HEADER TRANSFERASE 30-JUL-10 3O7L
TITLE CRYSTAL STRUCTURE OF PHOSPHOLAMBAN (1-19):PKA C-SUBUNIT:AMP-PNP:MG2+
TITLE 2 COMPLEX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CAMP-DEPENDENT PROTEIN KINASE CATALYTIC SUBUNIT ALPHA;
COMPND 3 CHAIN: B;
COMPND 4 FRAGMENT: PHOSPHOLAMBAN PEPTIDE;
COMPND 5 SYNONYM: PKA C-ALPHA;
COMPND 6 EC: 2.7.11.11;
COMPND 7 ENGINEERED: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: CAMP-DEPENDENT PROTEIN KINASE CATALYTIC SUBUNIT ALPHA;
COMPND 10 CHAIN: D;
COMPND 11 SYNONYM: PKA C-ALPHA;
COMPND 12 EC: 2.7.11.11;
COMPND 13 ENGINEERED: YES;
COMPND 14 MOL_ID: 3;
COMPND 15 MOLECULE: CARDIAC PHOSPHOLAMBAN;
COMPND 16 CHAIN: I;
COMPND 17 SYNONYM: PLB;
COMPND 18 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: PKACA, PRKACA;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 MOL_ID: 2;
SOURCE 9 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 10 ORGANISM_COMMON: MOUSE;
SOURCE 11 ORGANISM_TAXID: 10090;
SOURCE 12 GENE: PKACA, PRKACA;
SOURCE 13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 14 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 15 MOL_ID: 3;
SOURCE 16 SYNTHETIC: YES;
SOURCE 17 OTHER_DETAILS: CHEMICALLY SYNTHESIZED. THIS SEQUENCE OCCURS
SOURCE 18 NATURALLY FROM PHOSPHOLAMBAN
KEYWDS PROTEIN KINASE A, PHOSPHOLAMBAN, ALLOSTERY, SUBSTRATE RECOGNITION,
KEYWDS 2 CONFORMATIONAL SELECTION, INTRINSICALLY DISORDERED PROTEINS,
KEYWDS 3 MEMBRANE PROTEINS, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR C.Y.CHENG,S.S.TAYLOR
REVDAT 2 01-DEC-10 3O7L 1 JRNL
REVDAT 1 06-OCT-10 3O7L 0
JRNL AUTH L.R.MASTERSON,C.CHENG,T.YU,M.TONELLI,A.KORNEV,S.S.TAYLOR,
JRNL AUTH 2 G.VEGLIA
JRNL TITL DYNAMICS CONNECT SUBSTRATE RECOGNITION TO CATALYSIS IN
JRNL TITL 2 PROTEIN KINASE A.
JRNL REF NAT.CHEM.BIOL. V. 6 821 2010
JRNL REFN ISSN 1552-4450
JRNL PMID 20890288
JRNL DOI 10.1038/NCHEMBIO.452
REMARK 2
REMARK 2 RESOLUTION. 2.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-
REMARK 3 : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,
REMARK 3 : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL
REMARK 3 : MORIARTY,REETAL PAI,RANDY READ,JANE
REMARK 3 : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM
REMARK 3 : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,
REMARK 3 : LAURENT STORONI,TOM TERWILLIGER,PETER
REMARK 3 : ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 39.09
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 3 NUMBER OF REFLECTIONS : 25304
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.216
REMARK 3 R VALUE (WORKING SET) : 0.216
REMARK 3 FREE R VALUE : 0.287
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.090
REMARK 3 FREE R VALUE TEST SET COUNT : 1327
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 39.0906 - 5.5491 1.00 2786 149 0.2219 0.2480
REMARK 3 2 5.5491 - 4.4064 1.00 2788 142 0.1867 0.2485
REMARK 3 3 4.4064 - 3.8500 0.99 2731 154 0.1895 0.2596
REMARK 3 4 3.8500 - 3.4982 0.97 2681 152 0.2452 0.3288
REMARK 3 5 3.4982 - 3.2476 0.99 2737 151 0.2601 0.3608
REMARK 3 6 3.2476 - 3.0562 1.00 2758 148 0.2468 0.3292
REMARK 3 7 3.0562 - 2.9032 1.00 2727 161 0.2501 0.3404
REMARK 3 8 2.9032 - 2.8000 1.00 2767 137 0.2369 0.3589
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : 0.29
REMARK 3 B_SOL : 39.12
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.450
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : NULL
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 51.60
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 7.66090
REMARK 3 B22 (A**2) : 7.66090
REMARK 3 B33 (A**2) : -15.32180
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 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.006 5297
REMARK 3 ANGLE : 0.951 7204
REMARK 3 CHIRALITY : 0.068 802
REMARK 3 PLANARITY : 0.004 923
REMARK 3 DIHEDRAL : 19.331 1782
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 3
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN B
REMARK 3 ORIGIN FOR THE GROUP (A): -10.4702 32.0699 7.6142
REMARK 3 T TENSOR
REMARK 3 T11: -0.2216 T22: 0.0088
REMARK 3 T33: -0.1157 T12: -0.0080
REMARK 3 T13: -0.0067 T23: 0.2412
REMARK 3 L TENSOR
REMARK 3 L11: 1.6884 L22: 1.0574
REMARK 3 L33: 0.9496 L12: -0.5333
REMARK 3 L13: -0.6581 L23: -0.8000
REMARK 3 S TENSOR
REMARK 3 S11: -0.1226 S12: 0.2745 S13: -0.5068
REMARK 3 S21: -0.4984 S22: -0.1652 S23: 0.5459
REMARK 3 S31: 0.1614 S32: -0.4599 S33: -2.0574
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN D
REMARK 3 ORIGIN FOR THE GROUP (A): 17.7343 37.3507 33.9139
REMARK 3 T TENSOR
REMARK 3 T11: -0.0075 T22: 0.0553
REMARK 3 T33: 0.0325 T12: -0.0083
REMARK 3 T13: -0.0949 T23: -0.1350
REMARK 3 L TENSOR
REMARK 3 L11: 0.7369 L22: 0.5979
REMARK 3 L33: 0.6067 L12: 0.0179
REMARK 3 L13: -0.2419 L23: 0.0577
REMARK 3 S TENSOR
REMARK 3 S11: -0.0120 S12: -0.3447 S13: 0.0730
REMARK 3 S21: 0.2708 S22: 0.2006 S23: -0.0991
REMARK 3 S31: -0.0629 S32: 0.2308 S33: 0.0203
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN I
REMARK 3 ORIGIN FOR THE GROUP (A): 6.7467 32.7040 10.3398
REMARK 3 T TENSOR
REMARK 3 T11: -0.0050 T22: 0.0328
REMARK 3 T33: 0.1870 T12: -0.0305
REMARK 3 T13: 0.1205 T23: 0.1420
REMARK 3 L TENSOR
REMARK 3 L11: 0.0719 L22: 0.0063
REMARK 3 L33: 0.0130 L12: 0.0008
REMARK 3 L13: -0.0097 L23: -0.0043
REMARK 3 S TENSOR
REMARK 3 S11: 0.0190 S12: -0.0120 S13: -0.0314
REMARK 3 S21: 0.0395 S22: 0.0561 S23: 0.0293
REMARK 3 S31: 0.0099 S32: 0.0192 S33: 0.0619
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3O7L COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-AUG-10.
REMARK 100 THE RCSB ID CODE IS RCSB060765.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-JAN-09
REMARK 200 TEMPERATURE (KELVIN) : 200.0
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 8.2.2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.00
REMARK 200 MONOCHROMATOR : GRAPHITE
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 26095
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.800
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 264629.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 200 DATA REDUNDANCY : 10.500
REMARK 200 R MERGE (I) : 0.08400
REMARK 200 R SYM (I) : 0.06300
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 38.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.88
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
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 : 5.100
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASES
REMARK 200 STARTING MODEL: PDB ENTRY 1ATP
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 56.71
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.84
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: THE COMPLEX WAS OBTAINED BY COMBINING
REMARK 280 A 1:10:10:10 MOLAR RATIO MIXTURE OF PKA-C (7 MG/ML), PLN1-19,
REMARK 280 MGCL2, AND AMP-PNP IN 20 MM SODIUM ACETATE (PH 6.5), 180 MM KCL,
REMARK 280 AND 5 MM DTT, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298.0K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+5/6
REMARK 290 6555 X-Y,X,Z+1/6
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 64.06200
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 128.12400
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 96.09300
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 160.15500
REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 32.03100
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: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4360 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 28760 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -35.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, D, I
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 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 LYS B 7
REMARK 465 LYS B 8
REMARK 465 GLY B 9
REMARK 465 SER B 10
REMARK 465 GLU B 11
REMARK 465 GLN B 12
REMARK 465 GLU B 13
REMARK 465 SER B 14
REMARK 465 VAL B 15
REMARK 465 LYS B 16
REMARK 465 GLY B 52
REMARK 465 SER B 53
REMARK 465 PHE B 54
REMARK 465 ILE B 339
REMARK 465 ASN B 340
REMARK 465 GLU B 341
REMARK 465 LYS B 342
REMARK 465 GLY D 1
REMARK 465 ASN D 2
REMARK 465 ALA D 3
REMARK 465 ALA D 4
REMARK 465 ALA D 5
REMARK 465 ALA D 6
REMARK 465 LYS D 7
REMARK 465 LYS D 8
REMARK 465 GLY D 9
REMARK 465 SER D 10
REMARK 465 GLU D 11
REMARK 465 GLN D 12
REMARK 465 PHE D 318
REMARK 465 LYS D 319
REMARK 465 GLY D 320
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 B 17 CG CD OE1 OE2
REMARK 470 PHE B 18 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LYS B 21 CG CD CE NZ
REMARK 470 LYS B 23 CG CD CE NZ
REMARK 470 ASP B 25 CG OD1 OD2
REMARK 470 PHE B 26 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LYS B 28 CG CD CE NZ
REMARK 470 LYS B 29 CG CD CE NZ
REMARK 470 TRP B 30 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP B 30 CZ3 CH2
REMARK 470 GLU B 31 CG CD OE1 OE2
REMARK 470 THR B 32 OG1 CG2
REMARK 470 SER B 34 OG
REMARK 470 GLN B 35 CG CD OE1 NE2
REMARK 470 ASN B 36 CG OD1 ND2
REMARK 470 GLN B 39 CG CD OE1 NE2
REMARK 470 LEU B 40 CG CD1 CD2
REMARK 470 ASP B 41 CG OD1 OD2
REMARK 470 ASP B 44 CG OD1 OD2
REMARK 470 ARG B 45 CG CD NE CZ NH1 NH2
REMARK 470 ILE B 46 CG1 CG2 CD1
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 HIS B 62 CG ND1 CD2 CE1 NE2
REMARK 470 LYS B 63 CG CD CE NZ
REMARK 470 GLU B 64 CG CD OE1 OE2
REMARK 470 GLN B 77 CG CD OE1 NE2
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 LYS B 92 CG CD CE NZ
REMARK 470 GLN B 96 CG CD OE1 NE2
REMARK 470 LYS B 105 CG CD CE NZ
REMARK 470 PHE B 108 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 SER B 109 OG
REMARK 470 LYS B 111 CG CD CE NZ
REMARK 470 ASP B 112 CG OD1 OD2
REMARK 470 ASN B 113 CG OD1 ND2
REMARK 470 GLU B 121 CG CD OE1 OE2
REMARK 470 LYS B 189 CG CD CE NZ
REMARK 470 ARG B 190 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 192 CG CD CE NZ
REMARK 470 LYS B 213 CG CD CE NZ
REMARK 470 LYS B 254 CG CD CE NZ
REMARK 470 ARG B 256 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 309 CG CD CE NZ
REMARK 470 LYS B 317 CG CD CE NZ
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 CYS B 343 SG
REMARK 470 LYS B 345 CG CD CE NZ
REMARK 470 GLU B 346 CG CD OE1 OE2
REMARK 470 THR B 348 OG1 CG2
REMARK 470 GLU B 349 CG CD OE1 OE2
REMARK 470 PHE B 350 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 GLU D 13 CG CD OE1 OE2
REMARK 470 SER D 14 OG
REMARK 470 VAL D 15 CG1 CG2
REMARK 470 LYS D 16 CG CD CE NZ
REMARK 470 GLU D 17 CG CD OE1 OE2
REMARK 470 LEU D 19 CG CD1 CD2
REMARK 470 GLU D 24 CG CD OE1 OE2
REMARK 470 LYS D 28 CG CD CE NZ
REMARK 470 GLU D 64 CG CD OE1 OE2
REMARK 470 LYS D 83 CG CD CE NZ
REMARK 470 ASN D 99 CG OD1 ND2
REMARK 470 GLU D 121 CG CD OE1 OE2
REMARK 470 ARG D 133 CG CD NE CZ NH1 NH2
REMARK 470 ARG D 134 CG CD NE CZ NH1 NH2
REMARK 470 SER D 159 OG
REMARK 470 GLN D 176 CG CD OE1 NE2
REMARK 470 LYS D 189 CG CD CE NZ
REMARK 470 LYS D 192 CG CD CE NZ
REMARK 470 ARG D 194 CG CD NE CZ NH1 NH2
REMARK 470 LYS D 217 CG CD CE NZ
REMARK 470 LYS D 254 CG CD CE NZ
REMARK 470 ARG D 256 CG CD NE CZ NH1 NH2
REMARK 470 ASN D 283 CG OD1 ND2
REMARK 470 LYS D 285 CG CD CE NZ
REMARK 470 ASN D 286 CG OD1 ND2
REMARK 470 VAL D 288 CG1 CG2
REMARK 470 LYS D 295 CG CD CE NZ
REMARK 470 THR D 299 OG1 CG2
REMARK 470 ARG D 308 CG CD NE CZ NH1 NH2
REMARK 470 LYS D 309 CG CD CE NZ
REMARK 470 GLU D 311 CG CD OE1 OE2
REMARK 470 PHE D 314 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LYS D 317 CG CD CE NZ
REMARK 470 THR D 324 OG1 CG2
REMARK 470 SER D 325 OG
REMARK 470 ASN D 326 CG OD1 ND2
REMARK 470 ASP D 329 CG OD1 OD2
REMARK 470 GLU D 331 CG CD OE1 OE2
REMARK 470 GLU D 332 CG CD OE1 OE2
REMARK 470 GLU D 333 CG CD OE1 OE2
REMARK 470 GLU D 334 CG CD OE1 OE2
REMARK 470 ILE D 335 CG1 CG2 CD1
REMARK 470 ARG D 336 CG CD NE CZ NH1 NH2
REMARK 470 ILE D 339 CG1 CG2 CD1
REMARK 470 LYS D 342 CG CD CE NZ
REMARK 470 CYS D 343 SG
REMARK 470 GLU D 349 CG CD OE1 OE2
REMARK 470 VAL I 9 CG1 CG2
REMARK 470 GLN I 10 CG CD OE1 NE2
REMARK 470 THR I 22 OG1 CG2
REMARK 470 ILE I 23 CG1 CG2 CD1
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 MET B 71 CE
REMARK 480 LYS B 76 CD CE NZ
REMARK 480 ARG B 93 NE CZ NH1 NH2
REMARK 480 ILE B 163 CD1
REMARK 480 ARG B 194 CD NE CZ NH1 NH2
REMARK 480 LYS B 279 CD CE NZ
REMARK 480 LYS B 285 CD CE NZ
REMARK 480 LYS D 23 CD CE NZ
REMARK 480 GLU D 31 CG CD OE1 OE2
REMARK 480 LYS D 47 CE NZ
REMARK 480 LYS D 76 CD CE NZ
REMARK 480 LYS D 105 CE NZ
REMARK 480 GLU D 155 OE1 OE2
REMARK 480 GLN D 177 CD OE1 NE2
REMARK 480 LYS D 213 CD CE NZ
REMARK 480 LYS D 279 NZ
REMARK 480 ILE D 303 CD1
REMARK 480 LYS D 345 CD CE NZ
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 OD2 ASP B 184 O2A ANP B 354 1.94
REMARK 500 N ASP B 75 O4 PEG B 353 1.97
REMARK 500 NH1 ARG D 165 O2P TPO D 197 2.06
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 B 32 55.89 -169.57
REMARK 500 ASP B 41 30.14 -83.58
REMARK 500 ARG B 45 97.95 -49.30
REMARK 500 LYS B 63 -77.77 -54.60
REMARK 500 PHE B 110 161.23 176.79
REMARK 500 ASP B 112 42.24 -75.27
REMARK 500 SER B 114 -9.90 -149.32
REMARK 500 ASP B 166 29.66 -153.54
REMARK 500 LYS B 168 152.44 169.66
REMARK 500 ASP B 184 74.91 57.63
REMARK 500 LEU B 273 52.41 -91.02
REMARK 500 LEU B 284 -155.44 -109.26
REMARK 500 ASN D 36 72.72 21.30
REMARK 500 ALA D 38 -163.12 -168.10
REMARK 500 PHE D 110 173.29 166.77
REMARK 500 ASP D 112 -167.22 -107.01
REMARK 500 ASP D 166 21.54 -151.64
REMARK 500 LYS D 168 143.96 175.10
REMARK 500 ASP D 184 96.96 73.91
REMARK 500 CYS D 199 -38.18 -150.51
REMARK 500 PHE D 238 70.56 -116.88
REMARK 500 ALA D 240 141.00 -173.30
REMARK 500 HIS D 260 30.21 -80.88
REMARK 500 ASP D 276 94.46 -67.92
REMARK 500 THR D 299 48.45 -90.47
REMARK 500 LYS D 309 40.61 -98.04
REMARK 500 THR D 324 41.48 -73.90
REMARK 500 CYS D 343 52.99 26.43
REMARK 500 ARG I 14 3.06 -65.60
REMARK 500 THR I 22 103.54 -52.83
REMARK 500
REMARK 500 REMARK: NULL
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 ANP B 354
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 B 351 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 184 OD1
REMARK 620 2 ANP B 354 O1B 69.1
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B 352 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ANP B 354 O2A
REMARK 620 2 ASP B 184 OD2 61.1
REMARK 620 3 ANP B 354 O1B 80.8 56.7
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 MG B 351
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 352
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG B 353
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ANP B 354
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1ATP RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE C-SUBUNIT OF PKA
DBREF 3O7L B 1 350 UNP P05132 KAPCA_MOUSE 2 351
DBREF 3O7L D 1 350 UNP P05132 KAPCA_MOUSE 2 351
DBREF 3O7L I 9 23 UNP P61014 PPLA_MOUSE 4 18
SEQADV 3O7L ILE B 173 UNP P05132 LEU 174 CONFLICT
SEQADV 3O7L ILE B 211 UNP P05132 LEU 212 CONFLICT
SEQRES 1 B 350 GLY ASN ALA ALA ALA ALA LYS 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 ILE 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 ILE 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 SER
SEQRES 27 B 350 ILE ASN GLU LYS CYS GLY LYS GLU PHE THR GLU PHE
SEQRES 1 D 350 GLY ASN ALA ALA ALA ALA LYS LYS GLY SER GLU GLN GLU
SEQRES 2 D 350 SER VAL LYS GLU PHE LEU ALA LYS ALA LYS GLU ASP PHE
SEQRES 3 D 350 LEU LYS LYS TRP GLU THR PRO SER GLN ASN THR ALA GLN
SEQRES 4 D 350 LEU ASP GLN PHE ASP ARG ILE LYS THR LEU GLY THR GLY
SEQRES 5 D 350 SER PHE GLY ARG VAL MET LEU VAL LYS HIS LYS GLU SER
SEQRES 6 D 350 GLY ASN HIS TYR ALA MET LYS ILE LEU ASP LYS GLN LYS
SEQRES 7 D 350 VAL VAL LYS LEU LYS GLN ILE GLU HIS THR LEU ASN GLU
SEQRES 8 D 350 LYS ARG ILE LEU GLN ALA VAL ASN PHE PRO PHE LEU VAL
SEQRES 9 D 350 LYS LEU GLU PHE SER PHE LYS ASP ASN SER ASN LEU TYR
SEQRES 10 D 350 MET VAL MET GLU TYR VAL ALA GLY GLY GLU MET PHE SER
SEQRES 11 D 350 HIS LEU ARG ARG ILE GLY ARG PHE SER GLU PRO HIS ALA
SEQRES 12 D 350 ARG PHE TYR ALA ALA GLN ILE VAL LEU THR PHE GLU TYR
SEQRES 13 D 350 LEU HIS SER LEU ASP LEU ILE TYR ARG ASP LEU LYS PRO
SEQRES 14 D 350 GLU ASN LEU LEU ILE ASP GLN GLN GLY TYR ILE GLN VAL
SEQRES 15 D 350 THR ASP PHE GLY PHE ALA LYS ARG VAL LYS GLY ARG THR
SEQRES 16 D 350 TRP TPO LEU CYS GLY THR PRO GLU TYR LEU ALA PRO GLU
SEQRES 17 D 350 ILE ILE LEU SER LYS GLY TYR ASN LYS ALA VAL ASP TRP
SEQRES 18 D 350 TRP ALA LEU GLY VAL LEU ILE TYR GLU MET ALA ALA GLY
SEQRES 19 D 350 TYR PRO PRO PHE PHE ALA ASP GLN PRO ILE GLN ILE TYR
SEQRES 20 D 350 GLU LYS ILE VAL SER GLY LYS VAL ARG PHE PRO SER HIS
SEQRES 21 D 350 PHE SER SER ASP LEU LYS ASP LEU LEU ARG ASN LEU LEU
SEQRES 22 D 350 GLN VAL ASP LEU THR LYS ARG PHE GLY ASN LEU LYS ASN
SEQRES 23 D 350 GLY VAL ASN ASP ILE LYS ASN HIS LYS TRP PHE ALA THR
SEQRES 24 D 350 THR ASP TRP ILE ALA ILE TYR GLN ARG LYS VAL GLU ALA
SEQRES 25 D 350 PRO PHE ILE PRO LYS PHE LYS GLY PRO GLY ASP THR SER
SEQRES 26 D 350 ASN PHE ASP ASP TYR GLU GLU GLU GLU ILE ARG VAL SEP
SEQRES 27 D 350 ILE ASN GLU LYS CYS GLY LYS GLU PHE THR GLU PHE
SEQRES 1 I 15 VAL GLN TYR LEU THR ARG SER ALA ILE ARG ARG ALA SER
SEQRES 2 I 15 THR ILE
MODRES 3O7L TPO B 197 THR PHOSPHOTHREONINE
MODRES 3O7L TPO D 197 THR PHOSPHOTHREONINE
MODRES 3O7L SEP D 338 SER PHOSPHOSERINE
HET TPO B 197 11
HET TPO D 197 11
HET SEP D 338 10
HET MG B 351 1
HET MG B 352 1
HET PEG B 353 7
HET ANP B 354 27
HETNAM TPO PHOSPHOTHREONINE
HETNAM SEP PHOSPHOSERINE
HETNAM MG MAGNESIUM ION
HETNAM PEG DI(HYDROXYETHYL)ETHER
HETNAM ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER
HETSYN TPO PHOSPHONOTHREONINE
HETSYN SEP PHOSPHONOSERINE
FORMUL 1 TPO 2(C4 H10 N O6 P)
FORMUL 2 SEP C3 H8 N O6 P
FORMUL 4 MG 2(MG 2+)
FORMUL 6 PEG C4 H10 O3
FORMUL 7 ANP C10 H17 N6 O12 P3
FORMUL 8 HOH *21(H2 O)
HELIX 1 1 GLU B 17 GLU B 31 1 15
HELIX 2 2 GLN B 39 PHE B 43 5 5
HELIX 3 3 LYS B 76 LEU B 82 1 7
HELIX 4 4 GLN B 84 GLN B 96 1 13
HELIX 5 5 GLU B 127 GLY B 136 1 10
HELIX 6 6 SER B 139 LEU B 160 1 22
HELIX 7 7 LYS B 168 GLU B 170 5 3
HELIX 8 8 THR B 201 LEU B 205 5 5
HELIX 9 9 ALA B 206 SER B 212 1 7
HELIX 10 10 LYS B 217 GLY B 234 1 18
HELIX 11 11 GLN B 242 GLY B 253 1 12
HELIX 12 12 SER B 262 LEU B 273 1 12
HELIX 13 13 VAL B 288 ASN B 293 1 6
HELIX 14 14 HIS B 294 ALA B 298 5 5
HELIX 15 15 ASP B 301 ARG B 308 1 8
HELIX 16 16 GLY B 344 THR B 348 5 5
HELIX 17 17 GLU D 13 THR D 32 1 20
HELIX 18 18 GLN D 39 ASP D 41 5 3
HELIX 19 19 LYS D 76 LEU D 82 1 7
HELIX 20 20 GLN D 84 GLN D 96 1 13
HELIX 21 21 GLU D 127 GLY D 136 1 10
HELIX 22 22 SER D 139 LEU D 160 1 22
HELIX 23 23 LYS D 168 GLU D 170 5 3
HELIX 24 24 ALA D 206 LEU D 211 1 6
HELIX 25 25 LYS D 217 GLY D 234 1 18
HELIX 26 26 GLN D 242 GLY D 253 1 12
HELIX 27 27 SER D 262 LEU D 273 1 12
HELIX 28 28 VAL D 288 HIS D 294 1 7
HELIX 29 29 LYS D 295 ALA D 298 5 4
HELIX 30 30 ASP D 301 GLN D 307 1 7
HELIX 31 31 GLY D 344 THR D 348 5 5
SHEET 1 A 5 LYS B 47 GLY B 50 0
SHEET 2 A 5 ARG B 56 LYS B 61 -1 O VAL B 57 N LEU B 49
SHEET 3 A 5 HIS B 68 ASP B 75 -1 O MET B 71 N MET B 58
SHEET 4 A 5 ASN B 115 GLU B 121 -1 O LEU B 116 N LEU B 74
SHEET 5 A 5 LEU B 106 LYS B 111 -1 N PHE B 108 O VAL B 119
SHEET 1 B 2 LEU B 162 ILE B 163 0
SHEET 2 B 2 LYS B 189 ARG B 190 -1 O LYS B 189 N ILE B 163
SHEET 1 C 2 LEU B 172 ILE B 174 0
SHEET 2 C 2 ILE B 180 VAL B 182 -1 O GLN B 181 N ILE B 173
SHEET 1 D 5 PHE D 43 THR D 51 0
SHEET 2 D 5 GLY D 55 HIS D 62 -1 O LEU D 59 N LYS D 47
SHEET 3 D 5 HIS D 68 ASP D 75 -1 O MET D 71 N MET D 58
SHEET 4 D 5 ASN D 115 GLU D 121 -1 O MET D 120 N ALA D 70
SHEET 5 D 5 LEU D 106 LYS D 111 -1 N PHE D 108 O VAL D 119
SHEET 1 E 2 LEU D 162 ILE D 163 0
SHEET 2 E 2 LYS D 189 ARG D 190 -1 O LYS D 189 N ILE D 163
SHEET 1 F 2 LEU D 172 ILE D 174 0
SHEET 2 F 2 ILE D 180 VAL D 182 -1 O GLN D 181 N LEU D 173
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 TRP D 196 N TPO D 197 1555 1555 1.33
LINK C TPO D 197 N LEU D 198 1555 1555 1.44
LINK C VAL D 337 N SEP D 338 1555 1555 1.33
LINK C SEP D 338 N ILE D 339 1555 1555 1.33
LINK OD1 ASP B 184 MG MG B 351 1555 1555 1.73
LINK MG MG B 352 O2A ANP B 354 1555 1555 1.88
LINK OD2 ASP B 184 MG MG B 352 1555 1555 1.95
LINK MG MG B 351 O1B ANP B 354 1555 1555 2.49
LINK MG MG B 352 O1B ANP B 354 1555 1555 2.84
CISPEP 1 GLY D 322 ASP D 323 0 -7.55
SITE 1 AC1 3 ASP B 166 ASP B 184 ANP B 354
SITE 1 AC2 3 ASN B 171 ASP B 184 ANP B 354
SITE 1 AC3 4 GLY B 55 ILE B 73 LEU B 74 ASP B 75
SITE 1 AC4 18 GLY B 50 THR B 51 VAL B 57 ALA B 70
SITE 2 AC4 18 LYS B 72 MET B 120 GLU B 121 VAL B 123
SITE 3 AC4 18 GLU B 127 GLU B 170 ASN B 171 ILE B 173
SITE 4 AC4 18 THR B 183 ASP B 184 PHE B 327 MG B 351
SITE 5 AC4 18 MG B 352 ARG I 18
CRYST1 92.193 92.193 192.186 90.00 90.00 120.00 P 61 6
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 0.010847 0.006262 0.000000 0.00000
SCALE2 0.000000 0.012525 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005203 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
