HEADER HYDROLASE/HYDROLASE INHIBITOR 24-NOV-10 3AR7
TITLE CALCIUM PUMP CRYSTAL STRUCTURE WITH BOUND TNP-ATP AND TG IN THE
TITLE 2 ABSENCE OF CA2+
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SARCOPLASMIC/ENDOPLASMIC RETICULUM CALCIUM ATPASE 1;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: SERCA1, SR CA(2+)-ATPASE 1, CALCIUM PUMP 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: RABBITS;
SOURCE 4 ORGANISM_TAXID: 9986;
SOURCE 5 TISSUE: SKELETAL MUSCLE (WHITE)
KEYWDS P-TYPE ATPASE, HYDROLASE, CALCIUM TRANSPORT, CALCIUM BINDING, ATP
KEYWDS 2 BINDING, ENDOPLASMIC RETICULUM, SARCOPLASMIC RETICULUM, HYDROLASE-
KEYWDS 3 HYDROLASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR C.TOYOSHIMA,S.YONEKURA,J.TSUEDA,S.IWASAWA
REVDAT 3 03-APR-24 3AR7 1 COMPND REMARK SEQADV HETNAM
REVDAT 3 2 1 LINK
REVDAT 2 31-JUL-13 3AR7 1 JRNL VERSN
REVDAT 1 02-FEB-11 3AR7 0
JRNL AUTH C.TOYOSHIMA,S.YONEKURA,J.TSUEDA,S.IWASAWA
JRNL TITL TRINITROPHENYL DERIVATIVES BIND DIFFERENTLY FROM PARENT
JRNL TITL 2 ADENINE NUCLEOTIDES TO CA2+-ATPASE IN THE ABSENCE OF CA2+
JRNL REF PROC.NATL.ACAD.SCI.USA V. 108 1833 2011
JRNL REFN ISSN 0027-8424
JRNL PMID 21239683
JRNL DOI 10.1073/PNAS.1017659108
REMARK 2
REMARK 2 RESOLUTION. 2.15 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0109
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) : 2.15
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 15.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 80515
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) : 0.243
REMARK 3 R VALUE (WORKING SET) : 0.241
REMARK 3 FREE R VALUE : 0.268
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 4303
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) : 2.15
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.21
REMARK 3 REFLECTION IN BIN (WORKING SET) : 5718
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 BIN R VALUE (WORKING SET) : 0.3780
REMARK 3 BIN FREE R VALUE SET COUNT : 312
REMARK 3 BIN FREE R VALUE : 0.3580
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 : 150
REMARK 3 SOLVENT ATOMS : 181
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 70.22
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.74000
REMARK 3 B22 (A**2) : 1.74000
REMARK 3 B33 (A**2) : -3.47000
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 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.185
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): NULL
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.946
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.932
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 7968 ; 0.009 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 10821 ; 1.360 ; 1.994
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 993 ; 5.283 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 319 ;37.258 ;24.357
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1382 ;17.370 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 48 ;21.364 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1251 ; 0.107 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5873 ; 0.009 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 4950 ; 0.388 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 8016 ; 0.743 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 3018 ; 1.114 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2805 ; 1.997 ; 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): 50.8940 -9.2900 82.1630
REMARK 3 T TENSOR
REMARK 3 T11: 0.3057 T22: 0.8432
REMARK 3 T33: 0.5259 T12: -0.2171
REMARK 3 T13: -0.0371 T23: 0.0580
REMARK 3 L TENSOR
REMARK 3 L11: 1.0528 L22: 2.8642
REMARK 3 L33: 11.4270 L12: 0.9268
REMARK 3 L13: 2.7020 L23: 5.3620
REMARK 3 S TENSOR
REMARK 3 S11: -0.1328 S12: 0.2904 S13: 0.0822
REMARK 3 S21: -0.4120 S22: 0.3951 S23: -0.3349
REMARK 3 S31: -0.9349 S32: 1.1911 S33: -0.2623
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 3
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 238 A 329
REMARK 3 RESIDUE RANGE : A 1011 A 1011
REMARK 3 RESIDUE RANGE : A 1013 A 1013
REMARK 3 ORIGIN FOR THE GROUP (A): 39.4680 -20.4680 80.0460
REMARK 3 T TENSOR
REMARK 3 T11: 0.3001 T22: 0.6855
REMARK 3 T33: 0.4545 T12: -0.0213
REMARK 3 T13: -0.0313 T23: -0.0616
REMARK 3 L TENSOR
REMARK 3 L11: 0.2880 L22: 0.7485
REMARK 3 L33: 3.5355 L12: -0.2666
REMARK 3 L13: 0.0754 L23: 1.0450
REMARK 3 S TENSOR
REMARK 3 S11: 0.0468 S12: 0.1711 S13: 0.1016
REMARK 3 S21: -0.1075 S22: -0.0623 S23: -0.1760
REMARK 3 S31: 0.0679 S32: 0.1069 S33: 0.0156
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 1003 A 1003
REMARK 3 ORIGIN FOR THE GROUP (A): 24.6390 -14.4640 72.6670
REMARK 3 T TENSOR
REMARK 3 T11: 0.3151 T22: 0.7422
REMARK 3 T33: 0.3503 T12: 0.0005
REMARK 3 T13: -0.1441 T23: -0.0845
REMARK 3 L TENSOR
REMARK 3 L11: 1.4455 L22: 1.1101
REMARK 3 L33: 3.5423 L12: -0.0574
REMARK 3 L13: -0.8921 L23: 0.2621
REMARK 3 S TENSOR
REMARK 3 S11: -0.0940 S12: 0.3701 S13: 0.0292
REMARK 3 S21: -0.3095 S22: -0.1512 S23: 0.0933
REMARK 3 S31: 0.0054 S32: -0.7126 S33: 0.2453
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 3
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 0 A 0
REMARK 3 RESIDUE RANGE : A 1 A 44
REMARK 3 RESIDUE RANGE : A 123 A 237
REMARK 3 ORIGIN FOR THE GROUP (A): 63.4730 -1.6140 128.8780
REMARK 3 T TENSOR
REMARK 3 T11: 0.2784 T22: 0.2704
REMARK 3 T33: 0.6307 T12: -0.0258
REMARK 3 T13: -0.1862 T23: -0.0672
REMARK 3 L TENSOR
REMARK 3 L11: 3.1677 L22: 2.7414
REMARK 3 L33: 2.9943 L12: -0.4150
REMARK 3 L13: -0.0400 L23: 0.9838
REMARK 3 S TENSOR
REMARK 3 S11: -0.1746 S12: 0.2494 S13: 0.4029
REMARK 3 S21: 0.2216 S22: 0.1276 S23: -0.2122
REMARK 3 S31: -0.1064 S32: 0.2104 S33: 0.0469
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 1000 A 1000
REMARK 3 ORIGIN FOR THE GROUP (A): 31.5890 -8.6680 119.4810
REMARK 3 T TENSOR
REMARK 3 T11: 0.2336 T22: 0.4605
REMARK 3 T33: 0.5029 T12: 0.0009
REMARK 3 T13: -0.1137 T23: -0.1182
REMARK 3 L TENSOR
REMARK 3 L11: 2.2165 L22: 0.5141
REMARK 3 L33: 2.9539 L12: -0.3757
REMARK 3 L13: -0.2786 L23: 0.2893
REMARK 3 S TENSOR
REMARK 3 S11: -0.0779 S12: 0.1392 S13: -0.0898
REMARK 3 S21: -0.0176 S22: -0.0621 S23: 0.0387
REMARK 3 S31: -0.0085 S32: -0.3463 S33: 0.1400
REMARK 3
REMARK 3 TLS GROUP : 6
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 365 A 600
REMARK 3 ORIGIN FOR THE GROUP (A): 32.7020 9.8140 146.5440
REMARK 3 T TENSOR
REMARK 3 T11: 0.1862 T22: 0.3852
REMARK 3 T33: 0.5614 T12: 0.0890
REMARK 3 T13: -0.1297 T23: -0.1955
REMARK 3 L TENSOR
REMARK 3 L11: 4.8636 L22: 1.3735
REMARK 3 L33: 4.4725 L12: 0.0341
REMARK 3 L13: 1.1518 L23: 0.1707
REMARK 3 S TENSOR
REMARK 3 S11: -0.1455 S12: -0.1386 S13: 0.5850
REMARK 3 S21: 0.0030 S22: -0.0500 S23: -0.0501
REMARK 3 S31: -0.3706 S32: -0.0828 S33: 0.1954
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 3AR7 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 07-DEC-10.
REMARK 100 THE DEPOSITION ID IS D_1000029594.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 18-MAR-07
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.1
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) : 0.9
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 : 85138
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.150
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7
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) : 2.15
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.20
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.6
REMARK 200 DATA REDUNDANCY IN SHELL : 6.50
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.50700
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.271
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 1AGV
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 64.03
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.42
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 6.1, MICRODIALYSIS, TEMPERATURE
REMARK 280 283K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y+1/2,X+1/2,Z+1/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+3/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+1/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+3/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z+1/2
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 293.16700
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 35.75750
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 35.75750
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 146.58350
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 35.75750
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 35.75750
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 439.75050
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 35.75750
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 35.75750
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 146.58350
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 35.75750
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 35.75750
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 439.75050
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 293.16700
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 VAL A 155 128.52 -39.53
REMARK 500 PRO A 391 10.30 -68.96
REMARK 500 ASP A 399 -4.63 73.50
REMARK 500 ASN A 453 70.80 49.82
REMARK 500 SER A 504 -111.95 -104.18
REMARK 500 GLU A 519 -71.10 -49.46
REMARK 500 GLU A 588 53.84 -97.58
REMARK 500 ASP A 703 -20.29 -144.04
REMARK 500 VAL A 798 -65.33 -105.70
REMARK 500 MET A 857 -80.37 -110.49
REMARK 500 VAL A 865 63.18 -109.45
REMARK 500 TYR A 867 -8.97 63.60
REMARK 500 GLU A 878 -41.96 -135.22
REMARK 500 ASP A 951 -66.47 -10.41
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 PTY A 1011
REMARK 610 PTY A 1012
REMARK 610 PTY A 1013
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 A1000 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 LEU A 711 O
REMARK 620 2 LYS A 712 O 81.3
REMARK 620 3 ALA A 714 O 101.1 89.0
REMARK 620 4 GLU A 732 OE1 108.2 157.7 108.2
REMARK 620 5 HOH A9045 O 86.5 83.1 168.1 77.6
REMARK 620 6 HOH A9065 O 169.8 91.0 71.8 81.4 99.3
REMARK 620 N 1 2 3 4 5
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 1000
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TG1 A 1003
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 128 A 1002
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PTY A 1011
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PTY A 1012
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PTY A 1013
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2AGV RELATED DB: PDB
REMARK 900 THE SAME PROTEIN WITH BOUND TG AND BHQ IN THE ABSENCE OF 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: 2ZBD RELATED DB: PDB
REMARK 900 THE SAME PROTEIN WITH BOUND CALCIUM, ADP AND ALF4
REMARK 900 RELATED ID: 3AR2 RELATED DB: PDB
REMARK 900 RELATED ID: 3AR3 RELATED DB: PDB
REMARK 900 RELATED ID: 3AR4 RELATED DB: PDB
REMARK 900 RELATED ID: 3AR5 RELATED DB: PDB
REMARK 900 RELATED ID: 3AR6 RELATED DB: PDB
REMARK 900 RELATED ID: 3AR8 RELATED DB: PDB
REMARK 900 RELATED ID: 3AR9 RELATED DB: PDB
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 UNP P04191 SHOWS THE RESUDIES 994-1001 DPEDERRK --> G IN ISOFORM
REMARK 999 SERCA1A AS NATURAL VARIATIONS.
DBREF 3AR7 A 1 994 UNP P04191 AT2A1_RABIT 1 994
SEQADV 3AR7 ACE A 0 UNP P04191 ACETYLATION
SEQADV 3AR7 GLY A 994 UNP P04191 ASP 994 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 NA A1000 1
HET TG1 A1003 46
HET 128 A1002 46
HET PTY A1011 19
HET PTY A1012 19
HET PTY A1013 19
HETNAM ACE ACETYL GROUP
HETNAM NA SODIUM ION
HETNAM TG1 OCTANOIC ACID [3S-[3ALPHA, 3ABETA, 4ALPHA, 6BETA,
HETNAM 2 TG1 6ABETA, 7BETA, 8ALPHA(Z), 9BALPHA]]-6-(ACETYLOXY)-2,3,
HETNAM 3 TG1 -3A,4,5,6,6A,7,8,9B-DECAHYDRO-3,3A-DIHYDROXY-3,6,9-
HETNAM 4 TG1 TRIMETHYL-8-[(2-METHYL-1-OXO-2-BUTENYL)OX Y]-2-OXO-4-
HETNAM 5 TG1 (1-OXOBUTOXY)-AZULENO[4,5-B]FURAN-7-YL ESTER
HETNAM 128 SPIRO(2,4,6-TRINITROBENZENE[1,2A]-2O',3O'-METHYLENE-
HETNAM 2 128 ADENINE-TRIPHOSPHATE
HETNAM PTY PHOSPHATIDYLETHANOLAMINE
HETSYN TG1 THAPSIGARGIN
FORMUL 1 ACE C2 H4 O
FORMUL 2 NA NA 1+
FORMUL 3 TG1 C34 H50 O12
FORMUL 4 128 C16 H17 N8 O19 P3
FORMUL 5 PTY 3(C40 H80 N O8 P)
FORMUL 8 HOH *181(H2 O)
HELIX 1 1 ALA A 3 LYS A 7 5 5
HELIX 2 2 SER A 8 GLY A 17 1 10
HELIX 3 3 THR A 25 GLY A 37 1 13
HELIX 4 4 SER A 48 GLN A 56 1 9
HELIX 5 5 ASP A 59 PHE A 78 1 20
HELIX 6 6 GLU A 83 PHE A 88 1 6
HELIX 7 7 PHE A 88 ASN A 111 1 24
HELIX 8 8 ASN A 114 LEU A 119 1 6
HELIX 9 9 LYS A 120 GLU A 123 5 4
HELIX 10 10 ARG A 143 ILE A 145 5 3
HELIX 11 11 GLN A 177 GLY A 182 1 6
HELIX 12 12 VAL A 200 LYS A 204 5 5
HELIX 13 13 THR A 226 SER A 229 5 4
HELIX 14 14 THR A 230 ALA A 241 1 12
HELIX 15 15 THR A 247 ILE A 274 1 28
HELIX 16 16 ASN A 275 ASP A 281 5 7
HELIX 17 17 SER A 287 ILE A 307 1 21
HELIX 18 18 GLY A 310 LYS A 329 1 20
HELIX 19 19 PRO A 337 CYS A 344 1 8
HELIX 20 20 ARG A 403 GLN A 406 5 4
HELIX 21 21 PHE A 407 CYS A 420 1 14
HELIX 22 22 GLU A 439 ASN A 453 1 15
HELIX 23 23 SER A 463 ALA A 468 1 6
HELIX 24 24 ASN A 469 GLN A 477 1 9
HELIX 25 25 ALA A 517 ARG A 524 1 8
HELIX 26 26 THR A 538 GLY A 555 1 18
HELIX 27 27 LYS A 572 MET A 576 5 5
HELIX 28 28 ASP A 580 SER A 582 5 3
HELIX 29 29 ARG A 583 GLU A 588 1 6
HELIX 30 30 GLU A 606 ALA A 617 1 12
HELIX 31 31 ASN A 628 ILE A 639 1 12
HELIX 32 32 GLY A 655 ASP A 660 1 6
HELIX 33 33 PRO A 662 ALA A 673 1 12
HELIX 34 34 GLU A 680 SER A 693 1 14
HELIX 35 35 GLY A 704 ASN A 706 5 3
HELIX 36 36 ASP A 707 ALA A 714 1 8
HELIX 37 37 THR A 724 ALA A 730 1 7
HELIX 38 38 ASN A 739 LEU A 781 1 43
HELIX 39 39 ILE A 788 VAL A 798 1 11
HELIX 40 40 ASP A 800 GLY A 808 1 9
HELIX 41 41 ASP A 815 ARG A 819 5 5
HELIX 42 42 GLY A 831 MET A 857 1 27
HELIX 43 43 CYS A 888 GLU A 892 5 5
HELIX 44 44 ALA A 893 SER A 915 1 23
HELIX 45 45 PRO A 926 VAL A 929 5 4
HELIX 46 46 ASN A 930 VAL A 950 1 21
HELIX 47 47 ASP A 951 PHE A 957 1 7
HELIX 48 48 ASP A 963 LEU A 975 1 13
HELIX 49 49 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 GLU A 152 N LYS A 128
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 ARG A 164 O ILE A 222
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 LYS A 189 0
SHEET 2 B 3 LEU A 173 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 THR A 625 1 O ILE A 622 N SER A 350
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 CYS A 675
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 ILE A 368 O ASN A 380
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 ILE A 368 O ASN A 380
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 TYR A 527 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 PHE A 427 0
SHEET 2 F 2 TYR A 434 VAL A 437 -1 O GLU A 435 N ASP A 426
SSBOND 1 CYS A 876 CYS A 888 1555 1555 2.03
LINK C ACE A 0 N MET A 1 1555 1555 1.33
LINK O LEU A 711 NA NA A1000 1555 1555 2.50
LINK O LYS A 712 NA NA A1000 1555 1555 3.04
LINK O ALA A 714 NA NA A1000 1555 1555 2.35
LINK OE1 GLU A 732 NA NA A1000 1555 1555 2.41
LINK NA NA A1000 O HOH A9045 1555 1555 2.72
LINK NA NA A1000 O HOH A9065 1555 1555 2.71
SITE 1 AC1 7 LEU A 711 LYS A 712 ALA A 714 GLY A 717
SITE 2 AC1 7 GLU A 732 HOH A9045 HOH A9065
SITE 1 AC2 11 GLU A 255 PHE A 256 GLN A 259 LEU A 260
SITE 2 AC2 11 VAL A 263 ILE A 765 VAL A 769 VAL A 772
SITE 3 AC2 11 ILE A 829 PHE A 834 HOH A9050
SITE 1 AC3 13 THR A 353 PHE A 487 ARG A 489 MET A 494
SITE 2 AC3 13 LYS A 515 ARG A 560 LEU A 562 GLY A 626
SITE 3 AC3 13 ARG A 678 HOH A9072 HOH A9122 HOH A9146
SITE 4 AC3 13 HOH A9148
SITE 1 AC4 3 ASN A 101 ALA A 313 THR A 316
SITE 1 AC5 4 SER A 921 PHE A 986 ARG A 989 ASN A 990
SITE 1 AC6 6 LEU A 273 ILE A 274 ASN A 275 ALA A 780
SITE 2 AC6 6 MET A 923 TRP A 928
CRYST1 71.515 71.515 586.334 90.00 90.00 90.00 P 41 21 2 8
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 0.013983 0.000000 0.000000 0.00000
SCALE2 0.000000 0.013983 0.000000 0.00000
SCALE3 0.000000 0.000000 0.001706 0.00000
HETATM 1 C ACE A 0 66.125 -12.174 128.429 1.00 50.17 C
ANISOU 1 C ACE A 0 5561 5208 8291 310 -1607 -1198 C
HETATM 2 O ACE A 0 66.258 -13.390 128.593 1.00 51.10 O
ANISOU 2 O ACE A 0 5795 5221 8397 406 -1584 -1252 O
HETATM 3 CH3 ACE A 0 66.651 -11.504 127.197 1.00 49.84 C
ANISOU 3 CH3 ACE A 0 5283 5374 8277 231 -1600 -1208 C
(ATOM LINES ARE NOT SHOWN.)
END
