HEADER METAL TRANSPORT 27-JAN-13 3W5B
TITLE CRYSTAL STRUCTURE OF THE RECOMBINANT SERCA1A (CALCIUM PUMP OF FAST
TITLE 2 TWITCH SKELETAL MUSCLE) IN THE E1.MG2+ STATE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SERCA1A;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: SARCOPLASMIC/ENDOPLASMIC RETICULUM CALCIUM ATPASE 1;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ORYCTOLAGUS CUNICULUS;
SOURCE 3 ORGANISM_TAXID: 9986;
SOURCE 4 EXPRESSION_SYSTEM: CHLOROCEBUS SABAEUS;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 60711;
SOURCE 6 EXPRESSION_SYSTEM_CELL_LINE: COS-7
KEYWDS P-TYPE ATPASE, HYDROLASE, CALCIUM TRANSPORT, CALCIUM BINDING, ATP
KEYWDS 2 BINDING, ENDOPLASMIC RETICULUM, SARCOPLASMIC RETICULUM, RECOMBINANT,
KEYWDS 3 METAL TRANSPORT
EXPDTA X-RAY DIFFRACTION
AUTHOR C.TOYOSHIMA,S.IWASAWA,H.OGAWA,A.HIRATA,J.TSUEDA,G.INESI
REVDAT 2 27-MAR-13 3W5B 1 JRNL
REVDAT 1 06-MAR-13 3W5B 0
JRNL AUTH C.TOYOSHIMA,S.IWASAWA,H.OGAWA,A.HIRATA,J.TSUEDA,G.INESI
JRNL TITL CRYSTAL STRUCTURES OF THE CALCIUM PUMP AND SARCOLIPIN IN THE
JRNL TITL 2 MG2+-BOUND E1 STATE.
JRNL REF NATURE V. 495 260 2013
JRNL REFN ISSN 0028-0836
JRNL PMID 23455422
JRNL DOI 10.1038/NATURE11899
REMARK 2
REMARK 2 RESOLUTION. 3.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.6.0117
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 15.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.2
REMARK 3 NUMBER OF REFLECTIONS : 25290
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) : 0.269
REMARK 3 R VALUE (WORKING SET) : 0.268
REMARK 3 FREE R VALUE : 0.298
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1337
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) : 3.20
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.28
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1637
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 95.15
REMARK 3 BIN R VALUE (WORKING SET) : 0.4680
REMARK 3 BIN FREE R VALUE SET COUNT : 90
REMARK 3 BIN FREE R VALUE : 0.4750
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 7689
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 117
REMARK 3 SOLVENT ATOMS : 7
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 153.20
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.00000
REMARK 3 B22 (A**2) : 0.00000
REMARK 3 B33 (A**2) : 0.00000
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): 0.542
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.630
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 74.988
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.933
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.911
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 7946 ; 0.009 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 10781 ; 1.445 ; 1.988
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 996 ; 4.495 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 319 ;43.671 ;24.357
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1384 ;19.169 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 48 ;18.043 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1248 ; 0.080 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5863 ; 0.005 ; 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): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED 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 : 9
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 -2 A 314
REMARK 3 ORIGIN FOR THE GROUP (A): 52.8930 -1.5474 31.9569
REMARK 3 T TENSOR
REMARK 3 T11: 1.7380 T22: 1.6944
REMARK 3 T33: 0.5695 T12: 0.0906
REMARK 3 T13: -0.0703 T23: 0.1147
REMARK 3 L TENSOR
REMARK 3 L11: 0.7025 L22: 0.3754
REMARK 3 L33: 2.0816 L12: 0.3942
REMARK 3 L13: -0.8938 L23: -0.1894
REMARK 3 S TENSOR
REMARK 3 S11: 0.0515 S12: 0.3070 S13: 0.1625
REMARK 3 S21: 0.1297 S22: -0.2406 S23: 0.2141
REMARK 3 S31: -0.5686 S32: -1.2897 S33: 0.1891
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 315 A 358
REMARK 3 ORIGIN FOR THE GROUP (A): 73.3793 -11.3526 36.7264
REMARK 3 T TENSOR
REMARK 3 T11: 1.7408 T22: 0.5909
REMARK 3 T33: 0.3208 T12: -0.0760
REMARK 3 T13: -0.3264 T23: 0.1455
REMARK 3 L TENSOR
REMARK 3 L11: 1.4127 L22: 0.8715
REMARK 3 L33: 7.5408 L12: 0.3267
REMARK 3 L13: -1.5701 L23: -2.4718
REMARK 3 S TENSOR
REMARK 3 S11: 0.1432 S12: -0.0066 S13: 0.0844
REMARK 3 S21: 0.2798 S22: 0.6397 S23: 0.2117
REMARK 3 S31: -0.2512 S32: -1.7355 S33: -0.7829
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 359 A 400
REMARK 3 ORIGIN FOR THE GROUP (A): 88.7117 -37.4284 66.6058
REMARK 3 T TENSOR
REMARK 3 T11: 1.8342 T22: 0.3394
REMARK 3 T33: 0.4894 T12: -0.0885
REMARK 3 T13: -0.2809 T23: 0.1086
REMARK 3 L TENSOR
REMARK 3 L11: 8.2560 L22: 0.2574
REMARK 3 L33: 7.6588 L12: -1.3843
REMARK 3 L13: 5.1439 L23: -1.0400
REMARK 3 S TENSOR
REMARK 3 S11: 0.0008 S12: -0.1408 S13: -0.0948
REMARK 3 S21: 0.0306 S22: 0.1002 S23: 0.0599
REMARK 3 S31: 0.6923 S32: -0.2277 S33: -0.1010
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 401 A 517
REMARK 3 ORIGIN FOR THE GROUP (A): 73.2767 -33.6093 72.1751
REMARK 3 T TENSOR
REMARK 3 T11: 1.5551 T22: 1.5655
REMARK 3 T33: 0.4411 T12: -0.0952
REMARK 3 T13: -0.0265 T23: 0.5967
REMARK 3 L TENSOR
REMARK 3 L11: 2.9759 L22: 3.7135
REMARK 3 L33: 3.5803 L12: -1.7858
REMARK 3 L13: 1.2899 L23: 0.5425
REMARK 3 S TENSOR
REMARK 3 S11: -0.3577 S12: -1.2649 S13: -0.5408
REMARK 3 S21: 0.4126 S22: 0.8836 S23: 0.6263
REMARK 3 S31: 0.5667 S32: -2.0163 S33: -0.5259
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 518 A 557
REMARK 3 ORIGIN FOR THE GROUP (A): 93.6662 -27.0644 74.4670
REMARK 3 T TENSOR
REMARK 3 T11: 1.5048 T22: 0.4199
REMARK 3 T33: 0.3223 T12: 0.1604
REMARK 3 T13: -0.2638 T23: -0.0288
REMARK 3 L TENSOR
REMARK 3 L11: 4.0751 L22: 5.5333
REMARK 3 L33: 11.4713 L12: -2.5519
REMARK 3 L13: 0.5660 L23: 1.5900
REMARK 3 S TENSOR
REMARK 3 S11: -0.1934 S12: 0.0540 S13: -0.0253
REMARK 3 S21: 0.4482 S22: 0.4670 S23: -0.2647
REMARK 3 S31: -0.7846 S32: -0.0100 S33: -0.2736
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 558 A 601
REMARK 3 ORIGIN FOR THE GROUP (A): 80.3551 -21.3481 78.6331
REMARK 3 T TENSOR
REMARK 3 T11: 1.8745 T22: 0.8235
REMARK 3 T33: 0.5632 T12: 0.3710
REMARK 3 T13: -0.1034 T23: 0.0025
REMARK 3 L TENSOR
REMARK 3 L11: 4.4193 L22: 0.3902
REMARK 3 L33: 3.2424 L12: 0.9512
REMARK 3 L13: 2.6595 L23: 0.0806
REMARK 3 S TENSOR
REMARK 3 S11: 0.1573 S12: -0.9214 S13: 0.5058
REMARK 3 S21: -0.0343 S22: 0.0782 S23: 0.2736
REMARK 3 S31: -0.1509 S32: -1.1552 S33: -0.2355
REMARK 3
REMARK 3 TLS GROUP : 7
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 602 A 679
REMARK 3 ORIGIN FOR THE GROUP (A): 91.2872 -12.1760 50.7420
REMARK 3 T TENSOR
REMARK 3 T11: 1.6249 T22: 0.4577
REMARK 3 T33: 0.3706 T12: -0.0204
REMARK 3 T13: -0.2215 T23: -0.0084
REMARK 3 L TENSOR
REMARK 3 L11: 1.1219 L22: 3.3265
REMARK 3 L33: 3.1850 L12: -0.7956
REMARK 3 L13: 1.2322 L23: 0.6122
REMARK 3 S TENSOR
REMARK 3 S11: -0.3934 S12: 0.2389 S13: 0.2161
REMARK 3 S21: 0.2715 S22: 0.1959 S23: -0.3056
REMARK 3 S31: 0.0491 S32: 0.2678 S33: 0.1975
REMARK 3
REMARK 3 TLS GROUP : 8
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 680 A 747
REMARK 3 ORIGIN FOR THE GROUP (A): 76.5578 -7.1741 47.6357
REMARK 3 T TENSOR
REMARK 3 T11: 1.6676 T22: 0.5139
REMARK 3 T33: 0.3446 T12: 0.0557
REMARK 3 T13: -0.1714 T23: 0.1329
REMARK 3 L TENSOR
REMARK 3 L11: 3.1106 L22: 0.8566
REMARK 3 L33: 3.9198 L12: 0.2868
REMARK 3 L13: 0.9383 L23: -1.6258
REMARK 3 S TENSOR
REMARK 3 S11: -0.1047 S12: 0.1245 S13: 0.0756
REMARK 3 S21: 0.2693 S22: 0.3650 S23: 0.1203
REMARK 3 S31: -0.5590 S32: -0.5091 S33: -0.2603
REMARK 3
REMARK 3 TLS GROUP : 9
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 748 A 994
REMARK 3 ORIGIN FOR THE GROUP (A): 74.3967 -4.9840 0.7320
REMARK 3 T TENSOR
REMARK 3 T11: 1.6401 T22: 1.0733
REMARK 3 T33: 0.1717 T12: 0.0009
REMARK 3 T13: -0.1434 T23: 0.1310
REMARK 3 L TENSOR
REMARK 3 L11: 1.7874 L22: 1.7911
REMARK 3 L33: 5.3645 L12: -0.4128
REMARK 3 L13: 0.8266 L23: -1.1459
REMARK 3 S TENSOR
REMARK 3 S11: 0.3238 S12: 0.8327 S13: 0.0549
REMARK 3 S21: -0.2409 S22: -0.2582 S23: 0.1266
REMARK 3 S31: 0.5442 S32: -0.2235 S33: -0.0655
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN USED IF PRESENT IN
REMARK 3 THE INPUT
REMARK 4
REMARK 4 3W5B COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 31-JAN-13.
REMARK 100 THE RCSB ID CODE IS RCSB095904.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
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 : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RAYONIX MX225HE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 32602
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.200
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.600
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.3
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) : 3.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.29
REMARK 200 COMPLETENESS FOR SHELL (%) : 95.6
REMARK 200 DATA REDUNDANCY IN SHELL : 3.30
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.61100
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 66.60
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.68
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
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 93.39350
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 27.64650
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 93.39350
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 27.64650
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 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 SER A -5
REMARK 465 ASP A -4
REMARK 465 ASN A -3
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 PRO A 26 -31.83 -37.46
REMARK 500 LEU A 41 172.83 -58.47
REMARK 500 ALA A 43 77.25 -61.91
REMARK 500 GLU A 58 14.56 -157.60
REMARK 500 ALA A 76 5.73 -67.44
REMARK 500 GLU A 79 -167.54 -111.76
REMARK 500 ASP A 133 -72.78 -41.66
REMARK 500 PRO A 147 105.89 -56.51
REMARK 500 VAL A 159 106.31 -56.13
REMARK 500 SER A 170 -136.07 -75.10
REMARK 500 THR A 171 -56.24 -130.76
REMARK 500 LEU A 180 -71.38 -105.34
REMARK 500 LYS A 205 30.56 -87.58
REMARK 500 SER A 210 94.27 -59.57
REMARK 500 THR A 226 -146.78 -131.82
REMARK 500 GLU A 243 39.31 -84.60
REMARK 500 ASP A 245 141.77 142.78
REMARK 500 ILE A 267 27.32 -72.82
REMARK 500 ALA A 305 -77.08 -82.49
REMARK 500 ALA A 306 -17.74 -44.45
REMARK 500 LEU A 342 -39.12 -34.54
REMARK 500 THR A 353 106.27 -55.24
REMARK 500 GLN A 360 68.40 -101.05
REMARK 500 GLU A 392 54.78 -114.98
REMARK 500 ASP A 399 18.53 82.16
REMARK 500 SER A 424 -162.79 -162.86
REMARK 500 THR A 430 -73.73 -50.72
REMARK 500 ASN A 453 74.38 45.80
REMARK 500 ASN A 456 19.27 49.23
REMARK 500 VAL A 459 -52.33 -151.55
REMARK 500 ALA A 470 -79.31 -56.44
REMARK 500 LYS A 481 96.61 -68.29
REMARK 500 PHE A 487 170.18 -51.40
REMARK 500 SER A 488 113.18 -173.89
REMARK 500 ARG A 489 1.35 -51.47
REMARK 500 LYS A 492 54.80 71.19
REMARK 500 PRO A 500 176.75 -58.83
REMARK 500 ALA A 501 -69.89 -90.41
REMARK 500 ALA A 506 99.70 -62.29
REMARK 500 VAL A 508 46.61 -104.61
REMARK 500 GLU A 519 -78.81 -7.81
REMARK 500 ARG A 556 25.14 -75.51
REMARK 500 THR A 569 59.79 -116.36
REMARK 500 ARG A 573 -11.03 -46.65
REMARK 500 GLU A 575 -17.25 -48.84
REMARK 500 ASP A 579 -45.55 -148.92
REMARK 500 VAL A 594 -77.73 -83.43
REMARK 500 ALA A 649 -50.05 -27.29
REMARK 500 SER A 693 -4.35 -56.62
REMARK 500 ASP A 703 -8.07 -159.66
REMARK 500
REMARK 500 THIS ENTRY HAS 75 RAMACHANDRAN OUTLIERS.
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 1005
REMARK 610 PTY A 1006
REMARK 610 PTY A 1007
REMARK 610 PTY A 1008
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A1003 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A1102 O
REMARK 620 2 HOH A1105 O 133.7
REMARK 620 3 HOH A1103 O 70.1 72.6
REMARK 620 4 HOH A1101 O 123.1 74.3 79.3
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A1002 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN A 768 OD1
REMARK 620 2 GLU A 771 OE1 72.4
REMARK 620 3 HOH A1107 O 95.3 137.7
REMARK 620 4 ASN A 796 OD1 111.1 68.4 79.7
REMARK 620 5 ALA A 305 O 117.5 137.0 84.9 130.1
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA A1001 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 LYS A 712 O
REMARK 620 2 GLU A 732 OE2 135.1
REMARK 620 3 GLU A 732 OE1 163.9 48.0
REMARK 620 4 LEU A 711 O 83.3 141.3 94.0
REMARK 620 5 ALA A 714 O 71.2 108.5 92.7 75.8
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 NA A 1001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1002
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1003
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TM1 A 1004
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PTY A 1005
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PTY A 1006
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PTY A 1007
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3W5A RELATED DB: PDB
REMARK 900 RELATED ID: 3W5C RELATED DB: PDB
REMARK 900 RELATED ID: 3W5D RELATED DB: PDB
DBREF 3W5B A 1 994 UNP B6CAM1 B6CAM1_RABIT 1 994
SEQADV 3W5B SER A -5 UNP B6CAM1 EXPRESSION TAG
SEQADV 3W5B ASP A -4 UNP B6CAM1 EXPRESSION TAG
SEQADV 3W5B ASN A -3 UNP B6CAM1 EXPRESSION TAG
SEQADV 3W5B ALA A -2 UNP B6CAM1 EXPRESSION TAG
SEQADV 3W5B ILE A -1 UNP B6CAM1 EXPRESSION TAG
SEQADV 3W5B ALA A 0 UNP B6CAM1 EXPRESSION TAG
SEQRES 1 A 1000 SER ASP ASN ALA ILE ALA MET GLU ALA ALA HIS SER LYS
SEQRES 2 A 1000 SER THR GLU GLU CYS LEU ALA TYR PHE GLY VAL SER GLU
SEQRES 3 A 1000 THR THR GLY LEU THR PRO ASP GLN VAL LYS ARG HIS LEU
SEQRES 4 A 1000 GLU LYS TYR GLY HIS ASN GLU LEU PRO ALA GLU GLU GLY
SEQRES 5 A 1000 LYS SER LEU TRP GLU LEU VAL ILE GLU GLN PHE GLU ASP
SEQRES 6 A 1000 LEU LEU VAL ARG ILE LEU LEU LEU ALA ALA CYS ILE SER
SEQRES 7 A 1000 PHE VAL LEU ALA TRP PHE GLU GLU GLY GLU GLU THR ILE
SEQRES 8 A 1000 THR ALA PHE VAL GLU PRO PHE VAL ILE LEU LEU ILE LEU
SEQRES 9 A 1000 ILE ALA ASN ALA ILE VAL GLY VAL TRP GLN GLU ARG ASN
SEQRES 10 A 1000 ALA GLU ASN ALA ILE GLU ALA LEU LYS GLU TYR GLU PRO
SEQRES 11 A 1000 GLU MET GLY LYS VAL TYR ARG ALA ASP ARG LYS SER VAL
SEQRES 12 A 1000 GLN ARG ILE LYS ALA ARG ASP ILE VAL PRO GLY ASP ILE
SEQRES 13 A 1000 VAL GLU VAL ALA VAL GLY ASP LYS VAL PRO ALA ASP ILE
SEQRES 14 A 1000 ARG ILE LEU SER ILE LYS SER THR THR LEU ARG VAL ASP
SEQRES 15 A 1000 GLN SER ILE LEU THR GLY GLU SER VAL SER VAL ILE LYS
SEQRES 16 A 1000 HIS THR GLU PRO VAL PRO ASP PRO ARG ALA VAL ASN GLN
SEQRES 17 A 1000 ASP LYS LYS ASN MET LEU PHE SER GLY THR ASN ILE ALA
SEQRES 18 A 1000 ALA GLY LYS ALA LEU GLY ILE VAL ALA THR THR GLY VAL
SEQRES 19 A 1000 SER THR GLU ILE GLY LYS ILE ARG ASP GLN MET ALA ALA
SEQRES 20 A 1000 THR GLU GLN ASP LYS THR PRO LEU GLN GLN LYS LEU ASP
SEQRES 21 A 1000 GLU PHE GLY GLU GLN LEU SER LYS VAL ILE SER LEU ILE
SEQRES 22 A 1000 CYS VAL ALA VAL TRP LEU ILE ASN ILE GLY HIS PHE ASN
SEQRES 23 A 1000 ASP PRO VAL HIS GLY GLY SER TRP ILE ARG GLY ALA ILE
SEQRES 24 A 1000 TYR TYR PHE LYS ILE ALA VAL ALA LEU ALA VAL ALA ALA
SEQRES 25 A 1000 ILE PRO GLU GLY LEU PRO ALA VAL ILE THR THR CYS LEU
SEQRES 26 A 1000 ALA LEU GLY THR ARG ARG MET ALA LYS LYS ASN ALA ILE
SEQRES 27 A 1000 VAL ARG SER LEU PRO SER VAL GLU THR LEU GLY CYS THR
SEQRES 28 A 1000 SER VAL ILE CYS SER ASP LYS THR GLY THR LEU THR THR
SEQRES 29 A 1000 ASN GLN MET SER VAL CYS LYS MET PHE ILE ILE ASP LYS
SEQRES 30 A 1000 VAL ASP GLY ASP PHE CYS SER LEU ASN GLU PHE SER ILE
SEQRES 31 A 1000 THR GLY SER THR TYR ALA PRO GLU GLY GLU VAL LEU LYS
SEQRES 32 A 1000 ASN ASP LYS PRO ILE ARG SER GLY GLN PHE ASP GLY LEU
SEQRES 33 A 1000 VAL GLU LEU ALA THR ILE CYS ALA LEU CYS ASN ASP SER
SEQRES 34 A 1000 SER LEU ASP PHE ASN GLU THR LYS GLY VAL TYR GLU LYS
SEQRES 35 A 1000 VAL GLY GLU ALA THR GLU THR ALA LEU THR THR LEU VAL
SEQRES 36 A 1000 GLU LYS MET ASN VAL PHE ASN THR GLU VAL ARG ASN LEU
SEQRES 37 A 1000 SER LYS VAL GLU ARG ALA ASN ALA CYS ASN SER VAL ILE
SEQRES 38 A 1000 ARG GLN LEU MET LYS LYS GLU PHE THR LEU GLU PHE SER
SEQRES 39 A 1000 ARG ASP ARG LYS SER MET SER VAL TYR CYS SER PRO ALA
SEQRES 40 A 1000 LYS SER SER ARG ALA ALA VAL GLY ASN LYS MET PHE VAL
SEQRES 41 A 1000 LYS GLY ALA PRO GLU GLY VAL ILE ASP ARG CYS ASN TYR
SEQRES 42 A 1000 VAL ARG VAL GLY THR THR ARG VAL PRO MET THR GLY PRO
SEQRES 43 A 1000 VAL LYS GLU LYS ILE LEU SER VAL ILE LYS GLU TRP GLY
SEQRES 44 A 1000 THR GLY ARG ASP THR LEU ARG CYS LEU ALA LEU ALA THR
SEQRES 45 A 1000 ARG ASP THR PRO PRO LYS ARG GLU GLU MET VAL LEU ASP
SEQRES 46 A 1000 ASP SER SER ARG PHE MET GLU TYR GLU THR ASP LEU THR
SEQRES 47 A 1000 PHE VAL GLY VAL VAL GLY MET LEU ASP PRO PRO ARG LYS
SEQRES 48 A 1000 GLU VAL MET GLY SER ILE GLN LEU CYS ARG ASP ALA GLY
SEQRES 49 A 1000 ILE ARG VAL ILE MET ILE THR GLY ASP ASN LYS GLY THR
SEQRES 50 A 1000 ALA ILE ALA ILE CYS ARG ARG ILE GLY ILE PHE GLY GLU
SEQRES 51 A 1000 ASN GLU GLU VAL ALA ASP ARG ALA TYR THR GLY ARG GLU
SEQRES 52 A 1000 PHE ASP ASP LEU PRO LEU ALA GLU GLN ARG GLU ALA CYS
SEQRES 53 A 1000 ARG ARG ALA CYS CYS PHE ALA ARG VAL GLU PRO SER HIS
SEQRES 54 A 1000 LYS SER LYS ILE VAL GLU TYR LEU GLN SER TYR ASP GLU
SEQRES 55 A 1000 ILE THR ALA MET THR GLY ASP GLY VAL ASN ASP ALA PRO
SEQRES 56 A 1000 ALA LEU LYS LYS ALA GLU ILE GLY ILE ALA MET GLY SER
SEQRES 57 A 1000 GLY THR ALA VAL ALA LYS THR ALA SER GLU MET VAL LEU
SEQRES 58 A 1000 ALA ASP ASP ASN PHE SER THR ILE VAL ALA ALA VAL GLU
SEQRES 59 A 1000 GLU GLY ARG ALA ILE TYR ASN ASN MET LYS GLN PHE ILE
SEQRES 60 A 1000 ARG TYR LEU ILE SER SER ASN VAL GLY GLU VAL VAL CYS
SEQRES 61 A 1000 ILE PHE LEU THR ALA ALA LEU GLY LEU PRO GLU ALA LEU
SEQRES 62 A 1000 ILE PRO VAL GLN LEU LEU TRP VAL ASN LEU VAL THR ASP
SEQRES 63 A 1000 GLY LEU PRO ALA THR ALA LEU GLY PHE ASN PRO PRO ASP
SEQRES 64 A 1000 LEU ASP ILE MET ASP ARG PRO PRO ARG SER PRO LYS GLU
SEQRES 65 A 1000 PRO LEU ILE SER GLY TRP LEU PHE PHE ARG TYR MET ALA
SEQRES 66 A 1000 ILE GLY GLY TYR VAL GLY ALA ALA THR VAL GLY ALA ALA
SEQRES 67 A 1000 ALA TRP TRP PHE MET TYR ALA GLU ASP GLY PRO GLY VAL
SEQRES 68 A 1000 THR TYR HIS GLN LEU THR HIS PHE MET GLN CYS THR GLU
SEQRES 69 A 1000 ASP HIS PRO HIS PHE GLU GLY LEU ASP CYS GLU ILE PHE
SEQRES 70 A 1000 GLU ALA PRO GLU PRO MET THR MET ALA LEU SER VAL LEU
SEQRES 71 A 1000 VAL THR ILE GLU MET CYS ASN ALA LEU ASN SER LEU SER
SEQRES 72 A 1000 GLU ASN GLN SER LEU MET ARG MET PRO PRO TRP VAL ASN
SEQRES 73 A 1000 ILE TRP LEU LEU GLY SER ILE CYS LEU SER MET SER LEU
SEQRES 74 A 1000 HIS PHE LEU ILE LEU TYR VAL ASP PRO LEU PRO MET ILE
SEQRES 75 A 1000 PHE LYS LEU LYS ALA LEU ASP LEU THR GLN TRP LEU MET
SEQRES 76 A 1000 VAL LEU LYS ILE SER LEU PRO VAL ILE GLY LEU ASP GLU
SEQRES 77 A 1000 ILE LEU LYS PHE ILE ALA ARG ASN TYR LEU GLU GLY
HET NA A1001 1
HET MG A1002 1
HET MG A1003 1
HET TM1 A1004 38
HET PTY A1005 19
HET PTY A1006 19
HET PTY A1007 19
HET PTY A1008 19
HETNAM NA SODIUM ION
HETNAM MG MAGNESIUM ION
HETNAM TM1 2',3'-O-[(1R)-2,4,6-TRINITROCYCLOHEXA-2,5-DIENE-1,1-
HETNAM 2 TM1 DIYL]ADENOSINE 5'-(DIHYDROGEN PHOSPHATE)
HETNAM PTY PHOSPHATIDYLETHANOLAMINE
FORMUL 2 NA NA 1+
FORMUL 3 MG 2(MG 2+)
FORMUL 5 TM1 C16 H15 N8 O13 P
FORMUL 6 PTY 4(C40 H80 N O8 P)
FORMUL 10 HOH *7(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 TYR A 36 1 12
HELIX 4 4 SER A 48 PHE A 57 1 10
HELIX 5 5 ASP A 59 LEU A 75 1 17
HELIX 6 6 THR A 84 GLU A 121 1 38
HELIX 7 7 LYS A 141 ILE A 145 5 5
HELIX 8 8 GLN A 177 GLY A 182 1 6
HELIX 9 9 THR A 247 ASN A 275 1 29
HELIX 10 10 ASP A 281 GLY A 285 5 5
HELIX 11 11 SER A 287 ILE A 307 1 21
HELIX 12 12 GLY A 310 LYS A 329 1 20
HELIX 13 13 SER A 335 CYS A 344 1 10
HELIX 14 14 ARG A 403 GLN A 406 5 4
HELIX 15 15 PHE A 407 CYS A 420 1 14
HELIX 16 16 GLU A 439 ASN A 453 1 15
HELIX 17 17 GLU A 466 ALA A 468 5 3
HELIX 18 18 ASN A 469 GLN A 477 1 9
HELIX 19 19 ALA A 517 ARG A 524 1 8
HELIX 20 20 THR A 538 THR A 554 1 17
HELIX 21 21 ASP A 580 GLU A 588 1 9
HELIX 22 22 GLU A 606 ALA A 617 1 12
HELIX 23 23 ASN A 628 ILE A 639 1 12
HELIX 24 24 GLY A 655 ASP A 660 1 6
HELIX 25 25 PRO A 662 ARG A 671 1 10
HELIX 26 26 GLU A 680 SER A 693 1 14
HELIX 27 27 GLY A 704 ASN A 706 5 3
HELIX 28 28 ASP A 707 ALA A 714 1 8
HELIX 29 29 THR A 724 THR A 729 1 6
HELIX 30 30 ASN A 739 LEU A 781 1 43
HELIX 31 31 ILE A 788 ASP A 800 1 13
HELIX 32 32 ALA A 804 ASN A 810 5 7
HELIX 33 33 SER A 830 PHE A 856 1 27
HELIX 34 34 ASP A 887 PHE A 891 5 5
HELIX 35 35 PRO A 896 SER A 915 1 20
HELIX 36 36 PRO A 926 VAL A 929 5 4
HELIX 37 37 ASN A 930 VAL A 950 1 21
HELIX 38 38 ASP A 951 PHE A 957 1 7
HELIX 39 39 ASP A 963 LEU A 975 1 13
HELIX 40 40 LEU A 975 TYR A 991 1 17
SHEET 1 A 6 GLN A 138 ILE A 140 0
SHEET 2 A 6 GLY A 127 TYR A 130 -1 N VAL A 129 O GLN A 138
SHEET 3 A 6 ILE A 150 VAL A 153 -1 O GLU A 152 N LYS A 128
SHEET 4 A 6 ALA A 219 THR A 225 -1 O ALA A 219 N VAL A 153
SHEET 5 A 6 ASP A 162 SER A 167 -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 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 THR A 625 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 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 ASP A 373 O PHE A 376
SHEET 5 D 9 LEU A 591 LEU A 600 -1 O VAL A 596 N PHE A 367
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 MET A 494 O LYS A 515
SHEET 9 D 9 MET A 479 LEU A 485 -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 VAL A 596 N PHE A 367
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 THR A 533 N VAL A 530
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 2.03
LINK MG MG A1003 O HOH A1102 1555 1555 2.23
LINK OD1 ASN A 768 MG MG A1002 1555 1555 2.31
LINK MG MG A1003 O HOH A1105 1555 1555 2.43
LINK OE1 GLU A 771 MG MG A1002 1555 1555 2.50
LINK MG MG A1002 O HOH A1107 1555 1555 2.54
LINK O LYS A 712 NA NA A1001 1555 1555 2.62
LINK OD1 ASN A 796 MG MG A1002 1555 1555 2.62
LINK O ALA A 305 MG MG A1002 1555 1555 2.63
LINK MG MG A1003 O HOH A1103 1555 1555 2.68
LINK MG MG A1003 O HOH A1101 1555 1555 2.69
LINK OE2 GLU A 732 NA NA A1001 1555 1555 2.72
LINK OE1 GLU A 732 NA NA A1001 1555 1555 2.74
LINK O LEU A 711 NA NA A1001 1555 1555 2.80
LINK O ALA A 714 NA NA A1001 1555 1555 3.07
SITE 1 AC1 5 LEU A 711 LYS A 712 ALA A 714 ALA A 730
SITE 2 AC1 5 GLU A 732
SITE 1 AC2 7 ALA A 305 ALA A 306 ASN A 768 GLU A 771
SITE 2 AC2 7 ASN A 796 ASP A 800 HOH A1107
SITE 1 AC3 5 TM1 A1004 HOH A1101 HOH A1102 HOH A1103
SITE 2 AC3 5 HOH A1105
SITE 1 AC4 13 THR A 353 PHE A 487 ARG A 489 MET A 494
SITE 2 AC4 13 LYS A 515 ARG A 560 THR A 625 GLY A 626
SITE 3 AC4 13 ARG A 678 VAL A 679 GLU A 680 MG A1003
SITE 4 AC4 13 HOH A1101
SITE 1 AC5 1 GLY A 831
SITE 1 AC6 3 MET A 923 PHE A 986 ASN A 990
SITE 1 AC7 2 TRP A 107 TRP A 932
CRYST1 186.787 55.293 178.278 90.00 118.18 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 0.005354 0.000000 0.002869 0.00000
SCALE2 0.000000 0.018085 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006364 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
