HEADER METAL BINDING PROTEIN 10-DEC-13 4OVN
TITLE VOLTAGE-GATED SODIUM CHANNEL 1.5 (NAV1.5) C-TERMINAL DOMAIN IN COMPLEX
TITLE 2 WITH CALMODULIN POISED FOR ACTIVATION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CALMODULIN;
COMPND 3 CHAIN: A, B, C, D, E;
COMPND 4 SYNONYM: CAM;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: SODIUM CHANNEL PROTEIN TYPE 5 SUBUNIT ALPHA;
COMPND 8 CHAIN: F, G, H, I, J;
COMPND 9 FRAGMENT: C-TERMINAL DOMAIN (UNP RESIDUE 1773-1929);
COMPND 10 SYNONYM: HH1,SODIUM CHANNEL PROTEIN CARDIAC MUSCLE SUBUNIT ALPHA,
COMPND 11 SODIUM CHANNEL PROTEIN TYPE V SUBUNIT ALPHA,VOLTAGE-GATED SODIUM
COMPND 12 CHANNEL SUBUNIT ALPHA NAV1.5;
COMPND 13 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: CALM1, CALM, CAM, CAM1, CALM2, CAM2, CAMB, CALM3, CALML2,
SOURCE 6 CAM3, CAMC, CAMIII;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PET24;
SOURCE 12 MOL_ID: 2;
SOURCE 13 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 14 ORGANISM_COMMON: HUMAN;
SOURCE 15 ORGANISM_TAXID: 9606;
SOURCE 16 GENE: SCN5A;
SOURCE 17 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 18 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 20 EXPRESSION_SYSTEM_PLASMID: PGEX-6P-1
KEYWDS SCN5A, VOLTAGE GATED SODIUM CHANNEL, CALMODULIN, METAL BINDING
KEYWDS 2 PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR S.B.GABELLI,M.A.BIANCHET,A.BOTO,J.JAKONCIC,G.F.TOMASELLI,L.M.AMZEL
REVDAT 6 27-DEC-23 4OVN 1 LINK
REVDAT 5 04-DEC-19 4OVN 1 REMARK
REVDAT 4 27-SEP-17 4OVN 1 SOURCE REMARK
REVDAT 3 08-APR-15 4OVN 1 REMARK
REVDAT 2 10-DEC-14 4OVN 1 REMARK
REVDAT 1 03-DEC-14 4OVN 0
JRNL AUTH S.B.GABELLI,A.BOTO,V.H.KUHNS,M.A.BIANCHET,F.FARINELLI,
JRNL AUTH 2 S.ARIPIRALA,J.YODER,J.JAKONCIC,G.F.TOMASELLI,L.M.AMZEL
JRNL TITL REGULATION OF THE NAV1.5 CYTOPLASMIC DOMAIN BY CALMODULIN.
JRNL REF NAT COMMUN V. 5 5126 2014
JRNL REFN ESSN 2041-1723
JRNL PMID 25370050
JRNL DOI 10.1038/NCOMMS6126
REMARK 2
REMARK 2 RESOLUTION. 2.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.6.0117
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 28.70
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.570
REMARK 3 COMPLETENESS FOR RANGE (%) : 88.2
REMARK 3 NUMBER OF REFLECTIONS : 92851
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) : 0.215
REMARK 3 R VALUE (WORKING SET) : 0.211
REMARK 3 FREE R VALUE : 0.282
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.940
REMARK 3 FREE R VALUE TEST SET COUNT : 4588
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 30
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.80
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.83
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1694
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 52.00
REMARK 3 BIN R VALUE (WORKING SET) : 0.3670
REMARK 3 BIN FREE R VALUE SET COUNT : 91
REMARK 3 BIN FREE R VALUE : 0.4318
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 11669
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 53
REMARK 3 SOLVENT ATOMS : 62
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 77.01
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 93.06
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
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): NULL
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.480
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 : NULL
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): NULL ; NULL ; NULL
REMARK 3 GENERAL PLANES REFINED ATOMS (A): NULL ; NULL ; NULL
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 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
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 : 10
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 4 A 148
REMARK 3 ORIGIN FOR THE GROUP (A): 96.0027 20.0391 14.9656
REMARK 3 T TENSOR
REMARK 3 T11: 0.6199 T22: 0.7918
REMARK 3 T33: 0.8494 T12: 0.0241
REMARK 3 T13: 0.0242 T23: 0.0227
REMARK 3 L TENSOR
REMARK 3 L11: 1.2472 L22: 1.1519
REMARK 3 L33: 1.2544 L12: -0.1763
REMARK 3 L13: -0.3457 L23: 0.2233
REMARK 3 S TENSOR
REMARK 3 S11: 0.0199 S12: -0.0536 S13: 0.3706
REMARK 3 S21: -0.1441 S22: 0.0583 S23: -0.2979
REMARK 3 S31: 0.0457 S32: 0.2834 S33: 0.0001
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 : F 1782 F 1927
REMARK 3 ORIGIN FOR THE GROUP (A): 87.2731 35.1310 26.2727
REMARK 3 T TENSOR
REMARK 3 T11: 0.6254 T22: 0.7156
REMARK 3 T33: 0.9960 T12: -0.0447
REMARK 3 T13: -0.0360 T23: -0.0948
REMARK 3 L TENSOR
REMARK 3 L11: 0.5639 L22: 1.6978
REMARK 3 L33: 1.2404 L12: -0.4476
REMARK 3 L13: -0.6387 L23: 0.8350
REMARK 3 S TENSOR
REMARK 3 S11: 0.0778 S12: -0.0981 S13: 0.5384
REMARK 3 S21: 0.1282 S22: 0.1511 S23: -0.2335
REMARK 3 S31: -0.0856 S32: 0.2770 S33: -0.0000
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 : B 5 B 148
REMARK 3 ORIGIN FOR THE GROUP (A): 60.6924 50.6890 24.7351
REMARK 3 T TENSOR
REMARK 3 T11: 0.9796 T22: 0.8584
REMARK 3 T33: 0.8955 T12: -0.1064
REMARK 3 T13: 0.1772 T23: -0.0845
REMARK 3 L TENSOR
REMARK 3 L11: 1.3169 L22: 2.4577
REMARK 3 L33: 0.2897 L12: 0.1627
REMARK 3 L13: -0.1910 L23: 0.7805
REMARK 3 S TENSOR
REMARK 3 S11: -0.1718 S12: 0.4368 S13: -0.0324
REMARK 3 S21: -0.4677 S22: 0.3175 S23: -0.3596
REMARK 3 S31: -0.0684 S32: 0.0466 S33: -0.0000
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 : G 1783 G 1926
REMARK 3 ORIGIN FOR THE GROUP (A): 43.8549 38.5329 23.8563
REMARK 3 T TENSOR
REMARK 3 T11: 0.8268 T22: 0.7484
REMARK 3 T33: 0.6209 T12: -0.0560
REMARK 3 T13: -0.0301 T23: -0.0605
REMARK 3 L TENSOR
REMARK 3 L11: 1.2859 L22: 1.2155
REMARK 3 L33: 0.5794 L12: 0.2376
REMARK 3 L13: 0.1840 L23: 0.4699
REMARK 3 S TENSOR
REMARK 3 S11: 0.0937 S12: 0.2908 S13: 0.1375
REMARK 3 S21: -0.3480 S22: 0.1304 S23: -0.1982
REMARK 3 S31: -0.0939 S32: -0.0080 S33: -0.0000
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 : C 4 C 148
REMARK 3 ORIGIN FOR THE GROUP (A): 12.1423 47.0720 76.5033
REMARK 3 T TENSOR
REMARK 3 T11: 0.7894 T22: 0.7900
REMARK 3 T33: 0.7351 T12: -0.0183
REMARK 3 T13: -0.0007 T23: -0.0674
REMARK 3 L TENSOR
REMARK 3 L11: 1.4464 L22: 1.6366
REMARK 3 L33: 1.6185 L12: -0.3555
REMARK 3 L13: -0.7068 L23: -0.6544
REMARK 3 S TENSOR
REMARK 3 S11: -0.2538 S12: -0.0846 S13: 0.0254
REMARK 3 S21: 0.1148 S22: 0.2349 S23: -0.2133
REMARK 3 S31: 0.1512 S32: 0.1750 S33: -0.0001
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 : H 1778 H 1927
REMARK 3 ORIGIN FOR THE GROUP (A): -7.8519 49.5181 71.5899
REMARK 3 T TENSOR
REMARK 3 T11: 0.7398 T22: 0.8518
REMARK 3 T33: 0.5421 T12: -0.1180
REMARK 3 T13: -0.0451 T23: 0.0101
REMARK 3 L TENSOR
REMARK 3 L11: 0.9905 L22: 1.6722
REMARK 3 L33: 0.6848 L12: -0.5253
REMARK 3 L13: -0.2055 L23: -0.6265
REMARK 3 S TENSOR
REMARK 3 S11: -0.1071 S12: 0.2591 S13: 0.3587
REMARK 3 S21: -0.2232 S22: 0.2175 S23: 0.0072
REMARK 3 S31: 0.1116 S32: -0.1132 S33: -0.0001
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 : D 4 D 148
REMARK 3 ORIGIN FOR THE GROUP (A): 32.5196 15.0182 43.4544
REMARK 3 T TENSOR
REMARK 3 T11: 0.8119 T22: 0.7112
REMARK 3 T33: 0.7852 T12: -0.0615
REMARK 3 T13: -0.0150 T23: -0.0084
REMARK 3 L TENSOR
REMARK 3 L11: 0.8448 L22: 0.9999
REMARK 3 L33: 1.4633 L12: -0.4697
REMARK 3 L13: 0.4363 L23: -0.5602
REMARK 3 S TENSOR
REMARK 3 S11: -0.1040 S12: 0.0792 S13: -0.1456
REMARK 3 S21: -0.3489 S22: 0.1069 S23: 0.0953
REMARK 3 S31: 0.4328 S32: -0.0273 S33: 0.0000
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 : I 1784 I 1926
REMARK 3 ORIGIN FOR THE GROUP (A): 28.4434 22.6455 62.4738
REMARK 3 T TENSOR
REMARK 3 T11: 0.6173 T22: 0.6140
REMARK 3 T33: 0.6895 T12: 0.0432
REMARK 3 T13: -0.0445 T23: -0.0255
REMARK 3 L TENSOR
REMARK 3 L11: 0.7525 L22: 0.6649
REMARK 3 L33: 2.4367 L12: -0.1704
REMARK 3 L13: 0.5509 L23: -0.5404
REMARK 3 S TENSOR
REMARK 3 S11: -0.1072 S12: -0.1044 S13: 0.1054
REMARK 3 S21: 0.1740 S22: 0.1082 S23: 0.2269
REMARK 3 S31: 0.0936 S32: 0.1841 S33: -0.0000
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 : E 5 E 148
REMARK 3 ORIGIN FOR THE GROUP (A): 100.4409 30.0996 -35.7531
REMARK 3 T TENSOR
REMARK 3 T11: 0.8378 T22: 1.0931
REMARK 3 T33: 0.8827 T12: -0.0166
REMARK 3 T13: 0.0193 T23: 0.2116
REMARK 3 L TENSOR
REMARK 3 L11: 2.1343 L22: 1.7072
REMARK 3 L33: 1.1196 L12: 0.9215
REMARK 3 L13: 0.1301 L23: -0.6108
REMARK 3 S TENSOR
REMARK 3 S11: -0.2287 S12: 0.8539 S13: 0.2898
REMARK 3 S21: -0.4364 S22: 0.0820 S23: 0.1597
REMARK 3 S31: 0.2937 S32: 0.1849 S33: 0.0000
REMARK 3
REMARK 3 TLS GROUP : 10
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : J 1776 J 1926
REMARK 3 ORIGIN FOR THE GROUP (A): 93.9255 18.5753 -18.9198
REMARK 3 T TENSOR
REMARK 3 T11: 0.6952 T22: 0.7088
REMARK 3 T33: 0.6244 T12: -0.0040
REMARK 3 T13: -0.0628 T23: 0.0200
REMARK 3 L TENSOR
REMARK 3 L11: 1.3719 L22: 1.0020
REMARK 3 L33: 1.1741 L12: 1.0955
REMARK 3 L13: -0.6613 L23: -0.5375
REMARK 3 S TENSOR
REMARK 3 S11: -0.0931 S12: 0.2825 S13: -0.0262
REMARK 3 S21: -0.0528 S22: 0.1054 S23: 0.1738
REMARK 3 S31: 0.2563 S32: 0.0254 S33: -0.0001
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.11
REMARK 3 ION PROBE RADIUS : NULL
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4OVN COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 21-NOV-14.
REMARK 100 THE DEPOSITION ID IS D_1000200030.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 07-APR-10
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 : APS
REMARK 200 BEAMLINE : 31-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : NULL
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9792
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 48516
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.798
REMARK 200 RESOLUTION RANGE LOW (A) : 28.900
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 90.3
REMARK 200 DATA REDUNDANCY : 6.400
REMARK 200 R MERGE (I) : 0.11600
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.85
REMARK 200 COMPLETENESS FOR SHELL (%) : 58.3
REMARK 200 DATA REDUNDANCY IN SHELL : 4.30
REMARK 200 R MERGE FOR SHELL (I) : 0.74500
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 59.90
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.07
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 15% PEG 4K, 0.2 M MGSO4 AND 10%
REMARK 280 GLYCEROL, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 49.50300
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2900 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 17330 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -17.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, F
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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2840 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 16810 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -18.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, G
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 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2800 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 17340 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -16.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, H
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 350
REMARK 350 BIOMOLECULE: 4
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2710 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 17050 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -20.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, I
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 5
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2990 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 17200 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -17.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, J
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 MSE A 1
REMARK 465 ALA A 2
REMARK 465 ASP A 3
REMARK 465 LYS A 149
REMARK 465 GLU F 1773
REMARK 465 ASN F 1774
REMARK 465 PHE F 1775
REMARK 465 SER F 1776
REMARK 465 VAL F 1777
REMARK 465 ALA F 1778
REMARK 465 THR F 1779
REMARK 465 GLU F 1780
REMARK 465 GLU F 1781
REMARK 465 PHE F 1928
REMARK 465 ARG F 1929
REMARK 465 MSE B 1
REMARK 465 ALA B 2
REMARK 465 ASP B 3
REMARK 465 GLN B 4
REMARK 465 LYS B 149
REMARK 465 GLU G 1773
REMARK 465 ASN G 1774
REMARK 465 PHE G 1775
REMARK 465 SER G 1776
REMARK 465 VAL G 1777
REMARK 465 ALA G 1778
REMARK 465 THR G 1779
REMARK 465 GLU G 1780
REMARK 465 GLU G 1781
REMARK 465 SER G 1782
REMARK 465 LEU G 1927
REMARK 465 PHE G 1928
REMARK 465 ARG G 1929
REMARK 465 MSE C 1
REMARK 465 ALA C 2
REMARK 465 ASP C 3
REMARK 465 LYS C 149
REMARK 465 GLU H 1773
REMARK 465 ASN H 1774
REMARK 465 PHE H 1775
REMARK 465 SER H 1776
REMARK 465 PHE H 1928
REMARK 465 ARG H 1929
REMARK 465 MSE D 1
REMARK 465 ALA D 2
REMARK 465 ASP D 3
REMARK 465 LYS D 149
REMARK 465 GLU I 1773
REMARK 465 ASN I 1774
REMARK 465 PHE I 1775
REMARK 465 SER I 1776
REMARK 465 VAL I 1777
REMARK 465 ALA I 1778
REMARK 465 THR I 1779
REMARK 465 GLU I 1780
REMARK 465 GLU I 1781
REMARK 465 SER I 1782
REMARK 465 THR I 1783
REMARK 465 LEU I 1927
REMARK 465 PHE I 1928
REMARK 465 ARG I 1929
REMARK 465 MSE E 1
REMARK 465 ALA E 2
REMARK 465 ASP E 3
REMARK 465 GLN E 4
REMARK 465 LYS E 149
REMARK 465 GLU J 1773
REMARK 465 ASN J 1774
REMARK 465 PHE J 1775
REMARK 465 LEU J 1927
REMARK 465 PHE J 1928
REMARK 465 ARG J 1929
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 O GLN E 136 MG MG E 202 1.39
REMARK 500 OG SER H 1925 H PHE H 1926 1.46
REMARK 500 O GLU I 1823 H ARG I 1826 1.48
REMARK 500 OD2 ASP H 1846 HH12 ARG H 1898 1.50
REMARK 500 O ILE I 1827 HD22 ASN I 1831 1.51
REMARK 500 HE ARG A 87 OE1 GLU A 140 1.56
REMARK 500 O ILE D 101 H VAL D 137 1.57
REMARK 500 O ILE B 10 H LYS B 14 1.60
REMARK 500 OG1 THR A 63 O HOH A 301 1.68
REMARK 500 OD1 ASP A 94 OD1 ASN A 98 2.00
REMARK 500 O LEU I 1854 OG1 THR I 1858 2.03
REMARK 500 NH2 ARG A 107 OD1 ASP A 123 2.10
REMARK 500 OD1 ASP B 130 OD1 ASP B 132 2.10
REMARK 500 OD1 ASP E 130 OD1 ASP E 132 2.13
REMARK 500 O LEU J 1916 OG SER J 1920 2.16
REMARK 500 O GLN A 136 O HOH A 302 2.17
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 PRO G1830 C - N - CD ANGL. DEV. = -12.9 DEGREES
REMARK 500 PRO G1891 C - N - CA ANGL. DEV. = 9.4 DEGREES
REMARK 500 ASP C 21 OD1 - CG - OD2 ANGL. DEV. = 20.1 DEGREES
REMARK 500 ASP C 21 CB - CG - OD1 ANGL. DEV. = -8.7 DEGREES
REMARK 500 ASP C 21 CB - CG - OD2 ANGL. DEV. = -11.5 DEGREES
REMARK 500 PRO H1824 C - N - CD ANGL. DEV. = -15.4 DEGREES
REMARK 500 PRO H1830 C - N - CD ANGL. DEV. = -22.7 DEGREES
REMARK 500 PRO I1830 C - N - CD ANGL. DEV. = -21.4 DEGREES
REMARK 500 PRO J1830 C - N - CD ANGL. DEV. = -15.4 DEGREES
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 GLU A 7 -142.40 -135.77
REMARK 500 SER A 82 -161.90 -71.63
REMARK 500 ASP A 94 78.87 -105.70
REMARK 500 GLU A 115 92.14 -64.20
REMARK 500 GLN A 136 117.15 -164.56
REMARK 500 MSE A 146 70.24 -102.54
REMARK 500 THR A 147 37.60 -169.77
REMARK 500 PRO F1785 84.44 -42.86
REMARK 500 SER F1787 92.74 -57.34
REMARK 500 ASP F1802 74.62 -110.15
REMARK 500 SER F1812 55.01 -64.02
REMARK 500 VAL F1813 -17.47 173.59
REMARK 500 ALA F1820 13.08 -66.13
REMARK 500 LYS F1829 -178.66 -63.29
REMARK 500 PRO F1830 92.50 36.22
REMARK 500 ASN F1831 -31.49 -135.08
REMARK 500 LEU F1854 -74.86 -55.38
REMARK 500 SER F1865 144.37 -179.43
REMARK 500 ALA F1882 46.69 -84.53
REMARK 500 SER F1888 101.94 -55.81
REMARK 500 ILE F1892 -81.02 -84.85
REMARK 500 SER F1925 67.84 -100.16
REMARK 500 THR B 6 -131.86 -143.37
REMARK 500 GLU B 7 -152.93 -135.48
REMARK 500 LYS B 22 -78.50 -40.43
REMARK 500 GLU B 32 41.18 -103.42
REMARK 500 VAL B 56 -71.33 -66.02
REMARK 500 ALA B 58 35.44 -91.16
REMARK 500 ASP B 79 -158.39 -96.18
REMARK 500 HIS B 108 -73.58 -63.03
REMARK 500 GLU B 115 80.13 -45.77
REMARK 500 MSE B 145 -7.40 -58.03
REMARK 500 THR B 147 20.07 -145.00
REMARK 500 GLU G1784 -134.82 66.07
REMARK 500 SER G1812 11.66 -67.38
REMARK 500 VAL G1813 -1.38 -145.18
REMARK 500 LYS G1829 -164.61 -59.06
REMARK 500 PRO G1830 83.16 29.15
REMARK 500 GLN G1832 -68.74 -28.12
REMARK 500 SER G1844 128.02 -38.87
REMARK 500 SER G1885 44.02 -86.24
REMARK 500 ARG G1897 -9.40 -56.46
REMARK 500 ARG G1910 -73.82 -42.78
REMARK 500 GLU C 8 -42.30 64.74
REMARK 500 ASP C 25 26.87 -144.75
REMARK 500 GLU C 46 -19.51 -45.18
REMARK 500 ASP C 57 69.56 -115.30
REMARK 500 ASP C 96 29.67 -150.65
REMARK 500 ASP C 132 -74.93 -114.14
REMARK 500 MSE C 146 54.40 -94.69
REMARK 500
REMARK 500 THIS ENTRY HAS 114 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 LYS F 1829 PRO F 1830 -135.72
REMARK 500 LYS G 1829 PRO G 1830 -136.09
REMARK 500 GLU H 1823 PRO H 1824 -135.44
REMARK 500 LYS H 1829 PRO H 1830 -129.30
REMARK 500 GLU I 1823 PRO I 1824 -147.24
REMARK 500 LYS I 1829 PRO I 1830 -128.82
REMARK 500 LYS J 1829 PRO J 1830 -130.67
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH D1113 DISTANCE = 8.89 ANGSTROMS
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 A 201 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 21 OD1
REMARK 620 2 ASP A 23 OD1 93.5
REMARK 620 3 ASP A 25 OD1 86.0 88.0
REMARK 620 4 THR A 27 O 87.3 177.8 94.1
REMARK 620 5 HOH A 308 O 93.8 91.5 179.4 86.3
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 202 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 57 OD1
REMARK 620 2 THR A 63 O 85.4
REMARK 620 3 THR A 63 OG1 87.1 86.4
REMARK 620 4 GLU A 68 OE1 177.7 96.1 94.7
REMARK 620 5 HOH A 301 O 91.3 135.1 48.7 88.9
REMARK 620 6 HOH A 304 O 95.1 136.8 136.8 82.6 88.1
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 203 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 94 OD1
REMARK 620 2 ASP A 96 OD1 87.8
REMARK 620 3 ASN A 98 OD1 57.7 81.1
REMARK 620 4 TYR A 100 O 95.5 171.9 106.9
REMARK 620 5 HOH A 306 O 167.9 95.3 134.3 79.9
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 204 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 130 OD1
REMARK 620 2 ASP A 132 OD1 69.4
REMARK 620 3 ASP A 134 OD1 92.7 72.9
REMARK 620 4 GLN A 136 O 129.5 161.1 102.7
REMARK 620 5 HOH A 302 O 164.7 95.3 81.6 65.8
REMARK 620 6 HOH A 305 O 95.0 102.8 169.2 78.1 89.1
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B 201 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 21 OD1
REMARK 620 2 ASP B 23 OD1 94.5
REMARK 620 3 ASP B 25 OD1 89.7 83.7
REMARK 620 4 ASP B 25 OD2 137.1 81.6 47.4
REMARK 620 5 THR B 27 O 85.7 176.5 99.8 100.7
REMARK 620 6 HOH B 303 O 90.8 95.0 178.7 132.0 81.5
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B 202 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 94 OD1
REMARK 620 2 ASP B 96 OD1 92.7
REMARK 620 3 ASN B 98 OD1 87.9 91.1
REMARK 620 4 TYR B 100 O 84.8 177.5 88.3
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B 203 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 130 OD1
REMARK 620 2 ASP B 132 OD1 60.8
REMARK 620 3 ASP B 134 OD1 90.9 82.6
REMARK 620 4 GLN B 136 O 134.1 165.0 97.2
REMARK 620 5 HOH B 302 O 94.9 96.8 172.9 81.5
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG C 201 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP C 21 OD1
REMARK 620 2 ASP C 23 OD1 91.2
REMARK 620 3 ASP C 25 OD1 86.5 81.4
REMARK 620 4 THR C 27 O 90.3 178.3 99.4
REMARK 620 5 HOH C 304 O 177.7 89.2 91.3 89.2
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG C 202 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR C 63 O
REMARK 620 2 THR C 63 OG1 70.4
REMARK 620 3 HOH C 301 O 136.8 66.4
REMARK 620 4 HOH C 302 O 79.4 74.3 89.8
REMARK 620 5 HOH C 303 O 103.7 114.2 93.0 171.5
REMARK 620 6 HOH C 305 O 154.4 135.2 68.8 105.6 68.2
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG C 206 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP C 65 OD1
REMARK 620 2 ASP D 65 OD2 87.2
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG C 203 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP C 94 OD1
REMARK 620 2 ASP C 96 OD1 92.7
REMARK 620 3 ASN C 98 OD1 84.5 83.8
REMARK 620 4 TYR C 100 O 87.7 179.4 95.8
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG C 204 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP C 130 OD1
REMARK 620 2 ASP C 132 OD1 87.0
REMARK 620 3 ASP C 134 OD1 89.5 87.8
REMARK 620 4 GLN C 136 O 93.0 179.7 92.5
REMARK 620 5 HOH C 306 O 90.7 91.6 179.3 88.1
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG D 201 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP D 21 OD1
REMARK 620 2 ASP D 23 OD1 97.1
REMARK 620 3 ASP D 25 OD1 88.2 83.3
REMARK 620 4 THR D 27 O 82.2 177.7 98.9
REMARK 620 5 HOH D1103 O 91.4 95.3 178.5 82.5
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG D 202 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR D 63 O
REMARK 620 2 THR D 63 OG1 91.5
REMARK 620 3 HOH D1101 O 73.6 165.1
REMARK 620 4 HOH D1104 O 175.7 84.2 110.7
REMARK 620 5 HOH D1105 O 88.9 92.2 88.0 91.5
REMARK 620 6 HOH D1106 O 92.2 83.8 96.2 87.2 175.8
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG D 203 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP D 94 OD1
REMARK 620 2 ASP D 96 OD1 90.7
REMARK 620 3 ASN D 98 OD1 88.2 84.6
REMARK 620 4 TYR D 100 O 88.9 179.5 95.7
REMARK 620 5 HOH D1108 O 179.4 89.7 91.4 90.7
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG D 204 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP D 130 OD1
REMARK 620 2 ASP D 132 OD1 89.1
REMARK 620 3 ASP D 134 OD1 91.9 67.3
REMARK 620 4 GLN D 136 O 90.3 179.0 111.9
REMARK 620 5 HOH D1102 O 179.6 91.2 88.0 89.4
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG E 201 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP E 94 OD1
REMARK 620 2 ASP E 96 OD1 88.6
REMARK 620 3 ASN E 98 OD1 89.9 87.8
REMARK 620 4 TYR E 100 O 91.6 179.4 92.7
REMARK 620 5 HOH E 304 O 90.4 92.0 179.7 87.4
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG E 202 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP E 130 OD1
REMARK 620 2 ASP E 132 OD1 62.6
REMARK 620 3 ASP E 134 OD1 93.3 74.4
REMARK 620 4 HOH E 301 O 92.2 103.5 172.3
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 203
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 204
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 205
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 F 2101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG B 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG B 202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG B 203
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 B 204
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 G 2101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG C 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG C 202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG C 203
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG C 204
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 C 205
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG C 206
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 H 2101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG D 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG D 202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG D 203
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG D 204
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG E 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG E 202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 J 2101
DBREF 4OVN A 1 149 UNP P62158 CALM_HUMAN 1 149
DBREF 4OVN F 1773 1929 UNP Q14524 SCN5A_HUMAN 1773 1929
DBREF 4OVN B 1 149 UNP P62158 CALM_HUMAN 1 149
DBREF 4OVN G 1773 1929 UNP Q14524 SCN5A_HUMAN 1773 1929
DBREF 4OVN C 1 149 UNP P62158 CALM_HUMAN 1 149
DBREF 4OVN H 1773 1929 UNP Q14524 SCN5A_HUMAN 1773 1929
DBREF 4OVN D 1 149 UNP P62158 CALM_HUMAN 1 149
DBREF 4OVN I 1773 1929 UNP Q14524 SCN5A_HUMAN 1773 1929
DBREF 4OVN E 1 149 UNP P62158 CALM_HUMAN 1 149
DBREF 4OVN J 1773 1929 UNP Q14524 SCN5A_HUMAN 1773 1929
SEQRES 1 A 149 MSE ALA ASP GLN LEU THR GLU GLU GLN ILE ALA GLU PHE
SEQRES 2 A 149 LYS GLU ALA PHE SER LEU PHE ASP LYS ASP GLY ASP GLY
SEQRES 3 A 149 THR ILE THR THR LYS GLU LEU GLY THR VAL MSE ARG SER
SEQRES 4 A 149 LEU GLY GLN ASN PRO THR GLU ALA GLU LEU GLN ASP MSE
SEQRES 5 A 149 ILE ASN GLU VAL ASP ALA ASP GLY ASN GLY THR ILE ASP
SEQRES 6 A 149 PHE PRO GLU PHE LEU THR MSE MSE ALA ARG LYS MSE LYS
SEQRES 7 A 149 ASP THR ASP SER GLU GLU GLU ILE ARG GLU ALA PHE ARG
SEQRES 8 A 149 VAL PHE ASP LYS ASP GLY ASN GLY TYR ILE SER ALA ALA
SEQRES 9 A 149 GLU LEU ARG HIS VAL MSE THR ASN LEU GLY GLU LYS LEU
SEQRES 10 A 149 THR ASP GLU GLU VAL ASP GLU MSE ILE ARG GLU ALA ASP
SEQRES 11 A 149 ILE ASP GLY ASP GLY GLN VAL ASN TYR GLU GLU PHE VAL
SEQRES 12 A 149 GLN MSE MSE THR ALA LYS
SEQRES 1 F 157 GLU ASN PHE SER VAL ALA THR GLU GLU SER THR GLU PRO
SEQRES 2 F 157 LEU SER GLU ASP ASP PHE ASP MSE PHE TYR GLU ILE TRP
SEQRES 3 F 157 GLU LYS PHE ASP PRO GLU ALA THR GLN PHE ILE GLU TYR
SEQRES 4 F 157 SER VAL LEU SER ASP PHE ALA ASP ALA LEU SER GLU PRO
SEQRES 5 F 157 LEU ARG ILE ALA LYS PRO ASN GLN ILE SER LEU ILE ASN
SEQRES 6 F 157 MSE ASP LEU PRO MSE VAL SER GLY ASP ARG ILE HIS CYS
SEQRES 7 F 157 MSE ASP ILE LEU PHE ALA PHE THR LYS ARG VAL LEU GLY
SEQRES 8 F 157 GLU SER GLY GLU MSE ASP ALA LEU LYS ILE GLN MSE GLU
SEQRES 9 F 157 GLU LYS PHE MSE ALA ALA ASN PRO SER LYS ILE SER TYR
SEQRES 10 F 157 GLU PRO ILE THR THR THR LEU ARG ARG LYS HIS GLU GLU
SEQRES 11 F 157 VAL SER ALA MSE VAL ILE GLN ARG ALA PHE ARG ARG HIS
SEQRES 12 F 157 LEU LEU GLN ARG SER LEU LYS HIS ALA SER PHE LEU PHE
SEQRES 13 F 157 ARG
SEQRES 1 B 149 MSE ALA ASP GLN LEU THR GLU GLU GLN ILE ALA GLU PHE
SEQRES 2 B 149 LYS GLU ALA PHE SER LEU PHE ASP LYS ASP GLY ASP GLY
SEQRES 3 B 149 THR ILE THR THR LYS GLU LEU GLY THR VAL MSE ARG SER
SEQRES 4 B 149 LEU GLY GLN ASN PRO THR GLU ALA GLU LEU GLN ASP MSE
SEQRES 5 B 149 ILE ASN GLU VAL ASP ALA ASP GLY ASN GLY THR ILE ASP
SEQRES 6 B 149 PHE PRO GLU PHE LEU THR MSE MSE ALA ARG LYS MSE LYS
SEQRES 7 B 149 ASP THR ASP SER GLU GLU GLU ILE ARG GLU ALA PHE ARG
SEQRES 8 B 149 VAL PHE ASP LYS ASP GLY ASN GLY TYR ILE SER ALA ALA
SEQRES 9 B 149 GLU LEU ARG HIS VAL MSE THR ASN LEU GLY GLU LYS LEU
SEQRES 10 B 149 THR ASP GLU GLU VAL ASP GLU MSE ILE ARG GLU ALA ASP
SEQRES 11 B 149 ILE ASP GLY ASP GLY GLN VAL ASN TYR GLU GLU PHE VAL
SEQRES 12 B 149 GLN MSE MSE THR ALA LYS
SEQRES 1 G 157 GLU ASN PHE SER VAL ALA THR GLU GLU SER THR GLU PRO
SEQRES 2 G 157 LEU SER GLU ASP ASP PHE ASP MSE PHE TYR GLU ILE TRP
SEQRES 3 G 157 GLU LYS PHE ASP PRO GLU ALA THR GLN PHE ILE GLU TYR
SEQRES 4 G 157 SER VAL LEU SER ASP PHE ALA ASP ALA LEU SER GLU PRO
SEQRES 5 G 157 LEU ARG ILE ALA LYS PRO ASN GLN ILE SER LEU ILE ASN
SEQRES 6 G 157 MSE ASP LEU PRO MSE VAL SER GLY ASP ARG ILE HIS CYS
SEQRES 7 G 157 MSE ASP ILE LEU PHE ALA PHE THR LYS ARG VAL LEU GLY
SEQRES 8 G 157 GLU SER GLY GLU MSE ASP ALA LEU LYS ILE GLN MSE GLU
SEQRES 9 G 157 GLU LYS PHE MSE ALA ALA ASN PRO SER LYS ILE SER TYR
SEQRES 10 G 157 GLU PRO ILE THR THR THR LEU ARG ARG LYS HIS GLU GLU
SEQRES 11 G 157 VAL SER ALA MSE VAL ILE GLN ARG ALA PHE ARG ARG HIS
SEQRES 12 G 157 LEU LEU GLN ARG SER LEU LYS HIS ALA SER PHE LEU PHE
SEQRES 13 G 157 ARG
SEQRES 1 C 149 MSE ALA ASP GLN LEU THR GLU GLU GLN ILE ALA GLU PHE
SEQRES 2 C 149 LYS GLU ALA PHE SER LEU PHE ASP LYS ASP GLY ASP GLY
SEQRES 3 C 149 THR ILE THR THR LYS GLU LEU GLY THR VAL MSE ARG SER
SEQRES 4 C 149 LEU GLY GLN ASN PRO THR GLU ALA GLU LEU GLN ASP MSE
SEQRES 5 C 149 ILE ASN GLU VAL ASP ALA ASP GLY ASN GLY THR ILE ASP
SEQRES 6 C 149 PHE PRO GLU PHE LEU THR MSE MSE ALA ARG LYS MSE LYS
SEQRES 7 C 149 ASP THR ASP SER GLU GLU GLU ILE ARG GLU ALA PHE ARG
SEQRES 8 C 149 VAL PHE ASP LYS ASP GLY ASN GLY TYR ILE SER ALA ALA
SEQRES 9 C 149 GLU LEU ARG HIS VAL MSE THR ASN LEU GLY GLU LYS LEU
SEQRES 10 C 149 THR ASP GLU GLU VAL ASP GLU MSE ILE ARG GLU ALA ASP
SEQRES 11 C 149 ILE ASP GLY ASP GLY GLN VAL ASN TYR GLU GLU PHE VAL
SEQRES 12 C 149 GLN MSE MSE THR ALA LYS
SEQRES 1 H 157 GLU ASN PHE SER VAL ALA THR GLU GLU SER THR GLU PRO
SEQRES 2 H 157 LEU SER GLU ASP ASP PHE ASP MSE PHE TYR GLU ILE TRP
SEQRES 3 H 157 GLU LYS PHE ASP PRO GLU ALA THR GLN PHE ILE GLU TYR
SEQRES 4 H 157 SER VAL LEU SER ASP PHE ALA ASP ALA LEU SER GLU PRO
SEQRES 5 H 157 LEU ARG ILE ALA LYS PRO ASN GLN ILE SER LEU ILE ASN
SEQRES 6 H 157 MSE ASP LEU PRO MSE VAL SER GLY ASP ARG ILE HIS CYS
SEQRES 7 H 157 MSE ASP ILE LEU PHE ALA PHE THR LYS ARG VAL LEU GLY
SEQRES 8 H 157 GLU SER GLY GLU MSE ASP ALA LEU LYS ILE GLN MSE GLU
SEQRES 9 H 157 GLU LYS PHE MSE ALA ALA ASN PRO SER LYS ILE SER TYR
SEQRES 10 H 157 GLU PRO ILE THR THR THR LEU ARG ARG LYS HIS GLU GLU
SEQRES 11 H 157 VAL SER ALA MSE VAL ILE GLN ARG ALA PHE ARG ARG HIS
SEQRES 12 H 157 LEU LEU GLN ARG SER LEU LYS HIS ALA SER PHE LEU PHE
SEQRES 13 H 157 ARG
SEQRES 1 D 149 MSE ALA ASP GLN LEU THR GLU GLU GLN ILE ALA GLU PHE
SEQRES 2 D 149 LYS GLU ALA PHE SER LEU PHE ASP LYS ASP GLY ASP GLY
SEQRES 3 D 149 THR ILE THR THR LYS GLU LEU GLY THR VAL MSE ARG SER
SEQRES 4 D 149 LEU GLY GLN ASN PRO THR GLU ALA GLU LEU GLN ASP MSE
SEQRES 5 D 149 ILE ASN GLU VAL ASP ALA ASP GLY ASN GLY THR ILE ASP
SEQRES 6 D 149 PHE PRO GLU PHE LEU THR MSE MSE ALA ARG LYS MSE LYS
SEQRES 7 D 149 ASP THR ASP SER GLU GLU GLU ILE ARG GLU ALA PHE ARG
SEQRES 8 D 149 VAL PHE ASP LYS ASP GLY ASN GLY TYR ILE SER ALA ALA
SEQRES 9 D 149 GLU LEU ARG HIS VAL MSE THR ASN LEU GLY GLU LYS LEU
SEQRES 10 D 149 THR ASP GLU GLU VAL ASP GLU MSE ILE ARG GLU ALA ASP
SEQRES 11 D 149 ILE ASP GLY ASP GLY GLN VAL ASN TYR GLU GLU PHE VAL
SEQRES 12 D 149 GLN MSE MSE THR ALA LYS
SEQRES 1 I 157 GLU ASN PHE SER VAL ALA THR GLU GLU SER THR GLU PRO
SEQRES 2 I 157 LEU SER GLU ASP ASP PHE ASP MSE PHE TYR GLU ILE TRP
SEQRES 3 I 157 GLU LYS PHE ASP PRO GLU ALA THR GLN PHE ILE GLU TYR
SEQRES 4 I 157 SER VAL LEU SER ASP PHE ALA ASP ALA LEU SER GLU PRO
SEQRES 5 I 157 LEU ARG ILE ALA LYS PRO ASN GLN ILE SER LEU ILE ASN
SEQRES 6 I 157 MSE ASP LEU PRO MSE VAL SER GLY ASP ARG ILE HIS CYS
SEQRES 7 I 157 MSE ASP ILE LEU PHE ALA PHE THR LYS ARG VAL LEU GLY
SEQRES 8 I 157 GLU SER GLY GLU MSE ASP ALA LEU LYS ILE GLN MSE GLU
SEQRES 9 I 157 GLU LYS PHE MSE ALA ALA ASN PRO SER LYS ILE SER TYR
SEQRES 10 I 157 GLU PRO ILE THR THR THR LEU ARG ARG LYS HIS GLU GLU
SEQRES 11 I 157 VAL SER ALA MSE VAL ILE GLN ARG ALA PHE ARG ARG HIS
SEQRES 12 I 157 LEU LEU GLN ARG SER LEU LYS HIS ALA SER PHE LEU PHE
SEQRES 13 I 157 ARG
SEQRES 1 E 149 MSE ALA ASP GLN LEU THR GLU GLU GLN ILE ALA GLU PHE
SEQRES 2 E 149 LYS GLU ALA PHE SER LEU PHE ASP LYS ASP GLY ASP GLY
SEQRES 3 E 149 THR ILE THR THR LYS GLU LEU GLY THR VAL MSE ARG SER
SEQRES 4 E 149 LEU GLY GLN ASN PRO THR GLU ALA GLU LEU GLN ASP MSE
SEQRES 5 E 149 ILE ASN GLU VAL ASP ALA ASP GLY ASN GLY THR ILE ASP
SEQRES 6 E 149 PHE PRO GLU PHE LEU THR MSE MSE ALA ARG LYS MSE LYS
SEQRES 7 E 149 ASP THR ASP SER GLU GLU GLU ILE ARG GLU ALA PHE ARG
SEQRES 8 E 149 VAL PHE ASP LYS ASP GLY ASN GLY TYR ILE SER ALA ALA
SEQRES 9 E 149 GLU LEU ARG HIS VAL MSE THR ASN LEU GLY GLU LYS LEU
SEQRES 10 E 149 THR ASP GLU GLU VAL ASP GLU MSE ILE ARG GLU ALA ASP
SEQRES 11 E 149 ILE ASP GLY ASP GLY GLN VAL ASN TYR GLU GLU PHE VAL
SEQRES 12 E 149 GLN MSE MSE THR ALA LYS
SEQRES 1 J 157 GLU ASN PHE SER VAL ALA THR GLU GLU SER THR GLU PRO
SEQRES 2 J 157 LEU SER GLU ASP ASP PHE ASP MSE PHE TYR GLU ILE TRP
SEQRES 3 J 157 GLU LYS PHE ASP PRO GLU ALA THR GLN PHE ILE GLU TYR
SEQRES 4 J 157 SER VAL LEU SER ASP PHE ALA ASP ALA LEU SER GLU PRO
SEQRES 5 J 157 LEU ARG ILE ALA LYS PRO ASN GLN ILE SER LEU ILE ASN
SEQRES 6 J 157 MSE ASP LEU PRO MSE VAL SER GLY ASP ARG ILE HIS CYS
SEQRES 7 J 157 MSE ASP ILE LEU PHE ALA PHE THR LYS ARG VAL LEU GLY
SEQRES 8 J 157 GLU SER GLY GLU MSE ASP ALA LEU LYS ILE GLN MSE GLU
SEQRES 9 J 157 GLU LYS PHE MSE ALA ALA ASN PRO SER LYS ILE SER TYR
SEQRES 10 J 157 GLU PRO ILE THR THR THR LEU ARG ARG LYS HIS GLU GLU
SEQRES 11 J 157 VAL SER ALA MSE VAL ILE GLN ARG ALA PHE ARG ARG HIS
SEQRES 12 J 157 LEU LEU GLN ARG SER LEU LYS HIS ALA SER PHE LEU PHE
SEQRES 13 J 157 ARG
MODRES 4OVN MSE A 37 MET MODIFIED RESIDUE
MODRES 4OVN MSE A 52 MET MODIFIED RESIDUE
MODRES 4OVN MSE A 72 MET MODIFIED RESIDUE
MODRES 4OVN MSE A 73 MET MODIFIED RESIDUE
MODRES 4OVN MSE A 77 MET MODIFIED RESIDUE
MODRES 4OVN MSE A 110 MET MODIFIED RESIDUE
MODRES 4OVN MSE A 125 MET MODIFIED RESIDUE
MODRES 4OVN MSE A 145 MET MODIFIED RESIDUE
MODRES 4OVN MSE A 146 MET MODIFIED RESIDUE
MODRES 4OVN MSE F 1793 MET MODIFIED RESIDUE
MODRES 4OVN MSE F 1838 MET MODIFIED RESIDUE
MODRES 4OVN MSE F 1842 MET MODIFIED RESIDUE
MODRES 4OVN MSE F 1851 MET MODIFIED RESIDUE
MODRES 4OVN MSE F 1868 MET MODIFIED RESIDUE
MODRES 4OVN MSE F 1875 MET MODIFIED RESIDUE
MODRES 4OVN MSE F 1880 MET MODIFIED RESIDUE
MODRES 4OVN MSE F 1906 MET MODIFIED RESIDUE
MODRES 4OVN MSE B 37 MET MODIFIED RESIDUE
MODRES 4OVN MSE B 52 MET MODIFIED RESIDUE
MODRES 4OVN MSE B 72 MET MODIFIED RESIDUE
MODRES 4OVN MSE B 73 MET MODIFIED RESIDUE
MODRES 4OVN MSE B 77 MET MODIFIED RESIDUE
MODRES 4OVN MSE B 110 MET MODIFIED RESIDUE
MODRES 4OVN MSE B 125 MET MODIFIED RESIDUE
MODRES 4OVN MSE B 145 MET MODIFIED RESIDUE
MODRES 4OVN MSE B 146 MET MODIFIED RESIDUE
MODRES 4OVN MSE G 1793 MET MODIFIED RESIDUE
MODRES 4OVN MSE G 1838 MET MODIFIED RESIDUE
MODRES 4OVN MSE G 1842 MET MODIFIED RESIDUE
MODRES 4OVN MSE G 1851 MET MODIFIED RESIDUE
MODRES 4OVN MSE G 1868 MET MODIFIED RESIDUE
MODRES 4OVN MSE G 1875 MET MODIFIED RESIDUE
MODRES 4OVN MSE G 1880 MET MODIFIED RESIDUE
MODRES 4OVN MSE G 1906 MET MODIFIED RESIDUE
MODRES 4OVN MSE C 37 MET MODIFIED RESIDUE
MODRES 4OVN MSE C 52 MET MODIFIED RESIDUE
MODRES 4OVN MSE C 72 MET MODIFIED RESIDUE
MODRES 4OVN MSE C 73 MET MODIFIED RESIDUE
MODRES 4OVN MSE C 77 MET MODIFIED RESIDUE
MODRES 4OVN MSE C 110 MET MODIFIED RESIDUE
MODRES 4OVN MSE C 125 MET MODIFIED RESIDUE
MODRES 4OVN MSE C 145 MET MODIFIED RESIDUE
MODRES 4OVN MSE C 146 MET MODIFIED RESIDUE
MODRES 4OVN MSE H 1793 MET MODIFIED RESIDUE
MODRES 4OVN MSE H 1838 MET MODIFIED RESIDUE
MODRES 4OVN MSE H 1842 MET MODIFIED RESIDUE
MODRES 4OVN MSE H 1851 MET MODIFIED RESIDUE
MODRES 4OVN MSE H 1868 MET MODIFIED RESIDUE
MODRES 4OVN MSE H 1875 MET MODIFIED RESIDUE
MODRES 4OVN MSE H 1880 MET MODIFIED RESIDUE
MODRES 4OVN MSE H 1906 MET MODIFIED RESIDUE
MODRES 4OVN MSE D 37 MET MODIFIED RESIDUE
MODRES 4OVN MSE D 52 MET MODIFIED RESIDUE
MODRES 4OVN MSE D 72 MET MODIFIED RESIDUE
MODRES 4OVN MSE D 73 MET MODIFIED RESIDUE
MODRES 4OVN MSE D 77 MET MODIFIED RESIDUE
MODRES 4OVN MSE D 110 MET MODIFIED RESIDUE
MODRES 4OVN MSE D 125 MET MODIFIED RESIDUE
MODRES 4OVN MSE D 145 MET MODIFIED RESIDUE
MODRES 4OVN MSE D 146 MET MODIFIED RESIDUE
MODRES 4OVN MSE I 1793 MET MODIFIED RESIDUE
MODRES 4OVN MSE I 1838 MET MODIFIED RESIDUE
MODRES 4OVN MSE I 1842 MET MODIFIED RESIDUE
MODRES 4OVN MSE I 1851 MET MODIFIED RESIDUE
MODRES 4OVN MSE I 1868 MET MODIFIED RESIDUE
MODRES 4OVN MSE I 1875 MET MODIFIED RESIDUE
MODRES 4OVN MSE I 1880 MET MODIFIED RESIDUE
MODRES 4OVN MSE I 1906 MET MODIFIED RESIDUE
MODRES 4OVN MSE E 37 MET MODIFIED RESIDUE
MODRES 4OVN MSE E 52 MET MODIFIED RESIDUE
MODRES 4OVN MSE E 72 MET MODIFIED RESIDUE
MODRES 4OVN MSE E 73 MET MODIFIED RESIDUE
MODRES 4OVN MSE E 77 MET MODIFIED RESIDUE
MODRES 4OVN MSE E 110 MET MODIFIED RESIDUE
MODRES 4OVN MSE E 125 MET MODIFIED RESIDUE
MODRES 4OVN MSE E 145 MET MODIFIED RESIDUE
MODRES 4OVN MSE E 146 MET MODIFIED RESIDUE
MODRES 4OVN MSE J 1793 MET MODIFIED RESIDUE
MODRES 4OVN MSE J 1838 MET MODIFIED RESIDUE
MODRES 4OVN MSE J 1842 MET MODIFIED RESIDUE
MODRES 4OVN MSE J 1851 MET MODIFIED RESIDUE
MODRES 4OVN MSE J 1868 MET MODIFIED RESIDUE
MODRES 4OVN MSE J 1875 MET MODIFIED RESIDUE
MODRES 4OVN MSE J 1880 MET MODIFIED RESIDUE
MODRES 4OVN MSE J 1906 MET MODIFIED RESIDUE
HET MSE A 37 17
HET MSE A 52 17
HET MSE A 72 17
HET MSE A 73 17
HET MSE A 77 17
HET MSE A 110 17
HET MSE A 125 17
HET MSE A 145 17
HET MSE A 146 17
HET MSE F1793 17
HET MSE F1838 17
HET MSE F1842 17
HET MSE F1851 17
HET MSE F1868 17
HET MSE F1875 17
HET MSE F1880 17
HET MSE F1906 17
HET MSE B 37 17
HET MSE B 52 17
HET MSE B 72 17
HET MSE B 73 17
HET MSE B 77 17
HET MSE B 110 17
HET MSE B 125 17
HET MSE B 145 17
HET MSE B 146 17
HET MSE G1793 17
HET MSE G1838 17
HET MSE G1842 17
HET MSE G1851 17
HET MSE G1868 17
HET MSE G1875 17
HET MSE G1880 17
HET MSE G1906 17
HET MSE C 37 17
HET MSE C 52 17
HET MSE C 72 17
HET MSE C 73 17
HET MSE C 77 17
HET MSE C 110 17
HET MSE C 125 17
HET MSE C 145 17
HET MSE C 146 17
HET MSE H1793 17
HET MSE H1838 17
HET MSE H1842 17
HET MSE H1851 17
HET MSE H1868 17
HET MSE H1875 17
HET MSE H1880 17
HET MSE H1906 17
HET MSE D 37 17
HET MSE D 52 17
HET MSE D 72 17
HET MSE D 73 17
HET MSE D 77 17
HET MSE D 110 17
HET MSE D 125 17
HET MSE D 145 17
HET MSE D 146 17
HET MSE I1793 17
HET MSE I1838 17
HET MSE I1842 17
HET MSE I1851 17
HET MSE I1868 17
HET MSE I1875 17
HET MSE I1880 17
HET MSE I1906 17
HET MSE E 37 17
HET MSE E 52 17
HET MSE E 72 17
HET MSE E 73 17
HET MSE E 77 17
HET MSE E 110 17
HET MSE E 125 17
HET MSE E 145 17
HET MSE E 146 17
HET MSE J1793 17
HET MSE J1838 17
HET MSE J1842 17
HET MSE J1851 17
HET MSE J1868 17
HET MSE J1875 17
HET MSE J1880 17
HET MSE J1906 17
HET MG A 201 1
HET MG A 202 1
HET MG A 203 1
HET MG A 204 1
HET SO4 A 205 5
HET SO4 F2101 5
HET MG B 201 1
HET MG B 202 1
HET MG B 203 1
HET PO4 B 204 5
HET SO4 G2101 5
HET MG C 201 1
HET MG C 202 1
HET MG C 203 1
HET MG C 204 1
HET PO4 C 205 5
HET MG C 206 1
HET SO4 H2101 5
HET MG D 201 1
HET MG D 202 1
HET MG D 203 1
HET MG D 204 1
HET MG E 201 1
HET MG E 202 1
HET SO4 J2101 5
HETNAM MSE SELENOMETHIONINE
HETNAM MG MAGNESIUM ION
HETNAM SO4 SULFATE ION
HETNAM PO4 PHOSPHATE ION
FORMUL 1 MSE 85(C5 H11 N O2 SE)
FORMUL 11 MG 18(MG 2+)
FORMUL 15 SO4 5(O4 S 2-)
FORMUL 20 PO4 2(O4 P 3-)
FORMUL 36 HOH *62(H2 O)
HELIX 1 AA1 GLU A 8 ASP A 21 1 14
HELIX 2 AA2 THR A 30 SER A 39 1 10
HELIX 3 AA3 THR A 45 ASP A 57 1 13
HELIX 4 AA4 PHE A 66 ASP A 79 1 14
HELIX 5 AA5 GLU A 83 VAL A 92 1 10
HELIX 6 AA6 SER A 102 LEU A 113 1 12
HELIX 7 AA7 THR A 118 ASP A 130 1 13
HELIX 8 AA8 TYR A 139 GLN A 144 1 6
HELIX 9 AA9 ASP F 1790 ASP F 1802 1 13
HELIX 10 AB1 VAL F 1813 ALA F 1820 1 8
HELIX 11 AB2 ASN F 1831 MSE F 1838 1 8
HELIX 12 AB3 CYS F 1850 GLY F 1863 1 14
HELIX 13 AB4 GLU F 1867 ALA F 1882 1 16
HELIX 14 AB5 LEU F 1896 SER F 1925 1 30
HELIX 15 AB6 GLN B 9 ASP B 21 1 13
HELIX 16 AB7 LEU B 33 LEU B 40 1 8
HELIX 17 AB8 THR B 45 ASP B 51 1 7
HELIX 18 AB9 PHE B 66 LEU B 70 1 5
HELIX 19 AC1 MSE B 72 MSE B 77 1 6
HELIX 20 AC2 SER B 82 ASP B 94 1 13
HELIX 21 AC3 ALA B 103 LEU B 113 1 11
HELIX 22 AC4 THR B 118 ASP B 130 1 13
HELIX 23 AC5 ASN B 138 MSE B 145 1 8
HELIX 24 AC6 SER G 1787 ASP G 1802 1 16
HELIX 25 AC7 VAL G 1813 LEU G 1821 1 9
HELIX 26 AC8 ASN G 1831 ASN G 1837 1 7
HELIX 27 AC9 CYS G 1850 GLY G 1863 1 14
HELIX 28 AD1 GLU G 1867 ASN G 1883 1 17
HELIX 29 AD2 THR G 1895 PHE G 1926 1 32
HELIX 30 AD3 GLU C 8 ASP C 21 1 14
HELIX 31 AD4 GLU C 32 SER C 39 1 8
HELIX 32 AD5 ALA C 47 ASP C 57 1 11
HELIX 33 AD6 PHE C 66 ASP C 79 1 14
HELIX 34 AD7 SER C 82 VAL C 92 1 11
HELIX 35 AD8 ALA C 103 LEU C 113 1 11
HELIX 36 AD9 THR C 118 ASP C 130 1 13
HELIX 37 AE1 TYR C 139 MSE C 146 1 8
HELIX 38 AE2 SER H 1787 ASP H 1802 1 16
HELIX 39 AE3 VAL H 1813 LEU H 1821 1 9
HELIX 40 AE4 ASN H 1831 ASP H 1839 1 9
HELIX 41 AE5 CYS H 1850 GLY H 1863 1 14
HELIX 42 AE6 GLU H 1867 ASN H 1883 1 17
HELIX 43 AE7 THR H 1895 ALA H 1924 1 30
HELIX 44 AE8 GLU D 8 ASP D 21 1 14
HELIX 45 AE9 LYS D 31 LEU D 40 1 10
HELIX 46 AF1 THR D 45 ASP D 57 1 13
HELIX 47 AF2 PHE D 66 ASP D 79 1 14
HELIX 48 AF3 ASP D 81 VAL D 92 1 12
HELIX 49 AF4 ALA D 103 LEU D 113 1 11
HELIX 50 AF5 THR D 118 ASP D 130 1 13
HELIX 51 AF6 TYR D 139 MSE D 145 1 7
HELIX 52 AF7 SER I 1787 ASP I 1802 1 16
HELIX 53 AF8 VAL I 1813 LEU I 1821 1 9
HELIX 54 AF9 ASN I 1831 ASN I 1837 1 7
HELIX 55 AG1 CYS I 1850 GLY I 1863 1 14
HELIX 56 AG2 SER I 1865 ALA I 1882 1 18
HELIX 57 AG3 THR I 1895 HIS I 1923 1 29
HELIX 58 AG4 GLN E 9 PHE E 20 1 12
HELIX 59 AG5 THR E 30 SER E 39 1 10
HELIX 60 AG6 ALA E 47 ASP E 51 5 5
HELIX 61 AG7 PHE E 66 LYS E 76 1 11
HELIX 62 AG8 GLU E 83 PHE E 93 1 11
HELIX 63 AG9 SER E 102 THR E 111 1 10
HELIX 64 AH1 THR E 118 ASP E 130 1 13
HELIX 65 AH2 TYR E 139 MSE E 146 1 8
HELIX 66 AH3 SER J 1787 ASP J 1802 1 16
HELIX 67 AH4 VAL J 1813 LEU J 1821 1 9
HELIX 68 AH5 ASN J 1831 MSE J 1838 1 8
HELIX 69 AH6 CYS J 1850 GLY J 1863 1 14
HELIX 70 AH7 SER J 1865 ALA J 1882 1 18
HELIX 71 AH8 THR J 1895 ALA J 1924 1 30
SHEET 1 AA1 2 THR A 27 THR A 29 0
SHEET 2 AA1 2 THR A 63 ASP A 65 -1 O ILE A 64 N ILE A 28
SHEET 1 AA2 2 TYR A 100 ILE A 101 0
SHEET 2 AA2 2 VAL A 137 ASN A 138 -1 O VAL A 137 N ILE A 101
SHEET 1 AA3 2 PHE F1808 GLU F1810 0
SHEET 2 AA3 2 ARG F1847 HIS F1849 -1 O ILE F1848 N ILE F1809
SHEET 1 AA4 2 PRO F1841 VAL F1843 0
SHEET 2 AA4 2 PRO F1891 THR F1894 -1 O ILE F1892 N MSE F1842
SHEET 1 AA5 2 THR B 27 THR B 29 0
SHEET 2 AA5 2 THR B 63 ASP B 65 -1 O ILE B 64 N ILE B 28
SHEET 1 AA6 2 ILE B 101 SER B 102 0
SHEET 2 AA6 2 GLN B 136 VAL B 137 -1 O VAL B 137 N ILE B 101
SHEET 1 AA7 4 PHE G1808 GLU G1810 0
SHEET 2 AA7 4 ARG G1847 HIS G1849 -1 O ILE G1848 N ILE G1809
SHEET 3 AA7 4 PRO G1841 VAL G1843 -1 N VAL G1843 O ARG G1847
SHEET 4 AA7 4 PRO G1891 THR G1894 -1 O THR G1893 N MSE G1842
SHEET 1 AA8 2 THR C 27 THR C 29 0
SHEET 2 AA8 2 THR C 63 ASP C 65 -1 O ILE C 64 N ILE C 28
SHEET 1 AA9 2 TYR C 100 SER C 102 0
SHEET 2 AA9 2 GLN C 136 ASN C 138 -1 O VAL C 137 N ILE C 101
SHEET 1 AB1 2 PHE H1808 GLU H1810 0
SHEET 2 AB1 2 ARG H1847 HIS H1849 -1 O ILE H1848 N ILE H1809
SHEET 1 AB2 2 PRO H1841 MSE H1842 0
SHEET 2 AB2 2 THR H1893 THR H1894 -1 O THR H1893 N MSE H1842
SHEET 1 AB3 2 THR D 27 THR D 29 0
SHEET 2 AB3 2 THR D 63 ASP D 65 -1 O ILE D 64 N ILE D 28
SHEET 1 AB4 2 TYR D 100 SER D 102 0
SHEET 2 AB4 2 GLN D 136 ASN D 138 -1 O VAL D 137 N ILE D 101
SHEET 1 AB5 2 PHE I1808 GLU I1810 0
SHEET 2 AB5 2 ARG I1847 HIS I1849 -1 O ILE I1848 N ILE I1809
SHEET 1 AB6 2 PRO I1841 VAL I1843 0
SHEET 2 AB6 2 PRO I1891 THR I1894 -1 O ILE I1892 N MSE I1842
SHEET 1 AB7 2 THR E 27 ILE E 28 0
SHEET 2 AB7 2 ILE E 64 ASP E 65 -1 O ILE E 64 N ILE E 28
SHEET 1 AB8 2 TYR E 100 ILE E 101 0
SHEET 2 AB8 2 VAL E 137 ASN E 138 -1 O VAL E 137 N ILE E 101
SHEET 1 AB9 2 PHE J1808 GLU J1810 0
SHEET 2 AB9 2 ARG J1847 HIS J1849 -1 O ILE J1848 N ILE J1809
SHEET 1 AC1 2 PRO J1841 VAL J1843 0
SHEET 2 AC1 2 PRO J1891 THR J1894 -1 O ILE J1892 N MSE J1842
LINK C VAL A 36 N MSE A 37 1555 1555 1.33
LINK C MSE A 37 N ARG A 38 1555 1555 1.33
LINK C ASP A 51 N MSE A 52 1555 1555 1.33
LINK C MSE A 52 N ILE A 53 1555 1555 1.33
LINK C THR A 71 N MSE A 72 1555 1555 1.33
LINK C MSE A 72 N MSE A 73 1555 1555 1.33
LINK C MSE A 73 N ALA A 74 1555 1555 1.33
LINK C LYS A 76 N MSE A 77 1555 1555 1.34
LINK C MSE A 77 N LYS A 78 1555 1555 1.33
LINK C VAL A 109 N MSE A 110 1555 1555 1.33
LINK C MSE A 110 N THR A 111 1555 1555 1.32
LINK C GLU A 124 N MSE A 125 1555 1555 1.32
LINK C MSE A 125 N ILE A 126 1555 1555 1.33
LINK C GLN A 144 N MSE A 145 1555 1555 1.32
LINK C MSE A 145 N MSE A 146 1555 1555 1.33
LINK C MSE A 146 N THR A 147 1555 1555 1.32
LINK C ASP F1792 N MSE F1793 1555 1555 1.33
LINK C MSE F1793 N PHE F1794 1555 1555 1.33
LINK C ASN F1837 N MSE F1838 1555 1555 1.33
LINK C MSE F1838 N ASP F1839 1555 1555 1.33
LINK C PRO F1841 N MSE F1842 1555 1555 1.32
LINK C MSE F1842 N VAL F1843 1555 1555 1.33
LINK C CYS F1850 N MSE F1851 1555 1555 1.33
LINK C MSE F1851 N ASP F1852 1555 1555 1.33
LINK C GLU F1867 N MSE F1868 1555 1555 1.34
LINK C MSE F1868 N ASP F1869 1555 1555 1.33
LINK C GLN F1874 N MSE F1875 1555 1555 1.33
LINK C MSE F1875 N GLU F1876 1555 1555 1.33
LINK C PHE F1879 N MSE F1880 1555 1555 1.33
LINK C MSE F1880 N ALA F1881 1555 1555 1.33
LINK C ALA F1905 N MSE F1906 1555 1555 1.33
LINK C MSE F1906 N VAL F1907 1555 1555 1.33
LINK C VAL B 36 N MSE B 37 1555 1555 1.33
LINK C MSE B 37 N ARG B 38 1555 1555 1.33
LINK C ASP B 51 N MSE B 52 1555 1555 1.33
LINK C MSE B 52 N ILE B 53 1555 1555 1.33
LINK C THR B 71 N MSE B 72 1555 1555 1.33
LINK C MSE B 72 N MSE B 73 1555 1555 1.34
LINK C MSE B 73 N ALA B 74 1555 1555 1.33
LINK C LYS B 76 N MSE B 77 1555 1555 1.34
LINK C MSE B 77 N LYS B 78 1555 1555 1.33
LINK C VAL B 109 N MSE B 110 1555 1555 1.33
LINK C MSE B 110 N THR B 111 1555 1555 1.34
LINK C GLU B 124 N MSE B 125 1555 1555 1.33
LINK C MSE B 125 N ILE B 126 1555 1555 1.33
LINK C GLN B 144 N MSE B 145 1555 1555 1.33
LINK C MSE B 145 N MSE B 146 1555 1555 1.33
LINK C MSE B 146 N THR B 147 1555 1555 1.33
LINK C ASP G1792 N MSE G1793 1555 1555 1.32
LINK C MSE G1793 N PHE G1794 1555 1555 1.33
LINK C ASN G1837 N MSE G1838 1555 1555 1.33
LINK C MSE G1838 N ASP G1839 1555 1555 1.33
LINK C PRO G1841 N MSE G1842 1555 1555 1.32
LINK C MSE G1842 N VAL G1843 1555 1555 1.33
LINK C CYS G1850 N MSE G1851 1555 1555 1.32
LINK C MSE G1851 N ASP G1852 1555 1555 1.33
LINK C GLU G1867 N MSE G1868 1555 1555 1.33
LINK C MSE G1868 N ASP G1869 1555 1555 1.33
LINK C GLN G1874 N MSE G1875 1555 1555 1.33
LINK C MSE G1875 N GLU G1876 1555 1555 1.33
LINK C PHE G1879 N MSE G1880 1555 1555 1.33
LINK C MSE G1880 N ALA G1881 1555 1555 1.33
LINK C ALA G1905 N MSE G1906 1555 1555 1.33
LINK C MSE G1906 N VAL G1907 1555 1555 1.34
LINK C VAL C 36 N MSE C 37 1555 1555 1.32
LINK C MSE C 37 N ARG C 38 1555 1555 1.33
LINK C ASP C 51 N MSE C 52 1555 1555 1.33
LINK C MSE C 52 N ILE C 53 1555 1555 1.33
LINK C THR C 71 N MSE C 72 1555 1555 1.33
LINK C MSE C 72 N MSE C 73 1555 1555 1.33
LINK C MSE C 73 N ALA C 74 1555 1555 1.33
LINK C LYS C 76 N MSE C 77 1555 1555 1.33
LINK C MSE C 77 N LYS C 78 1555 1555 1.33
LINK C VAL C 109 N MSE C 110 1555 1555 1.33
LINK C MSE C 110 N THR C 111 1555 1555 1.33
LINK C GLU C 124 N MSE C 125 1555 1555 1.33
LINK C MSE C 125 N ILE C 126 1555 1555 1.32
LINK C GLN C 144 N MSE C 145 1555 1555 1.33
LINK C MSE C 145 N MSE C 146 1555 1555 1.33
LINK C MSE C 146 N THR C 147 1555 1555 1.33
LINK C ASP H1792 N MSE H1793 1555 1555 1.33
LINK C MSE H1793 N PHE H1794 1555 1555 1.33
LINK C ASN H1837 N MSE H1838 1555 1555 1.33
LINK C MSE H1838 N ASP H1839 1555 1555 1.33
LINK C PRO H1841 N MSE H1842 1555 1555 1.33
LINK C MSE H1842 N VAL H1843 1555 1555 1.33
LINK C CYS H1850 N MSE H1851 1555 1555 1.33
LINK C MSE H1851 N ASP H1852 1555 1555 1.33
LINK C GLU H1867 N MSE H1868 1555 1555 1.33
LINK C MSE H1868 N ASP H1869 1555 1555 1.33
LINK C GLN H1874 N MSE H1875 1555 1555 1.33
LINK C MSE H1875 N GLU H1876 1555 1555 1.33
LINK C PHE H1879 N MSE H1880 1555 1555 1.34
LINK C MSE H1880 N ALA H1881 1555 1555 1.33
LINK C ALA H1905 N MSE H1906 1555 1555 1.33
LINK C MSE H1906 N VAL H1907 1555 1555 1.32
LINK C VAL D 36 N MSE D 37 1555 1555 1.32
LINK C MSE D 37 N ARG D 38 1555 1555 1.33
LINK C ASP D 51 N MSE D 52 1555 1555 1.33
LINK C MSE D 52 N ILE D 53 1555 1555 1.33
LINK C THR D 71 N MSE D 72 1555 1555 1.33
LINK C MSE D 72 N MSE D 73 1555 1555 1.33
LINK C MSE D 73 N ALA D 74 1555 1555 1.33
LINK C LYS D 76 N MSE D 77 1555 1555 1.33
LINK C MSE D 77 N LYS D 78 1555 1555 1.33
LINK C VAL D 109 N MSE D 110 1555 1555 1.33
LINK C MSE D 110 N THR D 111 1555 1555 1.33
LINK C GLU D 124 N MSE D 125 1555 1555 1.33
LINK C MSE D 125 N ILE D 126 1555 1555 1.32
LINK C GLN D 144 N MSE D 145 1555 1555 1.33
LINK C MSE D 145 N MSE D 146 1555 1555 1.33
LINK C MSE D 146 N THR D 147 1555 1555 1.34
LINK C ASP I1792 N MSE I1793 1555 1555 1.33
LINK C MSE I1793 N PHE I1794 1555 1555 1.33
LINK C ASN I1837 N MSE I1838 1555 1555 1.33
LINK C MSE I1838 N ASP I1839 1555 1555 1.33
LINK C PRO I1841 N MSE I1842 1555 1555 1.32
LINK C MSE I1842 N VAL I1843 1555 1555 1.32
LINK C CYS I1850 N MSE I1851 1555 1555 1.33
LINK C MSE I1851 N ASP I1852 1555 1555 1.33
LINK C GLU I1867 N MSE I1868 1555 1555 1.33
LINK C MSE I1868 N ASP I1869 1555 1555 1.33
LINK C GLN I1874 N MSE I1875 1555 1555 1.33
LINK C MSE I1875 N GLU I1876 1555 1555 1.33
LINK C PHE I1879 N MSE I1880 1555 1555 1.32
LINK C MSE I1880 N ALA I1881 1555 1555 1.33
LINK C ALA I1905 N MSE I1906 1555 1555 1.33
LINK C MSE I1906 N VAL I1907 1555 1555 1.33
LINK C VAL E 36 N MSE E 37 1555 1555 1.33
LINK C MSE E 37 N ARG E 38 1555 1555 1.33
LINK C ASP E 51 N MSE E 52 1555 1555 1.33
LINK C MSE E 52 N ILE E 53 1555 1555 1.33
LINK C THR E 71 N MSE E 72 1555 1555 1.33
LINK C MSE E 72 N MSE E 73 1555 1555 1.33
LINK C MSE E 73 N ALA E 74 1555 1555 1.33
LINK C LYS E 76 N MSE E 77 1555 1555 1.33
LINK C MSE E 77 N LYS E 78 1555 1555 1.34
LINK C VAL E 109 N MSE E 110 1555 1555 1.34
LINK C MSE E 110 N THR E 111 1555 1555 1.33
LINK C GLU E 124 N MSE E 125 1555 1555 1.33
LINK C MSE E 125 N ILE E 126 1555 1555 1.33
LINK C GLN E 144 N MSE E 145 1555 1555 1.33
LINK C MSE E 145 N MSE E 146 1555 1555 1.33
LINK C MSE E 146 N THR E 147 1555 1555 1.33
LINK C ASP J1792 N MSE J1793 1555 1555 1.33
LINK C MSE J1793 N PHE J1794 1555 1555 1.32
LINK C ASN J1837 N MSE J1838 1555 1555 1.33
LINK C MSE J1838 N ASP J1839 1555 1555 1.34
LINK C PRO J1841 N MSE J1842 1555 1555 1.32
LINK C MSE J1842 N VAL J1843 1555 1555 1.34
LINK C CYS J1850 N MSE J1851 1555 1555 1.32
LINK C MSE J1851 N ASP J1852 1555 1555 1.33
LINK C GLU J1867 N MSE J1868 1555 1555 1.33
LINK C MSE J1868 N ASP J1869 1555 1555 1.33
LINK C GLN J1874 N MSE J1875 1555 1555 1.33
LINK C MSE J1875 N GLU J1876 1555 1555 1.33
LINK C PHE J1879 N MSE J1880 1555 1555 1.33
LINK C MSE J1880 N ALA J1881 1555 1555 1.32
LINK C ALA J1905 N MSE J1906 1555 1555 1.34
LINK C MSE J1906 N VAL J1907 1555 1555 1.33
LINK OD1 ASP A 21 MG MG A 201 1555 1555 2.07
LINK OD1 ASP A 23 MG MG A 201 1555 1555 2.06
LINK OD1 ASP A 25 MG MG A 201 1555 1555 2.07
LINK O THR A 27 MG MG A 201 1555 1555 2.06
LINK OD1 ASP A 57 MG MG A 202 1555 1555 2.09
LINK O THR A 63 MG MG A 202 1555 1555 2.08
LINK OG1 THR A 63 MG MG A 202 1555 1555 2.08
LINK OE1 GLU A 68 MG MG A 202 1555 1555 2.30
LINK OD1 ASP A 94 MG MG A 203 1555 1555 2.08
LINK OD1 ASP A 96 MG MG A 203 1555 1555 2.06
LINK OD1 ASN A 98 MG MG A 203 1555 1555 2.07
LINK O TYR A 100 MG MG A 203 1555 1555 2.04
LINK OD1 ASP A 130 MG MG A 204 1555 1555 2.07
LINK OD1 ASP A 132 MG MG A 204 1555 1555 2.07
LINK OD1 ASP A 134 MG MG A 204 1555 1555 2.05
LINK O GLN A 136 MG MG A 204 1555 1555 1.99
LINK MG MG A 201 O HOH A 308 1555 1555 1.98
LINK MG MG A 202 O HOH A 301 1555 1555 1.99
LINK MG MG A 202 O HOH A 304 1555 1555 2.07
LINK MG MG A 203 O HOH A 306 1555 1555 1.94
LINK MG MG A 204 O HOH A 302 1555 1555 2.00
LINK MG MG A 204 O HOH A 305 1555 1555 2.01
LINK OD1 ASP B 21 MG MG B 201 1555 1555 2.09
LINK OD1 ASP B 23 MG MG B 201 1555 1555 2.07
LINK OD1 ASP B 25 MG MG B 201 1555 1555 2.08
LINK OD2 ASP B 25 MG MG B 201 1555 1555 2.99
LINK O THR B 27 MG MG B 201 1555 1555 2.07
LINK OD1 ASP B 94 MG MG B 202 1555 1555 2.04
LINK OD1 ASP B 96 MG MG B 202 1555 1555 2.06
LINK OD1 ASN B 98 MG MG B 202 1555 1555 2.04
LINK O TYR B 100 MG MG B 202 1555 1555 2.05
LINK OD1 ASP B 130 MG MG B 203 1555 1555 2.07
LINK OD1 ASP B 132 MG MG B 203 1555 1555 2.07
LINK OD1 ASP B 134 MG MG B 203 1555 1555 2.07
LINK O GLN B 136 MG MG B 203 1555 1555 2.04
LINK MG MG B 201 O HOH B 303 1555 1555 2.11
LINK MG MG B 203 O HOH B 302 1555 1555 2.06
LINK OD1 ASP C 21 MG MG C 201 1555 1555 2.09
LINK OD1 ASP C 23 MG MG C 201 1555 1555 2.07
LINK OD1 ASP C 25 MG MG C 201 1555 1555 2.05
LINK O THR C 27 MG MG C 201 1555 1555 2.07
LINK O THR C 63 MG MG C 202 1555 1555 2.06
LINK OG1 THR C 63 MG MG C 202 1555 1555 2.10
LINK OD1 ASP C 65 MG MG C 206 1555 1555 2.54
LINK OD1 ASP C 94 MG MG C 203 1555 1555 2.07
LINK OD1 ASP C 96 MG MG C 203 1555 1555 2.07
LINK OD1 ASN C 98 MG MG C 203 1555 1555 2.03
LINK O TYR C 100 MG MG C 203 1555 1555 2.06
LINK OD1 ASP C 130 MG MG C 204 1555 1555 2.08
LINK OD1 ASP C 132 MG MG C 204 1555 1555 2.07
LINK OD1 ASP C 134 MG MG C 204 1555 1555 2.06
LINK O GLN C 136 MG MG C 204 1555 1555 2.09
LINK MG MG C 201 O HOH C 304 1555 1555 2.02
LINK MG MG C 202 O HOH C 301 1555 1555 1.99
LINK MG MG C 202 O HOH C 302 1555 1555 1.98
LINK MG MG C 202 O HOH C 303 1555 1555 2.07
LINK MG MG C 202 O HOH C 305 1555 1555 2.07
LINK MG MG C 204 O HOH C 306 1555 1555 2.11
LINK MG MG C 206 OD2 ASP D 65 2646 1555 2.23
LINK OD1 ASP D 21 MG MG D 201 1555 1555 2.07
LINK OD1 ASP D 23 MG MG D 201 1555 1555 2.06
LINK OD1 ASP D 25 MG MG D 201 1555 1555 2.07
LINK O THR D 27 MG MG D 201 1555 1555 2.06
LINK O THR D 63 MG MG D 202 1555 1555 2.07
LINK OG1 THR D 63 MG MG D 202 1555 1555 2.06
LINK OD1 ASP D 94 MG MG D 203 1555 1555 2.06
LINK OD1 ASP D 96 MG MG D 203 1555 1555 2.07
LINK OD1 ASN D 98 MG MG D 203 1555 1555 2.07
LINK O TYR D 100 MG MG D 203 1555 1555 2.07
LINK OD1 ASP D 130 MG MG D 204 1555 1555 2.07
LINK OD1 ASP D 132 MG MG D 204 1555 1555 2.08
LINK OD1 ASP D 134 MG MG D 204 1555 1555 2.06
LINK O GLN D 136 MG MG D 204 1555 1555 2.06
LINK MG MG D 201 O HOH D1103 1555 1555 2.07
LINK MG MG D 202 O HOH D1101 1555 1555 1.98
LINK MG MG D 202 O HOH D1104 1555 1555 2.07
LINK MG MG D 202 O HOH D1105 1555 1555 1.98
LINK MG MG D 202 O HOH D1106 1555 1555 2.24
LINK MG MG D 203 O HOH D1108 1555 1555 2.10
LINK MG MG D 204 O HOH D1102 1555 1555 2.10
LINK OD1 ASP E 94 MG MG E 201 1555 1555 2.08
LINK OD1 ASP E 96 MG MG E 201 1555 1555 2.07
LINK OD1 ASN E 98 MG MG E 201 1555 1555 2.08
LINK O TYR E 100 MG MG E 201 1555 1555 2.07
LINK OD1 ASP E 130 MG MG E 202 1555 1555 2.05
LINK OD1 ASP E 132 MG MG E 202 1555 1555 2.06
LINK OD1 ASP E 134 MG MG E 202 1555 1555 2.12
LINK MG MG E 201 O HOH E 304 1555 1555 2.02
LINK MG MG E 202 O HOH E 301 1555 1555 1.99
CISPEP 1 ALA J 1778 THR J 1779 0 6.66
SITE 1 AC1 5 ASP A 21 ASP A 23 ASP A 25 THR A 27
SITE 2 AC1 5 HOH A 308
SITE 1 AC2 5 ASP A 57 THR A 63 GLU A 68 HOH A 301
SITE 2 AC2 5 HOH A 304
SITE 1 AC3 5 ASP A 94 ASP A 96 ASN A 98 TYR A 100
SITE 2 AC3 5 HOH A 306
SITE 1 AC4 6 ASP A 130 ASP A 132 ASP A 134 GLN A 136
SITE 2 AC4 6 HOH A 302 HOH A 305
SITE 1 AC5 2 HIS A 108 ASN A 112
SITE 1 AC6 3 ARG A 127 ARG F1919 HIS F1923
SITE 1 AC7 5 ASP B 21 ASP B 23 ASP B 25 THR B 27
SITE 2 AC7 5 HOH B 303
SITE 1 AC8 4 ASP B 94 ASP B 96 ASN B 98 TYR B 100
SITE 1 AC9 5 ASP B 130 ASP B 132 ASP B 134 GLN B 136
SITE 2 AC9 5 HOH B 302
SITE 1 AD1 2 HIS B 108 ASN B 112
SITE 1 AD2 2 ARG G1826 ALA G1828
SITE 1 AD3 5 ASP C 21 ASP C 23 ASP C 25 THR C 27
SITE 2 AD3 5 HOH C 304
SITE 1 AD4 6 THR C 63 GLU C 68 HOH C 301 HOH C 302
SITE 2 AD4 6 HOH C 303 HOH C 305
SITE 1 AD5 4 ASP C 94 ASP C 96 ASN C 98 TYR C 100
SITE 1 AD6 5 ASP C 130 ASP C 132 ASP C 134 GLN C 136
SITE 2 AD6 5 HOH C 306
SITE 1 AD7 2 HIS C 108 ASN C 112
SITE 1 AD8 1 ASP C 65
SITE 1 AD9 3 ARG C 127 ARG H1919 HIS H1923
SITE 1 AE1 5 ASP D 21 ASP D 23 ASP D 25 THR D 27
SITE 2 AE1 5 HOH D1103
SITE 1 AE2 5 THR D 63 HOH D1101 HOH D1104 HOH D1105
SITE 2 AE2 5 HOH D1106
SITE 1 AE3 5 ASP D 94 ASP D 96 ASN D 98 TYR D 100
SITE 2 AE3 5 HOH D1108
SITE 1 AE4 5 ASP D 130 ASP D 132 ASP D 134 GLN D 136
SITE 2 AE4 5 HOH D1102
SITE 1 AE5 5 ASP E 94 ASP E 96 ASN E 98 TYR E 100
SITE 2 AE5 5 HOH E 304
SITE 1 AE6 6 ASP E 130 ASP E 132 ASP E 134 GLN E 136
SITE 2 AE6 6 VAL E 137 HOH E 301
SITE 1 AE7 2 ARG J1919 HIS J1923
CRYST1 106.128 99.006 109.281 90.00 106.11 90.00 P 1 21 1 10
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 0.009423 0.000000 0.002722 0.00000
SCALE2 0.000000 0.010100 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009525 0.00000
(ATOM LINES ARE NOT SHOWN.)
END