HEADER TRANSFERASE/PEPTIDE 07-DEC-12 4IB0
TITLE X-RAY STRUCTURE OF CAMP DEPENDENT PROTEIN KINASE A IN COMPLEX WITH
TITLE 2 HIGH NA+ CONCENTRATION, ADP AND PHOSPHORYLATED PEPTIDE PSP20
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 MOL_ID: 2;
COMPND 8 MOLECULE: PHOSPHORYLATED PSEUDO-SUBSTRATE PEPTIDE PSP20;
COMPND 9 CHAIN: S;
COMPND 10 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 SYNTHETIC: YES;
SOURCE 10 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 11 ORGANISM_COMMON: HUMAN;
SOURCE 12 ORGANISM_TAXID: 9606
KEYWDS KINASE ENZYME, PHOSPHOTRANSFER, PHOSPHORYLATED, TRANSFERASE-PEPTIDE
KEYWDS 2 COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR O.GERLITS,A.KOVALEVSKY
REVDAT 3 28-MAY-14 4IB0 1 JRNL
REVDAT 2 21-MAY-14 4IB0 1 JRNL
REVDAT 1 11-DEC-13 4IB0 0
JRNL AUTH O.GERLITS,A.DAS,M.M.KESHWANI,S.TAYLOR,M.J.WALTMAN,P.LANGAN,
JRNL AUTH 2 W.T.HELLER,A.KOVALEVSKY
JRNL TITL METAL-FREE CAMP-DEPENDENT PROTEIN KINASE CAN CATALYZE
JRNL TITL 2 PHOSPHORYL TRANSFER.
JRNL REF BIOCHEMISTRY V. 53 3179 2014
JRNL REFN ISSN 0006-2960
JRNL PMID 24786636
JRNL DOI 10.1021/BI5000965
REMARK 2
REMARK 2 RESOLUTION. 1.87 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : SHELXL-97
REMARK 3 AUTHORS : G.M.SHELDRICK
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.87
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : NULL
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (NO CUTOFF).
REMARK 3 R VALUE (WORKING + TEST SET, NO CUTOFF) : NULL
REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : 0.219
REMARK 3 FREE R VALUE (NO CUTOFF) : 0.287
REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : 1871
REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : NULL
REMARK 3
REMARK 3 FIT/AGREEMENT OF MODEL FOR DATA WITH F>4SIG(F).
REMARK 3 R VALUE (WORKING + TEST SET, F>4SIG(F)) : NULL
REMARK 3 R VALUE (WORKING SET, F>4SIG(F)) : NULL
REMARK 3 FREE R VALUE (F>4SIG(F)) : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%, F>4SIG(F)) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT (F>4SIG(F)) : NULL
REMARK 3 TOTAL NUMBER OF REFLECTIONS (F>4SIG(F)) : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2946
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 29
REMARK 3 SOLVENT ATOMS : 303
REMARK 3
REMARK 3 MODEL REFINEMENT.
REMARK 3 OCCUPANCY SUM OF NON-HYDROGEN ATOMS : NULL
REMARK 3 OCCUPANCY SUM OF HYDROGEN ATOMS : NULL
REMARK 3 NUMBER OF DISCRETELY DISORDERED RESIDUES : NULL
REMARK 3 NUMBER OF LEAST-SQUARES PARAMETERS : NULL
REMARK 3 NUMBER OF RESTRAINTS : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM RESTRAINT TARGET VALUES.
REMARK 3 BOND LENGTHS (A) : 0.022
REMARK 3 ANGLE DISTANCES (A) : NULL
REMARK 3 SIMILAR DISTANCES (NO TARGET VALUES) (A) : NULL
REMARK 3 DISTANCES FROM RESTRAINT PLANES (A) : NULL
REMARK 3 ZERO CHIRAL VOLUMES (A**3) : NULL
REMARK 3 NON-ZERO CHIRAL VOLUMES (A**3) : NULL
REMARK 3 ANTI-BUMPING DISTANCE RESTRAINTS (A) : NULL
REMARK 3 RIGID-BOND ADP COMPONENTS (A**2) : NULL
REMARK 3 SIMILAR ADP COMPONENTS (A**2) : NULL
REMARK 3 APPROXIMATELY ISOTROPIC ADPS (A**2) : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED: NULL
REMARK 3
REMARK 3 STEREOCHEMISTRY TARGET VALUES : ENGH & HUBER
REMARK 3 SPECIAL CASE: NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4IB0 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 10-JAN-13.
REMARK 100 THE RCSB ID CODE IS RCSB076527.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 23-MAR-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU MICROMAX-007 HF
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.54
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IV++
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-3000
REMARK 200 DATA SCALING SOFTWARE : HKL-3000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 30267
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.870
REMARK 200 RESOLUTION RANGE LOW (A) : 40.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 81.0
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: CNS
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 51.49
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.54
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM MES PH 6.5, 5 MM DTT, 15-20%
REMARK 280 PEG 4000, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 277K
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 28.63500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 49.02050
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 39.60100
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 49.02050
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 28.63500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 39.60100
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3300 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 15810 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -44.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, S
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 HIS A -5
REMARK 465 HIS A -4
REMARK 465 HIS A -3
REMARK 465 HIS A -2
REMARK 465 HIS A -1
REMARK 465 HIS A 0
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 GLU A 13
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 86 CD GLU A 86 OE2 -0.072
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 A 144 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 ARG A 144 NE - CZ - NH2 ANGL. DEV. = -3.9 DEGREES
REMARK 500 PRO A 321 C - N - CD ANGL. DEV. = -17.3 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 PHE A 54 17.35 -147.24
REMARK 500 ASP A 166 40.91 -147.56
REMARK 500 ASP A 184 82.22 65.62
REMARK 500 ASN A 216 -159.84 -126.57
REMARK 500 LYS A 319 77.73 -116.81
REMARK 500 HIS S 623 78.40 -159.34
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 GLY A 320 -11.98
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 NA A 402 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ADP A 403 O3B
REMARK 620 2 ADP A 403 O2A 78.9
REMARK 620 3 HOH A1002 O 96.4 87.5
REMARK 620 4 ASP A 184 OD2 92.2 82.2 165.1
REMARK 620 5 ASN A 171 OD1 163.6 85.1 79.6 88.7
REMARK 620 6 HOH S 701 O 98.4 154.9 117.6 72.9 97.5
REMARK 620 7 HOH S 728 O 76.4 144.1 69.9 124.2 116.2 55.8
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA A 401 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ADP A 403 O1B
REMARK 620 2 HOH S 727 O 113.1
REMARK 620 3 SEP S 621 O1P 95.9 80.4
REMARK 620 4 ASP A 184 OD2 80.9 161.7 86.7
REMARK 620 5 ASP A 184 OD1 88.0 138.7 134.6 49.2
REMARK 620 6 HOH A1188 O 157.6 89.2 90.1 77.9 72.7
REMARK 620 7 HOH A1001 O 77.5 74.3 148.5 121.8 76.5 107.8
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 NA A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP A 403
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4IAC RELATED DB: PDB
REMARK 900 RELATED ID: 4IAD RELATED DB: PDB
REMARK 900 RELATED ID: 4IAF RELATED DB: PDB
REMARK 900 RELATED ID: 4IAI RELATED DB: PDB
REMARK 900 RELATED ID: 4IAK RELATED DB: PDB
REMARK 900 RELATED ID: 4IAY RELATED DB: PDB
REMARK 900 RELATED ID: 4IAZ RELATED DB: PDB
REMARK 900 RELATED ID: 4IB1 RELATED DB: PDB
REMARK 900 RELATED ID: 4IB3 RELATED DB: PDB
DBREF 4IB0 A 1 350 UNP P05132 KAPCA_MOUSE 2 351
DBREF 4IB0 S 605 624 PDB 4IB0 4IB0 605 624
SEQADV 4IB0 HIS A -5 UNP P05132 EXPRESSION TAG
SEQADV 4IB0 HIS A -4 UNP P05132 EXPRESSION TAG
SEQADV 4IB0 HIS A -3 UNP P05132 EXPRESSION TAG
SEQADV 4IB0 HIS A -2 UNP P05132 EXPRESSION TAG
SEQADV 4IB0 HIS A -1 UNP P05132 EXPRESSION TAG
SEQADV 4IB0 HIS A 0 UNP P05132 EXPRESSION TAG
SEQRES 1 A 356 HIS HIS HIS HIS HIS HIS GLY ASN ALA ALA ALA ALA LYS
SEQRES 2 A 356 LYS GLY SER GLU GLN GLU SER VAL LYS GLU PHE LEU ALA
SEQRES 3 A 356 LYS ALA LYS GLU ASP PHE LEU LYS LYS TRP GLU THR PRO
SEQRES 4 A 356 SER GLN ASN THR ALA GLN LEU ASP GLN PHE ASP ARG ILE
SEQRES 5 A 356 LYS THR LEU GLY THR GLY SER PHE GLY ARG VAL MET LEU
SEQRES 6 A 356 VAL LYS HIS LYS GLU SER GLY ASN HIS TYR ALA MET LYS
SEQRES 7 A 356 ILE LEU ASP LYS GLN LYS VAL VAL LYS LEU LYS GLN ILE
SEQRES 8 A 356 GLU HIS THR LEU ASN GLU LYS ARG ILE LEU GLN ALA VAL
SEQRES 9 A 356 ASN PHE PRO PHE LEU VAL LYS LEU GLU PHE SER PHE LYS
SEQRES 10 A 356 ASP ASN SER ASN LEU TYR MET VAL MET GLU TYR VAL ALA
SEQRES 11 A 356 GLY GLY GLU MET PHE SER HIS LEU ARG ARG ILE GLY ARG
SEQRES 12 A 356 PHE SEP GLU PRO HIS ALA ARG PHE TYR ALA ALA GLN ILE
SEQRES 13 A 356 VAL LEU THR PHE GLU TYR LEU HIS SER LEU ASP LEU ILE
SEQRES 14 A 356 TYR ARG ASP LEU LYS PRO GLU ASN LEU LEU ILE ASP GLN
SEQRES 15 A 356 GLN GLY TYR ILE GLN VAL THR ASP PHE GLY PHE ALA LYS
SEQRES 16 A 356 ARG VAL LYS GLY ARG THR TRP TPO LEU CYS GLY THR PRO
SEQRES 17 A 356 GLU TYR LEU ALA PRO GLU ILE ILE LEU SER LYS GLY TYR
SEQRES 18 A 356 ASN LYS ALA VAL ASP TRP TRP ALA LEU GLY VAL LEU ILE
SEQRES 19 A 356 TYR GLU MET ALA ALA GLY TYR PRO PRO PHE PHE ALA ASP
SEQRES 20 A 356 GLN PRO ILE GLN ILE TYR GLU LYS ILE VAL SER GLY LYS
SEQRES 21 A 356 VAL ARG PHE PRO SER HIS PHE SER SER ASP LEU LYS ASP
SEQRES 22 A 356 LEU LEU ARG ASN LEU LEU GLN VAL ASP LEU THR LYS ARG
SEQRES 23 A 356 PHE GLY ASN LEU LYS ASN GLY VAL ASN ASP ILE LYS ASN
SEQRES 24 A 356 HIS LYS TRP PHE ALA THR THR ASP TRP ILE ALA ILE TYR
SEQRES 25 A 356 GLN ARG LYS VAL GLU ALA PRO PHE ILE PRO LYS PHE LYS
SEQRES 26 A 356 GLY PRO GLY ASP THR SER ASN PHE ASP ASP TYR GLU GLU
SEQRES 27 A 356 GLU GLU ILE ARG VAL SEP ILE ASN GLU LYS CYS GLY LYS
SEQRES 28 A 356 GLU PHE THR GLU PHE
SEQRES 1 S 20 THR THR TYR ALA ASP PHE ILE ALA SER GLY ARG THR GLY
SEQRES 2 S 20 ARG ARG ALA SEP ILE HIS ASP
MODRES 4IB0 SEP A 139 SER PHOSPHOSERINE
MODRES 4IB0 TPO A 197 THR PHOSPHOTHREONINE
MODRES 4IB0 SEP A 338 SER PHOSPHOSERINE
MODRES 4IB0 SEP S 621 SER PHOSPHOSERINE
HET SEP A 139 10
HET TPO A 197 11
HET SEP A 338 10
HET SEP S 621 10
HET NA A 401 1
HET NA A 402 1
HET ADP A 403 27
HETNAM SEP PHOSPHOSERINE
HETNAM TPO PHOSPHOTHREONINE
HETNAM NA SODIUM ION
HETNAM ADP ADENOSINE-5'-DIPHOSPHATE
HETSYN SEP PHOSPHONOSERINE
HETSYN TPO PHOSPHONOTHREONINE
FORMUL 1 SEP 3(C3 H8 N O6 P)
FORMUL 1 TPO C4 H10 N O6 P
FORMUL 3 NA 2(NA 1+)
FORMUL 5 ADP C10 H15 N5 O10 P2
FORMUL 6 HOH *303(H2 O)
HELIX 1 1 SER A 14 THR A 32 1 19
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 GLN A 96 1 13
HELIX 5 5 GLU A 127 GLY A 136 1 10
HELIX 6 6 SEP A 139 SER A 159 1 21
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 LYS A 217 GLY A 234 1 18
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 VAL A 288 ASN A 293 1 6
HELIX 14 14 HIS A 294 ALA A 298 5 5
HELIX 15 15 ASP A 301 GLN A 307 1 7
HELIX 16 16 THR S 606 ALA S 612 1 7
SHEET 1 A 5 PHE A 43 THR A 51 0
SHEET 2 A 5 GLY A 55 HIS A 62 -1 O VAL A 57 N LEU A 49
SHEET 3 A 5 HIS A 68 ASP A 75 -1 O MET A 71 N MET A 58
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 GLU A 107 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 CYS A 199 GLY A 200 0
SHEET 2 D 2 ILE S 622 HIS S 623 -1 O ILE S 622 N GLY A 200
LINK C PHE A 138 N SEP A 139 1555 1555 1.33
LINK C SEP A 139 N GLU A 140 1555 1555 1.32
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 1.33
LINK C SEP A 338 N ILE A 339 1555 1555 1.34
LINK C ALA S 620 N SEP S 621 1555 1555 1.33
LINK C SEP S 621 N ILE S 622 1555 1555 1.33
LINK NA NA A 402 O3B ADP A 403 1555 1555 2.05
LINK NA NA A 402 O2A ADP A 403 1555 1555 2.06
LINK NA NA A 401 O1B ADP A 403 1555 1555 2.24
LINK NA NA A 401 O HOH S 727 1555 1555 2.30
LINK O1P SEP S 621 NA NA A 401 1555 1555 2.31
LINK NA NA A 402 O HOH A1002 1555 1555 2.45
LINK OD2 ASP A 184 NA NA A 402 1555 1555 2.45
LINK OD2 ASP A 184 NA NA A 401 1555 1555 2.52
LINK OD1 ASP A 184 NA NA A 401 1555 1555 2.57
LINK OD1 ASN A 171 NA NA A 402 1555 1555 2.60
LINK NA NA A 401 O HOH A1188 1555 1555 2.61
LINK NA NA A 401 O HOH A1001 1555 1555 2.63
LINK NA NA A 402 O HOH S 701 1555 1555 2.68
LINK NA NA A 402 O HOH S 728 1555 1555 2.77
SITE 1 AC1 6 ASP A 184 ADP A 403 HOH A1001 HOH A1188
SITE 2 AC1 6 SEP S 621 HOH S 727
SITE 1 AC2 6 ASN A 171 ASP A 184 ADP A 403 HOH A1002
SITE 2 AC2 6 HOH S 701 HOH S 728
SITE 1 AC3 28 LEU A 49 GLY A 50 GLY A 52 GLY A 55
SITE 2 AC3 28 VAL A 57 ALA A 70 LYS A 72 VAL A 104
SITE 3 AC3 28 MET A 120 GLU A 121 VAL A 123 GLU A 127
SITE 4 AC3 28 GLU A 170 ASN A 171 LEU A 173 THR A 183
SITE 5 AC3 28 ASP A 184 PHE A 327 NA A 401 NA A 402
SITE 6 AC3 28 HOH A1001 HOH A1002 HOH A1003 HOH A1032
SITE 7 AC3 28 HOH A1057 ARG S 618 SEP S 621 HOH S 728
CRYST1 57.270 79.202 98.041 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 0.017461 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012626 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010200 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
