HEADER HYDROLASE 28-MAY-10 3N8G
TITLE STRUCTURE OF THE (SR)CA2+-ATPASE CA2-E1-CAAMPPCP FORM
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SARCOPLASMIC/ENDOPLASMIC RETICULUM CALCIUM ATPASE 1 ISOFORM
COMPND 3 SERCA 1A;
COMPND 4 CHAIN: A;
COMPND 5 EC: 3.6.3.8
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ORYCTOLAGUS CUNICULUS;
SOURCE 3 ORGANISM_COMMON: EUROPEAN RABBIT,JAPANESE WHITE RABBIT,DOMESTIC
SOURCE 4 RABBIT,RABBITS;
SOURCE 5 ORGANISM_TAXID: 9986
KEYWDS ADENOSINE DIPHOSPHATE, ADENOSINE TRIPHOSPHATE, ALUMINUM COMPOUNDS,
KEYWDS 2 CALCIUM-TRANSPORTING ATPASES, CRYSTALLIZATION, CYTOSOL, FLUORIDES,
KEYWDS 3 MUSCLE FIBERS, FAST-TWITCH, PHOSPHORYLATION, PROTEIN CONFORMATION,
KEYWDS 4 SARCOPLASMIC RETICULUM CALCIUM-TRANSPORTING ATPASES, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.BUBLITZ,C.OLESEN,H.POULSEN,J.P.MORTH,J.V.MOLLER,P.NISSEN
REVDAT 6 06-SEP-23 3N8G 1 REMARK LINK
REVDAT 5 19-MAR-14 3N8G 1 REMARK
REVDAT 4 01-MAY-13 3N8G 1 JRNL
REVDAT 3 27-FEB-13 3N8G 1 JRNL
REVDAT 2 04-APR-12 3N8G 1 REMARK VERSN
REVDAT 1 08-JUN-11 3N8G 0
JRNL AUTH M.BUBLITZ,M.MUSGAARD,H.POULSEN,L.THOGERSEN,C.OLESEN,
JRNL AUTH 2 B.SCHIOTT,J.P.MORTH,J.V.MOLLER,P.NISSEN
JRNL TITL ION PATHWAYS IN THE SARCOPLASMIC RETICULUM CA2+-ATPASE.
JRNL REF J.BIOL.CHEM. V. 288 10759 2013
JRNL REFN ISSN 0021-9258
JRNL PMID 23400778
JRNL DOI 10.1074/JBC.R112.436550
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH T.L.SORENSEN,J.V.MOLLER,P.NISSEN
REMARK 1 TITL PHOSPHORYL TRANSFER AND CALCIUM ION OCCLUSION IN THE CALCIUM
REMARK 1 TITL 2 PUMP.
REMARK 1 REF SCIENCE V. 304 1672 2004
REMARK 1 REFN ISSN 0036-8075
REMARK 1 PMID 15192230
REMARK 1 DOI 10.1126/SCIENCE.1099366
REMARK 1 REFERENCE 2
REMARK 1 AUTH M.PICARD,A.M.JENSEN,T.L.SORENSEN,P.CHAMPEIL,J.V.MOLLER,
REMARK 1 AUTH 2 P.NISSEN
REMARK 1 TITL CA2+ VERSUS MG2+ COORDINATION AT THE NUCLEOTIDE-BINDING SITE
REMARK 1 TITL 2 OF THE SARCOPLASMIC RETICULUM CA2+-ATPASE.
REMARK 1 REF J.MOL.BIOL. V. 368 1 2007
REMARK 1 REFN ISSN 0022-2836
REMARK 1 PMID 17335848
REMARK 1 DOI 10.1016/J.JMB.2007.01.082
REMARK 2
REMARK 2 RESOLUTION. 2.59 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.6.1_357)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.59
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.13
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.4
REMARK 3 NUMBER OF REFLECTIONS : 54059
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.204
REMARK 3 R VALUE (WORKING SET) : 0.202
REMARK 3 FREE R VALUE : 0.246
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 2.830
REMARK 3 FREE R VALUE TEST SET COUNT : 1529
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 30.1343 - 5.7361 0.98 4884 150 0.1902 0.2236
REMARK 3 2 5.7361 - 4.5580 1.00 4870 157 0.1763 0.2414
REMARK 3 3 4.5580 - 3.9833 1.00 4854 155 0.1640 0.1914
REMARK 3 4 3.9833 - 3.6197 1.00 4824 155 0.1835 0.2151
REMARK 3 5 3.6197 - 3.3607 1.00 4876 144 0.2047 0.2824
REMARK 3 6 3.3607 - 3.1627 1.00 4778 157 0.2335 0.2908
REMARK 3 7 3.1627 - 3.0045 1.00 4855 136 0.2272 0.2418
REMARK 3 8 3.0045 - 2.8738 1.00 4842 117 0.2308 0.2972
REMARK 3 9 2.8738 - 2.7633 1.00 4896 87 0.2360 0.3209
REMARK 3 10 2.7633 - 2.6680 1.00 4829 134 0.2604 0.2771
REMARK 3 11 2.6680 - 2.5846 0.84 4022 137 0.3112 0.3592
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 : 0.33
REMARK 3 B_SOL : 80.00
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.360
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : NULL
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 77.00
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 63.75
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.44740
REMARK 3 B22 (A**2) : -5.40490
REMARK 3 B33 (A**2) : 3.95750
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 2.33250
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 : 0.007 7845
REMARK 3 ANGLE : 1.093 10646
REMARK 3 CHIRALITY : 0.076 1235
REMARK 3 PLANARITY : 0.005 1359
REMARK 3 DIHEDRAL : 16.086 2933
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 3
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: ( CHAIN A AND ( RESID 45:122 OR RESID 238:329 ) )
REMARK 3 ORIGIN FOR THE GROUP (A): -5.7089 -9.4369 64.0738
REMARK 3 T TENSOR
REMARK 3 T11: 0.5937 T22: 1.7096
REMARK 3 T33: 0.2822 T12: 0.0210
REMARK 3 T13: -0.0235 T23: -0.0225
REMARK 3 L TENSOR
REMARK 3 L11: 0.2703 L22: 0.6209
REMARK 3 L33: 0.0476 L12: -0.2486
REMARK 3 L13: -0.0006 L23: 0.0844
REMARK 3 S TENSOR
REMARK 3 S11: -0.0145 S12: -0.0772 S13: -0.0799
REMARK 3 S21: -0.1984 S22: 0.2756 S23: 0.0479
REMARK 3 S31: 0.5500 S32: 0.3655 S33: -0.2101
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: ( CHAIN A AND ( RESID 742:994 OR RESID 1003:1004 ) )
REMARK 3 ORIGIN FOR THE GROUP (A): -4.2545 9.8833 71.6019
REMARK 3 T TENSOR
REMARK 3 T11: 0.7425 T22: 2.0100
REMARK 3 T33: 0.3474 T12: -0.2183
REMARK 3 T13: -0.0200 T23: -0.2185
REMARK 3 L TENSOR
REMARK 3 L11: -0.0473 L22: 0.1650
REMARK 3 L33: 0.1960 L12: 0.0149
REMARK 3 L13: 0.0072 L23: 0.1243
REMARK 3 S TENSOR
REMARK 3 S11: -0.2255 S12: -0.4821 S13: 0.0669
REMARK 3 S21: 0.0320 S22: 0.1051 S23: -0.1591
REMARK 3 S31: -0.7251 S32: 0.6170 S33: 0.1065
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: ( CHAIN A AND ( RESID 1:44 OR RESID 123:237 OR RESID
REMARK 3 330:741 OR RESID 1001:1001 OR RESID 1006:1006 ) )
REMARK 3 ORIGIN FOR THE GROUP (A): -21.5533 -4.4779 11.6651
REMARK 3 T TENSOR
REMARK 3 T11: 0.1733 T22: 0.1465
REMARK 3 T33: 0.2311 T12: 0.0032
REMARK 3 T13: -0.0408 T23: -0.0457
REMARK 3 L TENSOR
REMARK 3 L11: 2.7830 L22: 0.5117
REMARK 3 L33: 2.4810 L12: 0.1032
REMARK 3 L13: 0.4637 L23: -0.1856
REMARK 3 S TENSOR
REMARK 3 S11: 0.3800 S12: -0.2566 S13: -0.3095
REMARK 3 S21: -0.0473 S22: -0.2713 S23: 0.1006
REMARK 3 S31: -0.0100 S32: -0.1560 S33: -0.1206
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 3N8G COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-JUN-10.
REMARK 100 THE DEPOSITION ID IS D_1000059511.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 13-JAN-04; 04-FEB-04; 04-FEB-04
REMARK 200 TEMPERATURE (KELVIN) : NULL; NULL; NULL
REMARK 200 PH : 6.8
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y; Y; Y
REMARK 200 RADIATION SOURCE : BESSY; ESRF; ESRF
REMARK 200 BEAMLINE : 14.1; ID29; ID29
REMARK 200 X-RAY GENERATOR MODEL : NULL; NULL; NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M; M; M
REMARK 200 WAVELENGTH OR RANGE (A) : NULL; NULL; NULL
REMARK 200 MONOCHROMATOR : NULL; NULL; NULL
REMARK 200 OPTICS : NULL; NULL; NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD; CCD; CCD
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH; ADSC QUANTUM 4;
REMARK 200 ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 53349
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.600
REMARK 200 RESOLUTION RANGE LOW (A) : 40.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 7.000
REMARK 200 R MERGE (I) : 0.09200
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) : 2.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.66
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 6.60
REMARK 200 R MERGE FOR SHELL (I) : 0.75000
REMARK 200 R SYM FOR SHELL (I) : 0.75000
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.800
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH; SINGLE WAVELENGTH; SINGLE
REMARK 200 WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: RE-REFINEMENT
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: PDB ENTRY 1T5S
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 69.50
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.03
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 6000, TER-BUTANOL, SODIUM ACETATE,
REMARK 280 POTASSIUM CHLORIDE, MAGNESIUM CHLORIDE, GLYCEROL, MOPS, PH 6.8,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 929KK, TEMPERATURE
REMARK 280 292K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
REMARK 290 4555 -X+1/2,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 81.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 38.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 81.00000
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 38.00000
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: 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 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 ALA A 43 -108.04 -12.64
REMARK 500 LYS A 47 -117.01 69.61
REMARK 500 ASP A 59 -156.82 -66.04
REMARK 500 LEU A 60 -69.52 -104.34
REMARK 500 PHE A 78 41.11 -80.93
REMARK 500 GLU A 79 -5.58 59.22
REMARK 500 GLU A 80 -155.85 -125.69
REMARK 500 GLU A 82 -46.40 124.48
REMARK 500 THR A 84 -79.01 -36.26
REMARK 500 VAL A 155 122.96 -30.65
REMARK 500 MET A 239 119.16 108.35
REMARK 500 ALA A 241 71.86 56.05
REMARK 500 ASP A 245 -138.63 -90.94
REMARK 500 HIS A 278 24.00 -72.16
REMARK 500 TRP A 288 27.03 -75.29
REMARK 500 ILE A 289 -40.56 -147.33
REMARK 500 LYS A 352 -64.93 -90.47
REMARK 500 THR A 355 -69.29 -103.44
REMARK 500 PRO A 391 36.77 -72.57
REMARK 500 ASN A 453 60.76 30.87
REMARK 500 ALA A 501 -81.19 -64.57
REMARK 500 LYS A 502 -6.72 -55.23
REMARK 500 ALA A 506 34.39 -79.92
REMARK 500 ALA A 507 10.08 -173.61
REMARK 500 GLU A 588 55.06 -90.54
REMARK 500 ASP A 601 79.04 -159.64
REMARK 500 GLU A 646 122.30 -26.10
REMARK 500 ASP A 695 51.74 38.74
REMARK 500 ASP A 703 -17.19 -148.56
REMARK 500 ALA A 714 175.96 -58.47
REMARK 500 PRO A 789 -51.13 -28.88
REMARK 500 MET A 857 -100.56 -104.25
REMARK 500 TYR A 858 -2.71 -53.35
REMARK 500 THR A 866 149.50 56.03
REMARK 500 TYR A 867 147.32 -35.30
REMARK 500 HIS A 868 -6.57 89.32
REMARK 500 LEU A 870 -4.42 59.96
REMARK 500 THR A 871 -59.23 107.36
REMARK 500 HIS A 872 -162.75 -125.40
REMARK 500 GLN A 875 -75.55 -68.00
REMARK 500 CYS A 876 -97.81 82.73
REMARK 500 THR A 877 -108.08 -82.07
REMARK 500 ASP A 879 91.57 61.25
REMARK 500 PRO A 881 73.33 0.67
REMARK 500 HIS A 882 87.33 -47.43
REMARK 500 PHE A 883 78.90 -115.19
REMARK 500 CYS A 888 -73.01 -76.97
REMARK 500 ILE A 890 -66.10 14.83
REMARK 500 GLU A 892 0.78 107.37
REMARK 500 SER A 915 33.17 -97.28
REMARK 500
REMARK 500 THIS ENTRY HAS 53 RAMACHANDRAN OUTLIERS.
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 ALA A 4 HIS A 5 148.40
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A1003 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 VAL A 304 O
REMARK 620 2 ALA A 305 O 89.1
REMARK 620 3 ILE A 307 O 94.4 108.9
REMARK 620 4 GLU A 309 OE1 72.0 159.6 80.9
REMARK 620 5 GLU A 309 OE2 117.2 153.5 68.4 46.4
REMARK 620 6 ASN A 796 OD1 78.0 92.3 157.5 76.6 96.0
REMARK 620 7 ASP A 800 OD2 151.1 69.7 110.7 124.6 86.3 83.3
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A1002 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 351 OD2
REMARK 620 2 THR A 353 O 77.5
REMARK 620 3 ASP A 703 OD2 73.1 84.2
REMARK 620 4 HOH A 995 O 150.5 131.6 110.0
REMARK 620 5 ACP A1001 O3G 73.5 97.8 145.2 94.6
REMARK 620 6 HOH A1023 O 77.0 151.1 75.6 75.6 87.8
REMARK 620 7 HOH A1025 O 159.5 85.3 94.3 48.9 120.4 116.3
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K A1006 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 LEU A 711 O
REMARK 620 2 LYS A 712 O 75.1
REMARK 620 3 ALA A 714 O 96.1 75.1
REMARK 620 4 GLU A 732 OE1 89.5 157.7 123.4
REMARK 620 5 GLU A 732 OE2 107.9 131.2 147.8 38.7
REMARK 620 6 HOH A1028 O 84.6 80.3 154.3 82.3 52.5
REMARK 620 7 HOH A1091 O 130.3 59.8 54.8 139.5 117.0 105.9
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A1004 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN A 768 OD1
REMARK 620 2 GLU A 771 OE2 94.1
REMARK 620 3 THR A 799 OG1 150.0 93.9
REMARK 620 4 ASP A 800 OD1 85.8 176.0 84.2
REMARK 620 5 ASP A 800 OD2 73.4 137.6 117.3 46.2
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 CA A 1002
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 1003
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 1004
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K A 1006
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACP A 1001
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1T5S RELATED DB: PDB
REMARK 900 THE SAME STRUCTURE PREVIOUSLY MODELED AS MGAMPPCP COMPLEX.
DBREF 3N8G A 1 994 UNP B6CAM1 B6CAM1_RABIT 1 994
SEQRES 1 A 994 MET GLU ALA ALA HIS SER LYS SER THR GLU GLU CYS LEU
SEQRES 2 A 994 ALA TYR PHE GLY VAL SER GLU THR THR GLY LEU THR PRO
SEQRES 3 A 994 ASP GLN VAL LYS ARG HIS LEU GLU LYS TYR GLY HIS ASN
SEQRES 4 A 994 GLU LEU PRO ALA GLU GLU GLY LYS SER LEU TRP GLU LEU
SEQRES 5 A 994 VAL ILE GLU GLN PHE GLU ASP LEU LEU VAL ARG ILE LEU
SEQRES 6 A 994 LEU LEU ALA ALA CYS ILE SER PHE VAL LEU ALA TRP PHE
SEQRES 7 A 994 GLU GLU GLY GLU GLU THR ILE THR ALA PHE VAL GLU PRO
SEQRES 8 A 994 PHE VAL ILE LEU LEU ILE LEU ILE ALA ASN ALA ILE VAL
SEQRES 9 A 994 GLY VAL TRP GLN GLU ARG ASN ALA GLU ASN ALA ILE GLU
SEQRES 10 A 994 ALA LEU LYS GLU TYR GLU PRO GLU MET GLY LYS VAL TYR
SEQRES 11 A 994 ARG ALA ASP ARG LYS SER VAL GLN ARG ILE LYS ALA ARG
SEQRES 12 A 994 ASP ILE VAL PRO GLY ASP ILE VAL GLU VAL ALA VAL GLY
SEQRES 13 A 994 ASP LYS VAL PRO ALA ASP ILE ARG ILE LEU SER ILE LYS
SEQRES 14 A 994 SER THR THR LEU ARG VAL ASP GLN SER ILE LEU THR GLY
SEQRES 15 A 994 GLU SER VAL SER VAL ILE LYS HIS THR GLU PRO VAL PRO
SEQRES 16 A 994 ASP PRO ARG ALA VAL ASN GLN ASP LYS LYS ASN MET LEU
SEQRES 17 A 994 PHE SER GLY THR ASN ILE ALA ALA GLY LYS ALA LEU GLY
SEQRES 18 A 994 ILE VAL ALA THR THR GLY VAL SER THR GLU ILE GLY LYS
SEQRES 19 A 994 ILE ARG ASP GLN MET ALA ALA THR GLU GLN ASP LYS THR
SEQRES 20 A 994 PRO LEU GLN GLN LYS LEU ASP GLU PHE GLY GLU GLN LEU
SEQRES 21 A 994 SER LYS VAL ILE SER LEU ILE CYS VAL ALA VAL TRP LEU
SEQRES 22 A 994 ILE ASN ILE GLY HIS PHE ASN ASP PRO VAL HIS GLY GLY
SEQRES 23 A 994 SER TRP ILE ARG GLY ALA ILE TYR TYR PHE LYS ILE ALA
SEQRES 24 A 994 VAL ALA LEU ALA VAL ALA ALA ILE PRO GLU GLY LEU PRO
SEQRES 25 A 994 ALA VAL ILE THR THR CYS LEU ALA LEU GLY THR ARG ARG
SEQRES 26 A 994 MET ALA LYS LYS ASN ALA ILE VAL ARG SER LEU PRO SER
SEQRES 27 A 994 VAL GLU THR LEU GLY CYS THR SER VAL ILE CYS SER ASP
SEQRES 28 A 994 LYS THR GLY THR LEU THR THR ASN GLN MET SER VAL CYS
SEQRES 29 A 994 LYS MET PHE ILE ILE ASP LYS VAL ASP GLY ASP PHE CYS
SEQRES 30 A 994 SER LEU ASN GLU PHE SER ILE THR GLY SER THR TYR ALA
SEQRES 31 A 994 PRO GLU GLY GLU VAL LEU LYS ASN ASP LYS PRO ILE ARG
SEQRES 32 A 994 SER GLY GLN PHE ASP GLY LEU VAL GLU LEU ALA THR ILE
SEQRES 33 A 994 CYS ALA LEU CYS ASN ASP SER SER LEU ASP PHE ASN GLU
SEQRES 34 A 994 THR LYS GLY VAL TYR GLU LYS VAL GLY GLU ALA THR GLU
SEQRES 35 A 994 THR ALA LEU THR THR LEU VAL GLU LYS MET ASN VAL PHE
SEQRES 36 A 994 ASN THR GLU VAL ARG ASN LEU SER LYS VAL GLU ARG ALA
SEQRES 37 A 994 ASN ALA CYS ASN SER VAL ILE ARG GLN LEU MET LYS LYS
SEQRES 38 A 994 GLU PHE THR LEU GLU PHE SER ARG ASP ARG LYS SER MET
SEQRES 39 A 994 SER VAL TYR CYS SER PRO ALA LYS SER SER ARG ALA ALA
SEQRES 40 A 994 VAL GLY ASN LYS MET PHE VAL LYS GLY ALA PRO GLU GLY
SEQRES 41 A 994 VAL ILE ASP ARG CYS ASN TYR VAL ARG VAL GLY THR THR
SEQRES 42 A 994 ARG VAL PRO MET THR GLY PRO VAL LYS GLU LYS ILE LEU
SEQRES 43 A 994 SER VAL ILE LYS GLU TRP GLY THR GLY ARG ASP THR LEU
SEQRES 44 A 994 ARG CYS LEU ALA LEU ALA THR ARG ASP THR PRO PRO LYS
SEQRES 45 A 994 ARG GLU GLU MET VAL LEU ASP ASP SER SER ARG PHE MET
SEQRES 46 A 994 GLU TYR GLU THR ASP LEU THR PHE VAL GLY VAL VAL GLY
SEQRES 47 A 994 MET LEU ASP PRO PRO ARG LYS GLU VAL MET GLY SER ILE
SEQRES 48 A 994 GLN LEU CYS ARG ASP ALA GLY ILE ARG VAL ILE MET ILE
SEQRES 49 A 994 THR GLY ASP ASN LYS GLY THR ALA ILE ALA ILE CYS ARG
SEQRES 50 A 994 ARG ILE GLY ILE PHE GLY GLU ASN GLU GLU VAL ALA ASP
SEQRES 51 A 994 ARG ALA TYR THR GLY ARG GLU PHE ASP ASP LEU PRO LEU
SEQRES 52 A 994 ALA GLU GLN ARG GLU ALA CYS ARG ARG ALA CYS CYS PHE
SEQRES 53 A 994 ALA ARG VAL GLU PRO SER HIS LYS SER LYS ILE VAL GLU
SEQRES 54 A 994 TYR LEU GLN SER TYR ASP GLU ILE THR ALA MET THR GLY
SEQRES 55 A 994 ASP GLY VAL ASN ASP ALA PRO ALA LEU LYS LYS ALA GLU
SEQRES 56 A 994 ILE GLY ILE ALA MET GLY SER GLY THR ALA VAL ALA LYS
SEQRES 57 A 994 THR ALA SER GLU MET VAL LEU ALA ASP ASP ASN PHE SER
SEQRES 58 A 994 THR ILE VAL ALA ALA VAL GLU GLU GLY ARG ALA ILE TYR
SEQRES 59 A 994 ASN ASN MET LYS GLN PHE ILE ARG TYR LEU ILE SER SER
SEQRES 60 A 994 ASN VAL GLY GLU VAL VAL CYS ILE PHE LEU THR ALA ALA
SEQRES 61 A 994 LEU GLY LEU PRO GLU ALA LEU ILE PRO VAL GLN LEU LEU
SEQRES 62 A 994 TRP VAL ASN LEU VAL THR ASP GLY LEU PRO ALA THR ALA
SEQRES 63 A 994 LEU GLY PHE ASN PRO PRO ASP LEU ASP ILE MET ASP ARG
SEQRES 64 A 994 PRO PRO ARG SER PRO LYS GLU PRO LEU ILE SER GLY TRP
SEQRES 65 A 994 LEU PHE PHE ARG TYR MET ALA ILE GLY GLY TYR VAL GLY
SEQRES 66 A 994 ALA ALA THR VAL GLY ALA ALA ALA TRP TRP PHE MET TYR
SEQRES 67 A 994 ALA GLU ASP GLY PRO GLY VAL THR TYR HIS GLN LEU THR
SEQRES 68 A 994 HIS PHE MET GLN CYS THR GLU ASP HIS PRO HIS PHE GLU
SEQRES 69 A 994 GLY LEU ASP CYS GLU ILE PHE GLU ALA PRO GLU PRO MET
SEQRES 70 A 994 THR MET ALA LEU SER VAL LEU VAL THR ILE GLU MET CYS
SEQRES 71 A 994 ASN ALA LEU ASN SER LEU SER GLU ASN GLN SER LEU MET
SEQRES 72 A 994 ARG MET PRO PRO TRP VAL ASN ILE TRP LEU LEU GLY SER
SEQRES 73 A 994 ILE CYS LEU SER MET SER LEU HIS PHE LEU ILE LEU TYR
SEQRES 74 A 994 VAL ASP PRO LEU PRO MET ILE PHE LYS LEU LYS ALA LEU
SEQRES 75 A 994 ASP LEU THR GLN TRP LEU MET VAL LEU LYS ILE SER LEU
SEQRES 76 A 994 PRO VAL ILE GLY LEU ASP GLU ILE LEU LYS PHE ILE ALA
SEQRES 77 A 994 ARG ASN TYR LEU GLU GLY
HET CA A1002 1
HET CA A1003 1
HET CA A1004 1
HET K A1006 1
HET ACP A1001 31
HETNAM CA CALCIUM ION
HETNAM K POTASSIUM ION
HETNAM ACP PHOSPHOMETHYLPHOSPHONIC ACID ADENYLATE ESTER
HETSYN ACP ADENOSINE-5'-[BETA, GAMMA-METHYLENE]TRIPHOSPHATE
FORMUL 2 CA 3(CA 2+)
FORMUL 5 K K 1+
FORMUL 6 ACP C11 H18 N5 O12 P3
FORMUL 7 HOH *92(H2 O)
HELIX 1 1 SER A 8 GLY A 17 1 10
HELIX 2 2 THR A 25 GLY A 37 1 13
HELIX 3 3 LEU A 49 GLU A 55 1 7
HELIX 4 4 LEU A 60 LEU A 75 1 16
HELIX 5 5 ILE A 85 GLU A 123 1 39
HELIX 6 6 ARG A 143 ILE A 145 5 3
HELIX 7 7 GLN A 177 GLY A 182 1 6
HELIX 8 8 VAL A 200 LYS A 204 5 5
HELIX 9 9 THR A 230 ILE A 235 1 6
HELIX 10 10 THR A 247 ASN A 275 1 29
HELIX 11 11 ASP A 281 GLY A 285 5 5
HELIX 12 12 ILE A 289 ILE A 307 1 19
HELIX 13 13 GLY A 310 LYS A 329 1 20
HELIX 14 14 PRO A 337 CYS A 344 1 8
HELIX 15 15 ARG A 403 GLN A 406 5 4
HELIX 16 16 PHE A 407 CYS A 420 1 14
HELIX 17 17 GLU A 439 ASN A 453 1 15
HELIX 18 18 SER A 463 ALA A 468 1 6
HELIX 19 19 ASN A 469 GLN A 477 1 9
HELIX 20 20 ALA A 517 ARG A 524 1 8
HELIX 21 21 THR A 538 GLY A 555 1 18
HELIX 22 22 LYS A 572 MET A 576 5 5
HELIX 23 23 ASP A 580 SER A 582 5 3
HELIX 24 24 ARG A 583 GLU A 588 1 6
HELIX 25 25 GLU A 606 ALA A 617 1 12
HELIX 26 26 ASN A 628 ILE A 639 1 12
HELIX 27 27 GLY A 655 ASP A 660 1 6
HELIX 28 28 PRO A 662 ALA A 673 1 12
HELIX 29 29 GLU A 680 SER A 693 1 14
HELIX 30 30 GLY A 704 ASN A 706 5 3
HELIX 31 31 ASP A 707 ALA A 714 1 8
HELIX 32 32 THR A 724 ALA A 730 1 7
HELIX 33 33 PHE A 740 GLY A 782 1 43
HELIX 34 34 ILE A 788 ASP A 800 1 13
HELIX 35 35 GLY A 801 LEU A 807 1 7
HELIX 36 36 GLY A 808 ASN A 810 5 3
HELIX 37 37 SER A 830 MET A 857 1 28
HELIX 38 38 ALA A 893 ALA A 912 1 20
HELIX 39 39 LEU A 913 SER A 917 5 5
HELIX 40 40 PRO A 926 VAL A 929 5 4
HELIX 41 41 ASN A 930 VAL A 950 1 21
HELIX 42 42 PRO A 952 LYS A 958 1 7
HELIX 43 43 LEU A 962 LEU A 975 1 14
HELIX 44 44 LEU A 975 TYR A 991 1 17
SHEET 1 A 6 GLN A 138 LYS A 141 0
SHEET 2 A 6 MET A 126 TYR A 130 -1 N VAL A 129 O GLN A 138
SHEET 3 A 6 ILE A 150 ALA A 154 -1 O ILE A 150 N TYR A 130
SHEET 4 A 6 LYS A 218 THR A 225 -1 O GLY A 221 N VAL A 151
SHEET 5 A 6 ASP A 162 ILE A 168 -1 N SER A 167 O LEU A 220
SHEET 6 A 6 MET A 207 LEU A 208 -1 O LEU A 208 N ILE A 163
SHEET 1 B 3 VAL A 187 ILE A 188 0
SHEET 2 B 3 ARG A 174 ASP A 176 -1 N VAL A 175 O VAL A 187
SHEET 3 B 3 ASN A 213 ALA A 216 -1 O ASN A 213 N ASP A 176
SHEET 1 C 8 ALA A 331 VAL A 333 0
SHEET 2 C 8 MET A 733 LEU A 735 -1 O VAL A 734 N ILE A 332
SHEET 3 C 8 ILE A 716 MET A 720 1 N ALA A 719 O LEU A 735
SHEET 4 C 8 THR A 698 GLY A 702 1 N MET A 700 O ILE A 718
SHEET 5 C 8 VAL A 347 ASP A 351 1 N CYS A 349 O ALA A 699
SHEET 6 C 8 ARG A 620 ILE A 624 1 O ARG A 620 N ILE A 348
SHEET 7 C 8 CYS A 675 ALA A 677 1 O PHE A 676 N MET A 623
SHEET 8 C 8 ALA A 652 THR A 654 1 N TYR A 653 O ALA A 677
SHEET 1 D 9 LYS A 400 PRO A 401 0
SHEET 2 D 9 VAL A 395 LYS A 397 -1 N LYS A 397 O LYS A 400
SHEET 3 D 9 PHE A 376 ILE A 384 -1 N SER A 383 O LEU A 396
SHEET 4 D 9 SER A 362 ASP A 373 -1 N ASP A 370 O SER A 378
SHEET 5 D 9 LEU A 591 LEU A 600 -1 O GLY A 598 N LYS A 365
SHEET 6 D 9 ARG A 560 ARG A 567 -1 N THR A 566 O THR A 592
SHEET 7 D 9 LYS A 511 GLY A 516 -1 N VAL A 514 O ALA A 565
SHEET 8 D 9 SER A 493 PRO A 500 -1 N CYS A 498 O LYS A 511
SHEET 9 D 9 MET A 479 SER A 488 -1 N PHE A 483 O TYR A 497
SHEET 1 E 7 LYS A 400 PRO A 401 0
SHEET 2 E 7 VAL A 395 LYS A 397 -1 N LYS A 397 O LYS A 400
SHEET 3 E 7 PHE A 376 ILE A 384 -1 N SER A 383 O LEU A 396
SHEET 4 E 7 SER A 362 ASP A 373 -1 N ASP A 370 O SER A 378
SHEET 5 E 7 LEU A 591 LEU A 600 -1 O GLY A 598 N LYS A 365
SHEET 6 E 7 CYS A 525 VAL A 530 1 N ARG A 529 O PHE A 593
SHEET 7 E 7 THR A 533 PRO A 536 -1 O VAL A 535 N VAL A 528
SHEET 1 F 2 SER A 424 ASN A 428 0
SHEET 2 F 2 VAL A 433 VAL A 437 -1 O GLU A 435 N ASP A 426
LINK O VAL A 304 CA CA A1003 1555 1555 2.75
LINK O ALA A 305 CA CA A1003 1555 1555 2.64
LINK O ILE A 307 CA CA A1003 1555 1555 2.51
LINK OE1 GLU A 309 CA CA A1003 1555 1555 2.62
LINK OE2 GLU A 309 CA CA A1003 1555 1555 2.94
LINK OD2 ASP A 351 CA CA A1002 1555 1555 2.63
LINK O THR A 353 CA CA A1002 1555 1555 2.34
LINK OD2 ASP A 703 CA CA A1002 1555 1555 2.58
LINK O LEU A 711 K K A1006 1555 1555 3.14
LINK O LYS A 712 K K A1006 1555 1555 3.23
LINK O ALA A 714 K K A1006 1555 1555 3.07
LINK OE1 GLU A 732 K K A1006 1555 1555 3.22
LINK OE2 GLU A 732 K K A1006 1555 1555 3.41
LINK OD1 ASN A 768 CA CA A1004 1555 1555 2.56
LINK OE2 GLU A 771 CA CA A1004 1555 1555 2.73
LINK OD1 ASN A 796 CA CA A1003 1555 1555 2.54
LINK OG1 THR A 799 CA CA A1004 1555 1555 2.64
LINK OD2 ASP A 800 CA CA A1003 1555 1555 2.81
LINK OD1 ASP A 800 CA CA A1004 1555 1555 2.52
LINK OD2 ASP A 800 CA CA A1004 1555 1555 2.97
LINK O HOH A 995 CA CA A1002 1555 1555 3.13
LINK O3G ACP A1001 CA CA A1002 1555 1555 2.43
LINK CA CA A1002 O HOH A1023 1555 1555 2.45
LINK CA CA A1002 O HOH A1025 1555 1555 2.73
LINK K K A1006 O HOH A1028 1555 1555 3.40
LINK K K A1006 O HOH A1091 1555 1555 3.43
SITE 1 AC1 6 ASP A 351 THR A 353 ASP A 703 ACP A1001
SITE 2 AC1 6 HOH A1023 HOH A1025
SITE 1 AC2 6 VAL A 304 ALA A 305 ILE A 307 GLU A 309
SITE 2 AC2 6 ASN A 796 ASP A 800
SITE 1 AC3 5 ASN A 768 GLU A 771 THR A 799 ASP A 800
SITE 2 AC3 5 GLU A 908
SITE 1 AC4 4 LEU A 711 LYS A 712 ALA A 714 GLU A 732
SITE 1 AC5 21 ASP A 351 LYS A 352 THR A 353 GLU A 442
SITE 2 AC5 21 PHE A 487 ARG A 489 MET A 494 LYS A 515
SITE 3 AC5 21 GLY A 516 ALA A 517 ARG A 560 LEU A 562
SITE 4 AC5 21 THR A 625 GLY A 626 ASP A 627 ARG A 678
SITE 5 AC5 21 LYS A 684 ASN A 706 HOH A 997 CA A1002
SITE 6 AC5 21 HOH A1046
CRYST1 162.000 76.000 151.000 90.00 108.00 90.00 C 1 2 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 0.006173 0.000000 0.002006 0.00000
SCALE2 0.000000 0.013158 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006963 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
