REMARK 465 ALA B 6
REMARK 465 CYS B 7
REMARK 465 LYS B 8
REMARK 465 GLY B 9
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 GLN A 12 CG CD OE1 NE2
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 GLU A 24 CG CD OE1 OE2
REMARK 470 LYS A 29 CG CD CE NZ
REMARK 470 GLN A 39 CG CD OE1 NE2
REMARK 470 LEU A 40 CG CD1 CD2
REMARK 470 ASP A 41 CG OD1 OD2
REMARK 470 ASP A 44 CG OD1 OD2
REMARK 470 ARG A 45 CG CD NE CZ NH1 NH2
REMARK 470 ILE A 46 CG1 CG2 CD1
REMARK 470 LYS A 47 CG CD CE NZ
REMARK 470 LEU A 49 CG CD1 CD2
REMARK 470 THR A 51 OG1 CG2
REMARK 470 ARG A 56 CG CD NE CZ NH1 NH2
REMARK 470 MET A 58 CG SD CE
REMARK 470 VAL A 60 CG1 CG2
REMARK 470 LYS A 61 CG CD CE NZ
REMARK 470 LYS A 63 CG CD CE NZ
REMARK 470 ILE A 73 CD1
REMARK 470 LYS A 78 CG CD CE NZ
REMARK 470 LYS A 81 CG CD CE NZ
REMARK 470 LEU A 82 CG CD1 CD2
REMARK 470 LYS A 83 CG CD CE NZ
REMARK 470 GLU A 86 CG CD OE1 OE2
REMARK 470 SER A 114 OG
REMARK 470 ILE A 135 CD1
REMARK 470 VAL A 191 CG1 CG2
REMARK 470 ILE A 210 CD1
REMARK 470 LYS A 213 CG CD CE NZ
REMARK 470 ILE A 228 CD1
REMARK 470 GLN A 242 CD OE1 NE2
REMARK 470 ILE A 246 CD1
REMARK 470 LYS A 249 CG CD CE NZ
REMARK 470 SER A 252 OG
REMARK 470 VAL A 255 CG1 CG2
REMARK 470 ARG A 256 CG CD NE CZ NH1 NH2
REMARK 470 SER A 263 OG
REMARK 470 ARG A 270 CG CD NE CZ NH1 NH2
REMARK 470 VAL A 275 CG1 CG2
REMARK 470 LYS A 285 CG CD CE NZ
REMARK 470 ILE A 291 CD1
REMARK 470 LYS A 295 CG CD CE NZ
REMARK 470 ILE A 303 CD1
REMARK 470 GLU A 311 CG CD OE1 OE2
REMARK 470 ILE A 315 CD1
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 PRO A 321 CG CD
REMARK 470 ASP A 323 CG OD1 OD2
REMARK 470 THR A 324 OG1 CG2
REMARK 470 SER A 325 OG
REMARK 470 ASN A 326 CG OD1 ND2
REMARK 470 PHE A 327 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ASP A 328 CG OD1 OD2
REMARK 470 ASP A 329 CG OD1 OD2
REMARK 470 TYR A 330 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 GLU A 331 CG CD OE1 OE2
REMARK 470 GLU A 332 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 CD1
REMARK 470 VAL A 337 CG1 CG2
REMARK 470 LYS A 342 CG CD CE NZ
REMARK 470 THR A 348 OG1 CG2
REMARK 470 GLU B 11 CG CD OE1 OE2
REMARK 470 GLN B 12 CG CD OE1 NE2
REMARK 470 GLU B 13 CG CD OE1 OE2
REMARK 470 SER B 14 OG
REMARK 470 LYS B 16 CG CD CE NZ
REMARK 470 GLU B 17 CG CD OE1 OE2
REMARK 470 LYS B 21 CG CD CE NZ
REMARK 470 GLU B 24 CG CD OE1 OE2
REMARK 470 LYS B 29 CG CD CE NZ
REMARK 470 ASP B 44 CG OD1 OD2
REMARK 470 ARG B 45 CG CD NE CZ NH1 NH2
REMARK 470 ILE B 46 CD1
REMARK 470 LYS B 47 CG CD CE NZ
REMARK 470 LEU B 49 CG CD1 CD2
REMARK 470 ARG B 56 CG CD NE CZ NH1 NH2
REMARK 470 VAL B 60 CG1 CG2
REMARK 470 LYS B 61 CG CD CE NZ
REMARK 470 LYS B 63 CG CD CE NZ
REMARK 470 GLU B 64 CG CD OE1 OE2
REMARK 470 LYS B 72 CG CD CE NZ
REMARK 470 ILE B 73 CD1
REMARK 470 LYS B 78 CG CD CE NZ
REMARK 470 LYS B 81 CG CD CE NZ
REMARK 470 LEU B 82 CG CD1 CD2
REMARK 470 LYS B 83 CG CD CE NZ
REMARK 470 GLU B 86 CG CD OE1 OE2
REMARK 470 SER B 114 OG
REMARK 470 GLU B 127 CG CD OE1 OE2
REMARK 470 ILE B 135 CD1
REMARK 470 VAL B 191 CG1 CG2
REMARK 470 ILE B 210 CD1
REMARK 470 LYS B 213 CG CD CE NZ
REMARK 470 ILE B 228 CD1
REMARK 470 GLN B 242 CD OE1 NE2
REMARK 470 ILE B 246 CD1
REMARK 470 LYS B 249 CG CD CE NZ
REMARK 470 SER B 252 OG
REMARK 470 VAL B 255 CG1 CG2
REMARK 470 ARG B 256 CG CD NE CZ NH1 NH2
REMARK 470 SER B 263 OG
REMARK 470 VAL B 275 CG1 CG2
REMARK 470 LYS B 285 CG CD CE NZ
REMARK 470 ILE B 291 CD1
REMARK 470 LYS B 295 CG CD CE NZ
REMARK 470 ILE B 303 CD1
REMARK 470 GLU B 311 CG CD OE1 OE2
REMARK 470 ILE B 315 CD1
REMARK 470 LYS B 317 CG CD CE NZ
REMARK 470 PHE B 318 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LYS B 319 CG CD CE NZ
REMARK 470 PRO B 321 CG CD
REMARK 470 ASP B 323 CG OD1 OD2
REMARK 470 THR B 324 OG1 CG2
REMARK 470 SER B 325 OG
REMARK 470 ASN B 326 CG OD1 ND2
REMARK 470 ASP B 328 CG OD1 OD2
REMARK 470 ASP B 329 CG OD1 OD2
REMARK 470 GLU B 331 CG CD OE1 OE2
REMARK 470 GLU B 332 CG CD OE1 OE2
REMARK 470 GLU B 333 CG CD OE1 OE2
REMARK 470 GLU B 334 CG CD OE1 OE2
REMARK 470 ILE B 335 CG1 CG2 CD1
REMARK 470 ARG B 336 CG CD NE CZ NH1 NH2
REMARK 470 VAL B 337 CG1 CG2
REMARK 470 LYS B 342 CG CD CE NZ
REMARK 470 THR B 348 OG1 CG2
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 OH TYR B 204 OE2 GLU B 230 2.09
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 ARG A 137 CZ ARG A 137 NH2 0.087
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 ASN A 36 57.83 37.61
REMARK 500 ILE A 46 -63.95 -93.71
REMARK 500 LEU A 74 107.57 -162.35
REMARK 500 ASN A 99 114.94 -169.03
REMARK 500 ASP A 112 -125.14 -141.20
REMARK 500 THR A 183 -132.96 58.00
REMARK 500 LYS A 309 49.65 -79.53
REMARK 500 ASP A 329 -167.32 74.30
REMARK 500 GLU A 334 -150.34 57.97
REMARK 500 LYS B 83 71.55 44.80
REMARK 500 ASN B 99 98.84 -166.42
REMARK 500 PRO B 101 -35.73 -37.65
REMARK 500 PHE B 110 148.99 -175.17
REMARK 500 ASP B 166 46.04 -140.43
REMARK 500 ASP B 175 174.82 -55.95
REMARK 500 SER B 212 6.86 59.05
REMARK 500 ASP B 241 -73.89 -70.23
REMARK 500 HIS B 260 5.45 -68.35
REMARK 500 LEU B 273 53.17 -95.09
REMARK 500 ASN B 283 56.48 -109.12
REMARK 500 PHE B 297 50.99 -93.83
REMARK 500 ARG B 308 18.47 58.55
REMARK 500 LYS B 309 46.37 -94.44
REMARK 500 ASN B 326 49.21 32.60
REMARK 500 ASP B 328 151.58 74.14
REMARK 500 TYR B 330 -8.55 77.22
REMARK 500 GLU B 331 14.72 52.87
REMARK 500 GLU B 334 176.34 64.88
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 VAL A 182 THR A 183 142.43
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 MG A 402 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ADP A 401 O2A
REMARK 620 2 ASP A 184 OD2 103.2
REMARK 620 3 ADP A 401 O3B 69.1 76.8
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B 402 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ADP B 401 O2A
REMARK 620 2 ADP B 401 O3B 62.6
REMARK 620 3 ASP B 184 OD2 105.2 68.4
REMARK 620 N 1 2
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 402
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4NTS RELATED DB: PDB
REMARK 900 APO STRUCTURE OF THE C-SUBUNIT
REMARK 900 RELATED ID: 1J3H RELATED DB: PDB
REMARK 900 ANOTHER APO STRUCTURE OF THE C-SUBUNIT
REMARK 900 RELATED ID: 1CMK RELATED DB: PDB
REMARK 900 OPEN STRUCTURE OF THE C-SUBUNIT BOUND TO IP20
REMARK 900 RELATED ID: 1SYK RELATED DB: PDB
REMARK 900 ANOTHER APO STRUCTURE OF THE C-SUBUNIT WITH E230Q MUTATION
REMARK 900 RELATED ID: 1ATP RELATED DB: PDB
REMARK 900 STRUCTURE OF THE C-SUBUNIT BOUND TO ATP AND IP20
DBREF 4NTT A 1 350 UNP P05132 KAPCA_MOUSE 2 351
DBREF 4NTT B 1 350 UNP P05132 KAPCA_MOUSE 2 351
SEQADV 4NTT CYS A 7 UNP P05132 LYS 8 EXPRESSION TAG
SEQADV 4NTT CYS B 7 UNP P05132 LYS 8 ENGINEERED MUTATION
SEQRES 1 A 350 GLY ASN ALA ALA ALA ALA CYS 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 CYS 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 350 GLY ASN ALA ALA ALA ALA CYS LYS GLY SER GLU GLN GLU
SEQRES 2 B 350 SER VAL LYS GLU PHE LEU ALA LYS ALA LYS GLU ASP PHE
SEQRES 3 B 350 LEU LYS LYS TRP GLU THR PRO SER GLN ASN THR ALA GLN
SEQRES 4 B 350 LEU ASP GLN PHE ASP ARG ILE LYS THR LEU GLY THR GLY
SEQRES 5 B 350 SER PHE GLY ARG VAL MET LEU VAL LYS HIS LYS GLU SER
SEQRES 6 B 350 GLY ASN HIS TYR ALA MET LYS ILE LEU ASP LYS GLN LYS
SEQRES 7 B 350 VAL VAL LYS LEU LYS GLN ILE GLU HIS THR LEU ASN GLU
SEQRES 8 B 350 LYS ARG ILE LEU GLN ALA VAL ASN PHE PRO PHE LEU VAL
SEQRES 9 B 350 LYS LEU GLU PHE SER PHE LYS ASP ASN SER ASN LEU TYR
SEQRES 10 B 350 MET VAL MET GLU TYR VAL ALA GLY GLY GLU MET PHE SER
SEQRES 11 B 350 HIS LEU ARG ARG ILE GLY ARG PHE SER GLU PRO HIS ALA
SEQRES 12 B 350 ARG PHE TYR ALA ALA GLN ILE VAL LEU THR PHE GLU TYR
SEQRES 13 B 350 LEU HIS SER LEU ASP LEU ILE TYR ARG ASP LEU LYS PRO
SEQRES 14 B 350 GLU ASN LEU LEU ILE ASP GLN GLN GLY TYR ILE GLN VAL
SEQRES 15 B 350 THR ASP PHE GLY PHE ALA LYS ARG VAL LYS GLY ARG THR
SEQRES 16 B 350 TRP TPO LEU CYS GLY THR PRO GLU TYR LEU ALA PRO GLU
SEQRES 17 B 350 ILE ILE LEU SER LYS GLY TYR ASN LYS ALA VAL ASP TRP
SEQRES 18 B 350 TRP ALA LEU GLY VAL LEU ILE TYR GLU MET ALA ALA GLY
SEQRES 19 B 350 TYR PRO PRO PHE PHE ALA ASP GLN PRO ILE GLN ILE TYR
SEQRES 20 B 350 GLU LYS ILE VAL SER GLY LYS VAL ARG PHE PRO SER HIS
SEQRES 21 B 350 PHE SER SER ASP LEU LYS ASP LEU LEU ARG ASN LEU LEU
SEQRES 22 B 350 GLN VAL ASP LEU THR LYS ARG PHE GLY ASN LEU LYS ASN
SEQRES 23 B 350 GLY VAL ASN ASP ILE LYS ASN HIS LYS TRP PHE ALA THR
SEQRES 24 B 350 THR ASP TRP ILE ALA ILE TYR GLN ARG LYS VAL GLU ALA
SEQRES 25 B 350 PRO PHE ILE PRO LYS PHE LYS GLY PRO GLY ASP THR SER
SEQRES 26 B 350 ASN PHE ASP ASP TYR GLU GLU GLU GLU ILE ARG VAL SEP
SEQRES 27 B 350 ILE ASN GLU LYS CYS GLY LYS GLU PHE THR GLU PHE
MODRES 4NTT TPO A 197 THR PHOSPHOTHREONINE
MODRES 4NTT SEP A 338 SER PHOSPHOSERINE
MODRES 4NTT TPO B 197 THR PHOSPHOTHREONINE
MODRES 4NTT SEP B 338 SER PHOSPHOSERINE
HET TPO A 197 11
HET SEP A 338 10
HET TPO B 197 11
HET SEP B 338 10
HET ADP A 401 27
HET MG A 402 1
HET ADP B 401 27
HET MG B 402 1
HETNAM TPO PHOSPHOTHREONINE
HETNAM SEP PHOSPHOSERINE
HETNAM ADP ADENOSINE-5'-DIPHOSPHATE
HETNAM MG MAGNESIUM ION
HETSYN TPO PHOSPHONOTHREONINE
HETSYN SEP PHOSPHONOSERINE
FORMUL 1 TPO 2(C4 H10 N O6 P)
FORMUL 1 SEP 2(C3 H8 N O6 P)
FORMUL 3 ADP 2(C10 H15 N5 O10 P2)
FORMUL 4 MG 2(MG 2+)
HELIX 1 1 GLU A 13 THR A 32 1 20
HELIX 2 2 LYS A 76 LEU A 82 1 7
HELIX 3 3 GLN A 84 VAL A 98 1 15
HELIX 4 4 GLU A 127 ILE A 135 1 9
HELIX 5 5 SER A 139 LEU A 160 1 22
HELIX 6 6 ALA A 206 LEU A 211 1 6
HELIX 7 7 ALA A 218 GLY A 234 1 17
HELIX 8 8 GLN A 242 SER A 252 1 11
HELIX 9 9 SER A 262 LEU A 273 1 12
HELIX 10 10 VAL A 288 ASN A 293 1 6
HELIX 11 11 HIS A 294 ALA A 298 5 5
HELIX 12 12 ASP A 301 GLN A 307 1 7
HELIX 13 13 GLU B 13 THR B 32 1 20
HELIX 14 14 GLN B 39 ASP B 41 5 3
HELIX 15 15 LYS B 76 LEU B 82 1 7
HELIX 16 16 GLN B 84 VAL B 98 1 15
HELIX 17 17 GLU B 127 GLY B 136 1 10
HELIX 18 18 SER B 139 LEU B 160 1 22
HELIX 19 19 ALA B 206 LEU B 211 1 6
HELIX 20 20 ALA B 218 GLY B 234 1 17
HELIX 21 21 GLN B 242 SER B 252 1 11
HELIX 22 22 SER B 262 LEU B 273 1 12
HELIX 23 23 VAL B 288 ASN B 293 1 6
HELIX 24 24 HIS B 294 ALA B 298 5 5
HELIX 25 25 ASP B 301 GLN B 307 1 7
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 ILE A 46
SHEET 3 A 5 HIS A 68 ASP A 75 -1 O TYR A 69 N VAL A 60
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 110 O TYR A 117
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 5 PHE B 43 GLY B 50 0
SHEET 2 D 5 VAL B 57 HIS B 62 -1 O VAL B 57 N GLY B 50
SHEET 3 D 5 HIS B 68 ASP B 75 -1 O MET B 71 N MET B 58
SHEET 4 D 5 ASN B 115 GLU B 121 -1 O MET B 120 N ALA B 70
SHEET 5 D 5 LEU B 106 LYS B 111 -1 N GLU B 107 O VAL B 119
SHEET 1 E 2 LEU B 162 ILE B 163 0
SHEET 2 E 2 LYS B 189 ARG B 190 -1 O LYS B 189 N ILE B 163
SHEET 1 F 2 LEU B 172 ILE B 174 0
SHEET 2 F 2 ILE B 180 VAL B 182 -1 O GLN B 181 N LEU B 173
LINK C TRP A 196 N TPO A 197 1555 1555 1.33
LINK C TPO A 197 N LEU A 198 1555 1555 1.33
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 C TRP B 196 N TPO B 197 1555 1555 1.33
LINK C TPO B 197 N LEU B 198 1555 1555 1.33
LINK C VAL B 337 N SEP B 338 1555 1555 1.33
LINK C SEP B 338 N ILE B 339 1555 1555 1.33
LINK O2A ADP A 401 MG MG A 402 1555 1555 1.91
LINK OD2 ASP A 184 MG MG A 402 1555 1555 2.39
LINK O2A ADP B 401 MG MG B 402 1555 1555 2.40
LINK O3B ADP A 401 MG MG A 402 1555 1555 2.65
LINK O3B ADP B 401 MG MG B 402 1555 1555 2.67
LINK OD2 ASP B 184 MG MG B 402 1555 1555 2.70
SITE 1 AC1 8 SER A 53 ALA A 70 GLU A 121 TYR A 122
SITE 2 AC1 8 VAL A 123 THR A 183 ASP A 184 MG A 402
SITE 1 AC2 3 ASN A 171 ASP A 184 ADP A 401
SITE 1 AC3 8 SER B 53 VAL B 57 ALA B 70 GLU B 121
SITE 2 AC3 8 VAL B 123 THR B 183 ASP B 184 MG B 402
SITE 1 AC4 3 ASN B 171 ASP B 184 ADP B 401
CRYST1 50.480 143.150 62.570 90.00 103.61 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 0.019810 0.000000 0.004796 0.00000
SCALE2 0.000000 0.006986 0.000000 0.00000
SCALE3 0.000000 0.000000 0.016444 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
