HEADER HYDROLASE 20-OCT-07 2ZBD
TITLE CRYSTAL STRUCTURE OF THE SR CALCIUM PUMP WITH BOUND ALUMINIUM
TITLE 2 FLUORIDE, ADP AND CALCIUM
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SARCOPLASMIC/ENDOPLASMIC RETICULUM CALCIUM ATPASE 1;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: CALCIUM PUMP 1, SERCA1, SR CA(2+)-ATPASE 1, CALCIUM-
COMPND 5 TRANSPORTING ATPASE SARCOPLASMIC RETICULUM TYPE, FAST TWITCH SKELETAL
COMPND 6 MUSCLE ISOFORM, ENDOPLASMIC RETICULUM CLASS 1/2 CA(2+) ATPASE;
COMPND 7 EC: 3.6.3.8
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ORYCTOLAGUS CUNICULUS;
SOURCE 3 ORGANISM_COMMON: RABBIT;
SOURCE 4 ORGANISM_TAXID: 9986;
SOURCE 5 TISSUE: SKELETAL MUSCLE (WHITE)
KEYWDS MEMBRANE PROTEIN, P-TYPE ATPASE, HAD FOLD, ALTERNATIVE SPLICING, ATP-
KEYWDS 2 BINDING, CALCIUM, CALCIUM TRANSPORT, ENDOPLASMIC RETICULUM,
KEYWDS 3 HYDROLASE, ION TRANSPORT, MAGNESIUM, METAL-BINDING, NUCLEOTIDE-
KEYWDS 4 BINDING, PHOSPHORYLATION, SARCOPLASMIC RETICULUM, TRANSMEMBRANE,
KEYWDS 5 TRANSPORT
EXPDTA X-RAY DIFFRACTION
AUTHOR C.TOYOSHIMA,H.NOMURA,T.TSUDA,H.OGAWA,Y.NORIMATSU
REVDAT 3 01-NOV-23 2ZBD 1 REMARK LINK
REVDAT 2 24-FEB-09 2ZBD 1 VERSN
REVDAT 1 20-NOV-07 2ZBD 0
SPRSDE 20-NOV-07 2ZBD 2Z9R
JRNL AUTH C.TOYOSHIMA,H.NOMURA,T.TSUDA
JRNL TITL LUMENAL GATING MECHANISM REVEALED IN CALCIUM PUMP CRYSTAL
JRNL TITL 2 STRUCTURES WITH PHOSPHATE ANALOGUES
JRNL REF NATURE V. 432 361 2004
JRNL REFN ISSN 0028-0836
JRNL PMID 15448704
JRNL DOI 10.1038/NATURE02981
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH C.TOYOSHIMA,M.NAKASAKO,H.NOMURA,H.OGAWA
REMARK 1 TITL CRYSTAL STRUCTURE OF THE CALCIUM PUMP OF SARCOPLASMIC
REMARK 1 TITL 2 RETICULUM AT 2.6 A RESOLUTION
REMARK 1 REF NATURE V. 405 647 2000
REMARK 1 REFN ISSN 0028-0836
REMARK 1 PMID 10864315
REMARK 1 DOI 10.1038/35015017
REMARK 1 REFERENCE 2
REMARK 1 AUTH C.TOYOSHIMA,H.NOMURA
REMARK 1 TITL STRUCTURAL CHANGES IN THE CALCIUM PUMP ACCOMPANYING THE
REMARK 1 TITL 2 DISSOCIATION OF CALCIUM
REMARK 1 REF NATURE V. 418 605 2002
REMARK 1 REFN ISSN 0028-0836
REMARK 1 PMID 12167852
REMARK 1 DOI 10.1038/NATURE00944
REMARK 1 REFERENCE 3
REMARK 1 AUTH C.TOYOSHIMA,T.MIZUTANI
REMARK 1 TITL CRYSTAL STRUCTURE OF THE CALCIUM PUMP WITH A BOUND ATP
REMARK 1 TITL 2 ANALOGUE
REMARK 1 REF NATURE V. 430 529 2004
REMARK 1 REFN ISSN 0028-0836
REMARK 1 PMID 15229613
REMARK 1 DOI 10.1038/NATURE02680
REMARK 1 REFERENCE 4
REMARK 1 AUTH K.OBARA,N.MIYASHITA,C.XU,I.TOYOSHIMA,Y.SUGITA,G.INESI,
REMARK 1 AUTH 2 C.TOYOSHIMA
REMARK 1 TITL STRUCTURAL ROLE OF COUNTERTRANSPORT REVEALED IN CA(2+) PUMP
REMARK 1 TITL 2 CRYSTAL STRUCTURE IN THE ABSENCE OF CA(2+)
REMARK 1 REF PROC.NATL.ACAD.SCI.USA V. 102 14489 2005
REMARK 1 REFN ISSN 0027-8424
REMARK 1 PMID 16150713
REMARK 1 DOI 10.1073/PNAS.0506222102
REMARK 1 REFERENCE 5
REMARK 1 AUTH M.TAKAHASHI,Y.KONDOU,C.TOYOSHIMA
REMARK 1 TITL INTERDOMAIN COMMUNICATION IN CALCIUM PUMP AS REVEALED IN THE
REMARK 1 TITL 2 CRYSTAL STRUCTURES WITH TRANSMEMBRANE INHIBITORS
REMARK 1 REF PROC.NATL.ACAD.SCI.USA V. 104 5800 2007
REMARK 1 REFN ISSN 0027-8424
REMARK 1 PMID 17389383
REMARK 1 DOI 10.1073/PNAS.0700979104
REMARK 2
REMARK 2 RESOLUTION. 2.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 12.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 58265
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) : 0.248
REMARK 3 R VALUE (WORKING SET) : 0.246
REMARK 3 FREE R VALUE : 0.271
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 3093
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.40
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.46
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2663
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 BIN R VALUE (WORKING SET) : 0.3760
REMARK 3 BIN FREE R VALUE SET COUNT : 156
REMARK 3 BIN FREE R VALUE : 0.3510
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 7674
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 144
REMARK 3 SOLVENT ATOMS : 98
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 92.57
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -4.73000
REMARK 3 B22 (A**2) : 12.10000
REMARK 3 B33 (A**2) : -11.31000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -5.97000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.328
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.244
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.246
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 22.182
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.940
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.929
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 7954 ; 0.007 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 10770 ; 1.010 ; 1.990
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 993 ; 4.722 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 319 ;35.696 ;24.357
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1382 ;16.348 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 48 ;16.924 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1245 ; 0.065 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5816 ; 0.002 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 3774 ; 0.182 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 5525 ; 0.293 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 271 ; 0.118 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): 8 ; 0.096 ; 0.200
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 31 ; 0.094 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 9 ; 0.109 ; 0.200
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 5112 ; 0.407 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 8013 ; 0.607 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 3216 ; 0.602 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2757 ; 0.969 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 6
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 45 A 122
REMARK 3 ORIGIN FOR THE GROUP (A): 71.0212 16.1036 7.2371
REMARK 3 T TENSOR
REMARK 3 T11: 0.0241 T22: 0.4233
REMARK 3 T33: -0.2472 T12: 0.1112
REMARK 3 T13: 0.0008 T23: -0.0055
REMARK 3 L TENSOR
REMARK 3 L11: 7.2821 L22: 1.2492
REMARK 3 L33: 16.4936 L12: 1.5200
REMARK 3 L13: 8.8305 L23: 1.5349
REMARK 3 S TENSOR
REMARK 3 S11: 0.5975 S12: 0.6130 S13: -0.7648
REMARK 3 S21: 0.0124 S22: 0.3864 S23: -0.1034
REMARK 3 S31: 1.8220 S32: 0.5476 S33: -0.9839
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 238 A 329
REMARK 3 ORIGIN FOR THE GROUP (A): 57.8679 21.8503 6.9987
REMARK 3 T TENSOR
REMARK 3 T11: -0.1306 T22: 0.7229
REMARK 3 T33: -0.3599 T12: -0.0636
REMARK 3 T13: 0.0193 T23: 0.1502
REMARK 3 L TENSOR
REMARK 3 L11: 4.7046 L22: 1.0569
REMARK 3 L33: 11.2157 L12: 0.3513
REMARK 3 L13: 5.3166 L23: 1.2923
REMARK 3 S TENSOR
REMARK 3 S11: 0.3819 S12: 0.5868 S13: -0.4131
REMARK 3 S21: 0.1382 S22: 0.2142 S23: 0.0584
REMARK 3 S31: 1.1708 S32: -0.5869 S33: -0.5961
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 751 A 994
REMARK 3 RESIDUE RANGE : A 995 A 996
REMARK 3 ORIGIN FOR THE GROUP (A): 61.4507 38.7967 -0.5729
REMARK 3 T TENSOR
REMARK 3 T11: -0.0667 T22: 0.6939
REMARK 3 T33: -0.5413 T12: 0.1655
REMARK 3 T13: 0.0230 T23: 0.2485
REMARK 3 L TENSOR
REMARK 3 L11: 1.2195 L22: 1.5629
REMARK 3 L33: 9.1425 L12: 0.0803
REMARK 3 L13: 0.9615 L23: 1.0822
REMARK 3 S TENSOR
REMARK 3 S11: -0.1994 S12: 0.5720 S13: 0.0627
REMARK 3 S21: -0.1741 S22: 0.1194 S23: 0.1065
REMARK 3 S31: -1.1526 S32: -0.7670 S33: 0.0801
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 1 A 44
REMARK 3 RESIDUE RANGE : A 123 A 237
REMARK 3 ORIGIN FOR THE GROUP (A): 83.3975 3.9435 52.0783
REMARK 3 T TENSOR
REMARK 3 T11: 0.0902 T22: -0.2485
REMARK 3 T33: 0.3358 T12: 0.2261
REMARK 3 T13: -0.2175 T23: -0.2091
REMARK 3 L TENSOR
REMARK 3 L11: 5.6627 L22: 1.5749
REMARK 3 L33: 2.7531 L12: -0.0754
REMARK 3 L13: 0.1395 L23: -0.2840
REMARK 3 S TENSOR
REMARK 3 S11: 0.4793 S12: 0.6641 S13: -0.8461
REMARK 3 S21: -0.2493 S22: -0.3380 S23: 0.3404
REMARK 3 S31: 0.5943 S32: 0.2922 S33: -0.1413
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 NUMBER OF COMPONENTS GROUP : 3
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 330 A 364
REMARK 3 RESIDUE RANGE : A 601 A 750
REMARK 3 RESIDUE RANGE : A 998 A 998
REMARK 3 ORIGIN FOR THE GROUP (A): 67.6244 34.5452 48.1159
REMARK 3 T TENSOR
REMARK 3 T11: 0.0316 T22: -0.2831
REMARK 3 T33: 0.0285 T12: 0.1360
REMARK 3 T13: 0.0663 T23: 0.0278
REMARK 3 L TENSOR
REMARK 3 L11: 2.2287 L22: 0.0414
REMARK 3 L33: 4.7331 L12: 0.2219
REMARK 3 L13: 0.7829 L23: -0.2157
REMARK 3 S TENSOR
REMARK 3 S11: 0.2315 S12: 0.4822 S13: 0.0737
REMARK 3 S21: 0.1510 S22: -0.1677 S23: 0.0268
REMARK 3 S31: -0.3579 S32: -0.0254 S33: -0.0639
REMARK 3
REMARK 3 TLS GROUP : 6
REMARK 3 NUMBER OF COMPONENTS GROUP : 3
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 365 A 600
REMARK 3 RESIDUE RANGE : A 997 A 997
REMARK 3 RESIDUE RANGE : A 1001 A 1002
REMARK 3 ORIGIN FOR THE GROUP (A): 83.0994 27.9923 73.0619
REMARK 3 T TENSOR
REMARK 3 T11: -0.0221 T22: -0.2449
REMARK 3 T33: 0.0421 T12: -0.1764
REMARK 3 T13: -0.0168 T23: 0.0865
REMARK 3 L TENSOR
REMARK 3 L11: 3.0833 L22: 0.5097
REMARK 3 L33: 2.5019 L12: -0.3684
REMARK 3 L13: 0.1176 L23: 0.3327
REMARK 3 S TENSOR
REMARK 3 S11: 0.2570 S12: -0.3002 S13: -0.1844
REMARK 3 S21: 0.0241 S22: -0.2313 S23: -0.0568
REMARK 3 S31: -0.1103 S32: 0.2369 S33: -0.0257
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH 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: NULL
REMARK 4
REMARK 4 2ZBD COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 23-OCT-07.
REMARK 100 THE DEPOSITION ID IS D_1000027757.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 13-JUL-05
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 6.10
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SPRING-8
REMARK 200 BEAMLINE : BL41XU
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.8
REMARK 200 MONOCHROMATOR : ROTATED-INCLINED DOUBLE- CRYSTAL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 61807
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.400
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 90.8
REMARK 200 DATA REDUNDANCY : 3.500
REMARK 200 R MERGE (I) : 0.05400
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 27.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.46
REMARK 200 COMPLETENESS FOR SHELL (%) : 58.5
REMARK 200 DATA REDUNDANCY IN SHELL : 2.90
REMARK 200 R MERGE FOR SHELL (I) : 0.35000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.700
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: PDB ENTRY 1WPE
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 69.29
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.01
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 400, PH 6.10, MICRODIALYSIS,
REMARK 280 TEMPERATURE 283K
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 81.45000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 37.55000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 81.45000
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 37.55000
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 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: 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 OD1 ASP A 351 AL ALF A 998 1.86
REMARK 500 AL ALF A 998 O3B ADP A 1002 1.96
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 LYS A 47 -93.80 -77.51
REMARK 500 LEU A 49 42.30 -100.71
REMARK 500 GLU A 82 -76.06 -59.69
REMARK 500 GLU A 83 58.52 -93.74
REMARK 500 VAL A 155 128.74 -36.98
REMARK 500 LEU A 180 -71.29 -108.17
REMARK 500 GLN A 238 -64.43 -125.05
REMARK 500 ALA A 240 52.32 -93.55
REMARK 500 THR A 388 -166.48 -79.33
REMARK 500 PRO A 391 38.44 -71.55
REMARK 500 LYS A 502 44.04 72.54
REMARK 500 SER A 503 -64.35 -135.39
REMARK 500 SER A 504 -70.06 -110.73
REMARK 500 VAL A 508 -77.69 -66.25
REMARK 500 THR A 558 63.26 37.57
REMARK 500 GLU A 588 55.48 -105.55
REMARK 500 ASP A 601 85.77 -152.94
REMARK 500 MET A 857 -88.74 -100.00
REMARK 500 ALA A 859 102.21 -56.09
REMARK 500 HIS A 872 78.02 -116.94
REMARK 500 MET A 874 36.29 -87.38
REMARK 500 CYS A 888 39.50 -90.87
REMARK 500 GLU A 889 6.74 -154.32
REMARK 500 LEU A 992 -101.18 -77.46
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 A 996 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 VAL A 304 O
REMARK 620 2 ALA A 305 O 80.9
REMARK 620 3 ILE A 307 O 92.6 112.9
REMARK 620 4 GLU A 309 OE1 111.5 166.0 74.0
REMARK 620 5 GLU A 309 OE2 64.0 141.8 84.7 48.3
REMARK 620 6 ASN A 796 OD1 75.6 86.2 156.0 90.6 71.3
REMARK 620 7 ASP A 800 OD2 153.2 77.1 109.9 89.2 130.4 87.7
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A1001 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 351 OD2
REMARK 620 2 THR A 353 O 84.6
REMARK 620 3 ASP A 703 OD1 73.3 88.2
REMARK 620 4 HOH A1038 O 85.3 165.4 78.8
REMARK 620 5 HOH A1041 O 163.2 78.7 107.4 111.4
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 995 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN A 768 OD1
REMARK 620 2 GLU A 771 OE2 87.4
REMARK 620 3 THR A 799 OG1 162.5 98.8
REMARK 620 4 ASP A 800 OD1 84.9 144.3 80.6
REMARK 620 5 GLU A 908 OE2 125.3 77.0 72.2 134.3
REMARK 620 6 HOH A1014 O 81.3 71.4 85.2 73.0 137.6
REMARK 620 7 HOH A1015 O 101.1 142.1 84.1 73.6 67.9 146.1
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 CA A 995
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 996
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 997
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ALF A 998
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP A 1002
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PC1 A 1011
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PC1 A 1012
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1SU4 RELATED DB: PDB
REMARK 900 THE SAME PROTEIN WITH BOUND CALCIUM
REMARK 900 RELATED ID: 1IWO RELATED DB: PDB
REMARK 900 THE SAME PROTEIN WITHOUT CALCIUM
REMARK 900 RELATED ID: 1VFP RELATED DB: PDB
REMARK 900 THE SAME PROTEIN WITH BOUND AMPPCP AND CALCIUM
REMARK 900 RELATED ID: 1WPG RELATED DB: PDB
REMARK 900 THE SAME PROTEIN WITH BOUND MAGNESIUM FLUORIDE AND THAPSIGARGIN IN
REMARK 900 THE ABSENCE OF CALCIUM
REMARK 900 RELATED ID: 2AGV RELATED DB: PDB
REMARK 900 THE SAME PROTEIN WITH BOUND BHQ AND THAPSIGARGIN IN THE ABSENCE OF
REMARK 900 CALCIUM
REMARK 900 RELATED ID: 2DQS RELATED DB: PDB
REMARK 900 THE SAME PROTEIN WITH BOUND AMPPCP IN THE ABSENCE OF CALCIUM
REMARK 900 RELATED ID: 2EAR RELATED DB: PDB
REMARK 900 THE SAME PROTEIN WITH BOUND TG
REMARK 900 RELATED ID: 2EAS RELATED DB: PDB
REMARK 900 THE SAME PROTEIN WITH BOUND CPA
REMARK 900 RELATED ID: 2EAT RELATED DB: PDB
REMARK 900 THE SAME PROTEIN WITH BOUND CPA AND TG
REMARK 900 RELATED ID: 2EAU RELATED DB: PDB
REMARK 900 THE SAME PROTEIN WITH BOUND CPA IN THE PRESENCE OF CURCUMIN
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THE C-TERMINAL RESIDUES IN UNP ENTRY P04191
REMARK 999 ARE FROM 994 TO 1001, DPEDERRK.
REMARK 999 IN ISOFORM SERCA1A, THERE IS ONLY ONE C-TERMINAL
REMARK 999 RESIDUE 994 GLY.
DBREF 2ZBD A 1 993 UNP P04191 AT2A1_RABIT 1 993
SEQADV 2ZBD GLY A 994 UNP P04191 SEE REMARK 999
SEQRES 1 A 995 ACE MET GLU ALA ALA HIS SER LYS SER THR GLU GLU CYS
SEQRES 2 A 995 LEU ALA TYR PHE GLY VAL SER GLU THR THR GLY LEU THR
SEQRES 3 A 995 PRO ASP GLN VAL LYS ARG HIS LEU GLU LYS TYR GLY HIS
SEQRES 4 A 995 ASN GLU LEU PRO ALA GLU GLU GLY LYS SER LEU TRP GLU
SEQRES 5 A 995 LEU VAL ILE GLU GLN PHE GLU ASP LEU LEU VAL ARG ILE
SEQRES 6 A 995 LEU LEU LEU ALA ALA CYS ILE SER PHE VAL LEU ALA TRP
SEQRES 7 A 995 PHE GLU GLU GLY GLU GLU THR ILE THR ALA PHE VAL GLU
SEQRES 8 A 995 PRO PHE VAL ILE LEU LEU ILE LEU ILE ALA ASN ALA ILE
SEQRES 9 A 995 VAL GLY VAL TRP GLN GLU ARG ASN ALA GLU ASN ALA ILE
SEQRES 10 A 995 GLU ALA LEU LYS GLU TYR GLU PRO GLU MET GLY LYS VAL
SEQRES 11 A 995 TYR ARG ALA ASP ARG LYS SER VAL GLN ARG ILE LYS ALA
SEQRES 12 A 995 ARG ASP ILE VAL PRO GLY ASP ILE VAL GLU VAL ALA VAL
SEQRES 13 A 995 GLY ASP LYS VAL PRO ALA ASP ILE ARG ILE LEU SER ILE
SEQRES 14 A 995 LYS SER THR THR LEU ARG VAL ASP GLN SER ILE LEU THR
SEQRES 15 A 995 GLY GLU SER VAL SER VAL ILE LYS HIS THR GLU PRO VAL
SEQRES 16 A 995 PRO ASP PRO ARG ALA VAL ASN GLN ASP LYS LYS ASN MET
SEQRES 17 A 995 LEU PHE SER GLY THR ASN ILE ALA ALA GLY LYS ALA LEU
SEQRES 18 A 995 GLY ILE VAL ALA THR THR GLY VAL SER THR GLU ILE GLY
SEQRES 19 A 995 LYS ILE ARG ASP GLN MET ALA ALA THR GLU GLN ASP LYS
SEQRES 20 A 995 THR PRO LEU GLN GLN LYS LEU ASP GLU PHE GLY GLU GLN
SEQRES 21 A 995 LEU SER LYS VAL ILE SER LEU ILE CYS VAL ALA VAL TRP
SEQRES 22 A 995 LEU ILE ASN ILE GLY HIS PHE ASN ASP PRO VAL HIS GLY
SEQRES 23 A 995 GLY SER TRP ILE ARG GLY ALA ILE TYR TYR PHE LYS ILE
SEQRES 24 A 995 ALA VAL ALA LEU ALA VAL ALA ALA ILE PRO GLU GLY LEU
SEQRES 25 A 995 PRO ALA VAL ILE THR THR CYS LEU ALA LEU GLY THR ARG
SEQRES 26 A 995 ARG MET ALA LYS LYS ASN ALA ILE VAL ARG SER LEU PRO
SEQRES 27 A 995 SER VAL GLU THR LEU GLY CYS THR SER VAL ILE CYS SER
SEQRES 28 A 995 ASP LYS THR GLY THR LEU THR THR ASN GLN MET SER VAL
SEQRES 29 A 995 CYS LYS MET PHE ILE ILE ASP LYS VAL ASP GLY ASP PHE
SEQRES 30 A 995 CYS SER LEU ASN GLU PHE SER ILE THR GLY SER THR TYR
SEQRES 31 A 995 ALA PRO GLU GLY GLU VAL LEU LYS ASN ASP LYS PRO ILE
SEQRES 32 A 995 ARG SER GLY GLN PHE ASP GLY LEU VAL GLU LEU ALA THR
SEQRES 33 A 995 ILE CYS ALA LEU CYS ASN ASP SER SER LEU ASP PHE ASN
SEQRES 34 A 995 GLU THR LYS GLY VAL TYR GLU LYS VAL GLY GLU ALA THR
SEQRES 35 A 995 GLU THR ALA LEU THR THR LEU VAL GLU LYS MET ASN VAL
SEQRES 36 A 995 PHE ASN THR GLU VAL ARG ASN LEU SER LYS VAL GLU ARG
SEQRES 37 A 995 ALA ASN ALA CYS ASN SER VAL ILE ARG GLN LEU MET LYS
SEQRES 38 A 995 LYS GLU PHE THR LEU GLU PHE SER ARG ASP ARG LYS SER
SEQRES 39 A 995 MET SER VAL TYR CYS SER PRO ALA LYS SER SER ARG ALA
SEQRES 40 A 995 ALA VAL GLY ASN LYS MET PHE VAL LYS GLY ALA PRO GLU
SEQRES 41 A 995 GLY VAL ILE ASP ARG CYS ASN TYR VAL ARG VAL GLY THR
SEQRES 42 A 995 THR ARG VAL PRO MET THR GLY PRO VAL LYS GLU LYS ILE
SEQRES 43 A 995 LEU SER VAL ILE LYS GLU TRP GLY THR GLY ARG ASP THR
SEQRES 44 A 995 LEU ARG CYS LEU ALA LEU ALA THR ARG ASP THR PRO PRO
SEQRES 45 A 995 LYS ARG GLU GLU MET VAL LEU ASP ASP SER SER ARG PHE
SEQRES 46 A 995 MET GLU TYR GLU THR ASP LEU THR PHE VAL GLY VAL VAL
SEQRES 47 A 995 GLY MET LEU ASP PRO PRO ARG LYS GLU VAL MET GLY SER
SEQRES 48 A 995 ILE GLN LEU CYS ARG ASP ALA GLY ILE ARG VAL ILE MET
SEQRES 49 A 995 ILE THR GLY ASP ASN LYS GLY THR ALA ILE ALA ILE CYS
SEQRES 50 A 995 ARG ARG ILE GLY ILE PHE GLY GLU ASN GLU GLU VAL ALA
SEQRES 51 A 995 ASP ARG ALA TYR THR GLY ARG GLU PHE ASP ASP LEU PRO
SEQRES 52 A 995 LEU ALA GLU GLN ARG GLU ALA CYS ARG ARG ALA CYS CYS
SEQRES 53 A 995 PHE ALA ARG VAL GLU PRO SER HIS LYS SER LYS ILE VAL
SEQRES 54 A 995 GLU TYR LEU GLN SER TYR ASP GLU ILE THR ALA MET THR
SEQRES 55 A 995 GLY ASP GLY VAL ASN ASP ALA PRO ALA LEU LYS LYS ALA
SEQRES 56 A 995 GLU ILE GLY ILE ALA MET GLY SER GLY THR ALA VAL ALA
SEQRES 57 A 995 LYS THR ALA SER GLU MET VAL LEU ALA ASP ASP ASN PHE
SEQRES 58 A 995 SER THR ILE VAL ALA ALA VAL GLU GLU GLY ARG ALA ILE
SEQRES 59 A 995 TYR ASN ASN MET LYS GLN PHE ILE ARG TYR LEU ILE SER
SEQRES 60 A 995 SER ASN VAL GLY GLU VAL VAL CYS ILE PHE LEU THR ALA
SEQRES 61 A 995 ALA LEU GLY LEU PRO GLU ALA LEU ILE PRO VAL GLN LEU
SEQRES 62 A 995 LEU TRP VAL ASN LEU VAL THR ASP GLY LEU PRO ALA THR
SEQRES 63 A 995 ALA LEU GLY PHE ASN PRO PRO ASP LEU ASP ILE MET ASP
SEQRES 64 A 995 ARG PRO PRO ARG SER PRO LYS GLU PRO LEU ILE SER GLY
SEQRES 65 A 995 TRP LEU PHE PHE ARG TYR MET ALA ILE GLY GLY TYR VAL
SEQRES 66 A 995 GLY ALA ALA THR VAL GLY ALA ALA ALA TRP TRP PHE MET
SEQRES 67 A 995 TYR ALA GLU ASP GLY PRO GLY VAL THR TYR HIS GLN LEU
SEQRES 68 A 995 THR HIS PHE MET GLN CYS THR GLU ASP HIS PRO HIS PHE
SEQRES 69 A 995 GLU GLY LEU ASP CYS GLU ILE PHE GLU ALA PRO GLU PRO
SEQRES 70 A 995 MET THR MET ALA LEU SER VAL LEU VAL THR ILE GLU MET
SEQRES 71 A 995 CYS ASN ALA LEU ASN SER LEU SER GLU ASN GLN SER LEU
SEQRES 72 A 995 MET ARG MET PRO PRO TRP VAL ASN ILE TRP LEU LEU GLY
SEQRES 73 A 995 SER ILE CYS LEU SER MET SER LEU HIS PHE LEU ILE LEU
SEQRES 74 A 995 TYR VAL ASP PRO LEU PRO MET ILE PHE LYS LEU LYS ALA
SEQRES 75 A 995 LEU ASP LEU THR GLN TRP LEU MET VAL LEU LYS ILE SER
SEQRES 76 A 995 LEU PRO VAL ILE GLY LEU ASP GLU ILE LEU LYS PHE ILE
SEQRES 77 A 995 ALA ARG ASN TYR LEU GLU GLY
HET ACE A 0 3
HET CA A 995 1
HET CA A 996 1
HET MG A 997 1
HET ALF A 998 5
HET MG A1001 1
HET ADP A1002 27
HET PC1 A1011 54
HET PC1 A1012 54
HETNAM ACE ACETYL GROUP
HETNAM CA CALCIUM ION
HETNAM MG MAGNESIUM ION
HETNAM ALF TETRAFLUOROALUMINATE ION
HETNAM ADP ADENOSINE-5'-DIPHOSPHATE
HETNAM PC1 1,2-DIACYL-SN-GLYCERO-3-PHOSPHOCHOLINE
HETSYN PC1 3-SN-PHOSPHATIDYLCHOLINE
FORMUL 1 ACE C2 H4 O
FORMUL 2 CA 2(CA 2+)
FORMUL 4 MG 2(MG 2+)
FORMUL 5 ALF AL F4 1-
FORMUL 7 ADP C10 H15 N5 O10 P2
FORMUL 8 PC1 2(C44 H88 N O8 P)
FORMUL 10 HOH *98(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 LEU A 49 1 1
HELIX 4 4 TRP A 50 PHE A 57 1 8
HELIX 5 5 ASP A 59 LEU A 75 1 17
HELIX 6 6 GLU A 80 GLU A 82 5 3
HELIX 7 7 GLU A 83 GLU A 123 1 41
HELIX 8 8 ARG A 143 ILE A 145 5 3
HELIX 9 9 GLN A 177 GLY A 182 1 6
HELIX 10 10 THR A 226 THR A 230 5 5
HELIX 11 11 THR A 247 LEU A 273 1 27
HELIX 12 12 ASN A 275 PHE A 279 5 5
HELIX 13 13 ILE A 289 ILE A 307 1 19
HELIX 14 14 GLY A 310 LYS A 329 1 20
HELIX 15 15 PRO A 337 THR A 345 1 9
HELIX 16 16 ARG A 403 GLN A 406 5 4
HELIX 17 17 PHE A 407 CYS A 420 1 14
HELIX 18 18 GLU A 439 MET A 452 1 14
HELIX 19 19 SER A 463 ALA A 468 1 6
HELIX 20 20 ASN A 469 GLN A 477 1 9
HELIX 21 21 SER A 504 VAL A 508 5 5
HELIX 22 22 ALA A 517 ARG A 524 1 8
HELIX 23 23 THR A 538 GLY A 555 1 18
HELIX 24 24 LYS A 572 MET A 576 5 5
HELIX 25 25 ARG A 583 GLU A 588 1 6
HELIX 26 26 GLU A 606 ALA A 617 1 12
HELIX 27 27 ASN A 628 ILE A 639 1 12
HELIX 28 28 GLY A 655 ASP A 660 1 6
HELIX 29 29 PRO A 662 ALA A 673 1 12
HELIX 30 30 GLU A 680 SER A 693 1 14
HELIX 31 31 GLY A 704 ASN A 706 5 3
HELIX 32 32 ASP A 707 ALA A 714 1 8
HELIX 33 33 THR A 724 ALA A 730 1 7
HELIX 34 34 PHE A 740 GLY A 782 1 43
HELIX 35 35 ILE A 788 ASP A 800 1 13
HELIX 36 36 GLY A 801 ALA A 806 1 6
HELIX 37 37 LEU A 807 ASN A 810 5 4
HELIX 38 38 SER A 830 MET A 857 1 28
HELIX 39 39 GLU A 889 GLU A 892 5 4
HELIX 40 40 ALA A 893 SER A 915 1 23
HELIX 41 41 PRO A 926 VAL A 929 5 4
HELIX 42 42 ASN A 930 VAL A 950 1 21
HELIX 43 43 PRO A 952 PHE A 957 1 6
HELIX 44 44 THR A 965 LEU A 975 1 11
HELIX 45 45 LEU A 975 ASN A 990 1 16
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 ALA A 219 N VAL A 153
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 SER A 350 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 373 O PHE A 376
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 LEU A 564 O GLY A 595
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 LEU A 485 O SER A 495
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 373 O PHE A 376
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
SSBOND 1 CYS A 876 CYS A 888 1555 1555 2.04
LINK C ACE A 0 N MET A 1 1555 1555 1.34
LINK O VAL A 304 CA CA A 996 1555 1555 2.63
LINK O ALA A 305 CA CA A 996 1555 1555 2.59
LINK O ILE A 307 CA CA A 996 1555 1555 2.28
LINK OE1 GLU A 309 CA CA A 996 1555 1555 2.71
LINK OE2 GLU A 309 CA CA A 996 1555 1555 2.64
LINK OD2 ASP A 351 MG MG A1001 1555 1555 2.43
LINK O THR A 353 MG MG A1001 1555 1555 2.18
LINK OD1 ASP A 703 MG MG A1001 1555 1555 2.12
LINK OD1 ASN A 768 CA CA A 995 1555 1555 2.37
LINK OE2 GLU A 771 CA CA A 995 1555 1555 2.37
LINK OD1 ASN A 796 CA CA A 996 1555 1555 2.25
LINK OG1 THR A 799 CA CA A 995 1555 1555 2.56
LINK OD1 ASP A 800 CA CA A 995 1555 1555 2.30
LINK OD2 ASP A 800 CA CA A 996 1555 1555 2.34
LINK OE2 GLU A 908 CA CA A 995 1555 1555 2.45
LINK CA CA A 995 O HOH A1014 1555 1555 2.37
LINK CA CA A 995 O HOH A1015 1555 1555 2.43
LINK MG MG A 997 O1B ADP A1002 1555 1555 2.13
LINK MG MG A1001 O HOH A1038 1555 1555 2.01
LINK MG MG A1001 O HOH A1041 1555 1555 2.05
SITE 1 AC1 7 ASN A 768 GLU A 771 THR A 799 ASP A 800
SITE 2 AC1 7 GLU A 908 HOH A1014 HOH A1015
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 ALF A 998 ADP A1002 HOH A1041 HOH A1046
SITE 2 AC3 5 HOH A1059
SITE 1 AC4 12 ASP A 351 LYS A 352 THR A 353 THR A 625
SITE 2 AC4 12 GLY A 626 LYS A 684 ASN A 706 MG A 997
SITE 3 AC4 12 MG A1001 ADP A1002 HOH A1038 HOH A1041
SITE 1 AC5 6 ASP A 351 THR A 353 ASP A 703 ALF A 998
SITE 2 AC5 6 HOH A1038 HOH A1041
SITE 1 AC6 20 THR A 353 GLU A 439 GLU A 442 PHE A 487
SITE 2 AC6 20 ARG A 489 MET A 494 LYS A 515 GLY A 516
SITE 3 AC6 20 ALA A 517 ARG A 560 THR A 625 GLY A 626
SITE 4 AC6 20 ASP A 627 ARG A 678 MG A 997 ALF A 998
SITE 5 AC6 20 HOH A1046 HOH A1059 HOH A1062 HOH A1077
SITE 1 AC7 8 VAL A 104 GLN A 108 ARG A 324 PHE A 809
SITE 2 AC7 8 TRP A 932 SER A 936 LEU A 946 VAL A 950
SITE 1 AC8 3 SER A 830 GLY A 831 PHE A 834
CRYST1 162.900 75.100 152.100 90.00 109.30 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 0.006139 0.000000 0.002150 0.00000
SCALE2 0.000000 0.013316 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006966 0.00000
HETATM 1 C ACE A 0 88.089 -5.513 48.527 1.00 87.18 C
HETATM 2 O ACE A 0 89.047 -6.110 49.064 1.00 87.38 O
HETATM 3 CH3 ACE A 0 88.140 -5.128 47.070 1.00 87.33 C
(ATOM LINES ARE NOT SHOWN.)
END