HEADER PROTEIN BINDING 11-JAN-12 4D8O
TITLE CRYSTAL STRUCTURE OF THE ANKYRIN-B ZU5-ZU5-UPA-DD TANDEM
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ANKYRIN-2;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RESIDUES 966-1535;
COMPND 5 SYNONYM: ANK-2, ANKYRIN-B, BRAIN ANKYRIN, NON-ERYTHROID ANKYRIN;
COMPND 6 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: ANK2;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET32A
KEYWDS ZU5, UPA, DEATH DOMAIN, SUPRAMODULE, PROTEIN BINDING
EXPDTA X-RAY DIFFRACTION
AUTHOR Z.WEI,C.WANG,C.YU,M.ZHANG
REVDAT 5 08-NOV-23 4D8O 1 SEQADV
REVDAT 4 15-NOV-17 4D8O 1 REMARK
REVDAT 3 16-AUG-17 4D8O 1 SOURCE REMARK
REVDAT 2 26-JUN-13 4D8O 1 JRNL
REVDAT 1 28-MAR-12 4D8O 0
JRNL AUTH C.WANG,C.YU,F.YE,Z.WEI,M.ZHANG
JRNL TITL STRUCTURE OF THE ZU5-ZU5-UPA-DD TANDEM OF ANKYRIN-B REVEALS
JRNL TITL 2 INTERACTION SURFACES NECESSARY FOR ANKYRIN FUNCTION
JRNL REF PROC.NATL.ACAD.SCI.USA V. 109 4822 2012
JRNL REFN ISSN 0027-8424
JRNL PMID 22411828
JRNL DOI 10.1073/PNAS.1200613109
REMARK 2
REMARK 2 RESOLUTION. 2.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.6.4_486
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 36.89
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 95.3
REMARK 3 NUMBER OF REFLECTIONS : 28402
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.210
REMARK 3 R VALUE (WORKING SET) : 0.208
REMARK 3 FREE R VALUE : 0.245
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.130
REMARK 3 FREE R VALUE TEST SET COUNT : 1457
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 36.8918 - 4.7433 0.95 2855 137 0.2052 0.2309
REMARK 3 2 4.7433 - 3.7661 0.99 2870 144 0.1753 0.1727
REMARK 3 3 3.7661 - 3.2904 1.00 2816 153 0.2016 0.2895
REMARK 3 4 3.2904 - 2.9897 0.99 2815 162 0.2218 0.2488
REMARK 3 5 2.9897 - 2.7755 0.97 2707 163 0.2331 0.2657
REMARK 3 6 2.7755 - 2.6119 0.96 2698 149 0.2284 0.2904
REMARK 3 7 2.6119 - 2.4811 0.94 2636 141 0.2332 0.3035
REMARK 3 8 2.4811 - 2.3731 0.93 2589 145 0.2352 0.2974
REMARK 3 9 2.3731 - 2.2818 0.90 2524 122 0.2396 0.2909
REMARK 3 10 2.2818 - 2.2030 0.89 2435 141 0.2536 0.2988
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.30
REMARK 3 SHRINKAGE RADIUS : 1.06
REMARK 3 K_SOL : 0.38
REMARK 3 B_SOL : 59.33
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.240
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.650
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 57.15
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 15.18160
REMARK 3 B22 (A**2) : -6.49460
REMARK 3 B33 (A**2) : -8.68690
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 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.005 4076
REMARK 3 ANGLE : 0.874 5527
REMARK 3 CHIRALITY : 0.059 631
REMARK 3 PLANARITY : 0.004 715
REMARK 3 DIHEDRAL : 13.521 1509
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 4
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN A AND RESSEQ 964:1124
REMARK 3 ORIGIN FOR THE GROUP (A): -28.2016 -22.3099 34.5137
REMARK 3 T TENSOR
REMARK 3 T11: 0.4399 T22: 0.3420
REMARK 3 T33: 0.3158 T12: 0.0105
REMARK 3 T13: 0.0367 T23: 0.0092
REMARK 3 L TENSOR
REMARK 3 L11: 1.3405 L22: 1.4262
REMARK 3 L33: 3.8855 L12: 1.6989
REMARK 3 L13: -1.2893 L23: -1.8471
REMARK 3 S TENSOR
REMARK 3 S11: 0.1385 S12: -0.2502 S13: -0.0619
REMARK 3 S21: 0.1088 S22: -0.1579 S23: -0.0161
REMARK 3 S31: 0.3297 S32: 0.2674 S33: 0.0209
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN A AND RESSEQ 1125:1289
REMARK 3 ORIGIN FOR THE GROUP (A): -38.6041 -13.9007 3.6514
REMARK 3 T TENSOR
REMARK 3 T11: 0.3111 T22: 0.2955
REMARK 3 T33: 0.3435 T12: -0.0445
REMARK 3 T13: -0.0165 T23: -0.0145
REMARK 3 L TENSOR
REMARK 3 L11: 1.5745 L22: 1.3897
REMARK 3 L33: 2.3705 L12: 0.0550
REMARK 3 L13: 0.5349 L23: -1.0386
REMARK 3 S TENSOR
REMARK 3 S11: 0.0373 S12: -0.1119 S13: -0.1427
REMARK 3 S21: -0.1251 S22: 0.0224 S23: 0.1597
REMARK 3 S31: 0.0887 S32: -0.1679 S33: -0.0332
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN A AND RESSEQ 1290:1423
REMARK 3 ORIGIN FOR THE GROUP (A): -7.1032 -0.5432 24.0622
REMARK 3 T TENSOR
REMARK 3 T11: 0.3377 T22: 0.3152
REMARK 3 T33: 0.2964 T12: -0.0449
REMARK 3 T13: 0.0512 T23: 0.0110
REMARK 3 L TENSOR
REMARK 3 L11: 2.1789 L22: 2.7071
REMARK 3 L33: 1.9270 L12: 1.6010
REMARK 3 L13: 0.1522 L23: 0.9869
REMARK 3 S TENSOR
REMARK 3 S11: -0.0884 S12: 0.0954 S13: -0.0274
REMARK 3 S21: -0.2854 S22: 0.1900 S23: -0.1811
REMARK 3 S31: -0.3410 S32: 0.2359 S33: -0.1027
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN A AND RESSEQ 1452:1529
REMARK 3 ORIGIN FOR THE GROUP (A): 11.1842 -15.9627 21.3993
REMARK 3 T TENSOR
REMARK 3 T11: 0.5062 T22: 0.4596
REMARK 3 T33: 0.4440 T12: -0.0068
REMARK 3 T13: 0.0384 T23: -0.1092
REMARK 3 L TENSOR
REMARK 3 L11: 1.9104 L22: 4.5910
REMARK 3 L33: 1.8036 L12: 1.3817
REMARK 3 L13: 0.5274 L23: 2.2729
REMARK 3 S TENSOR
REMARK 3 S11: -0.1953 S12: 0.2347 S13: 0.2141
REMARK 3 S21: 0.3847 S22: 0.2913 S23: 0.2817
REMARK 3 S31: 0.4602 S32: 0.3209 S33: -0.0474
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4D8O COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 25-JAN-12.
REMARK 100 THE DEPOSITION ID IS D_1000070021.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 18-DEC-10
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRF
REMARK 200 BEAMLINE : BL17U
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.98
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO, HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK, HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 29634
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.200
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 200 DATA REDUNDANCY : 6.800
REMARK 200 R MERGE (I) : 0.08500
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.24
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 7.30
REMARK 200 R MERGE FOR SHELL (I) : 0.48300
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: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 3F59, 3G5B, 2YVI
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 43.45
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.18
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 18% PEG3350, 0.2M AMMONIUM ACETATE, 5%
REMARK 280 N-OCTYL-BETA-D-GLUCOSIDE, PH 7.5, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 289K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
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 37.83700
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 47.49400
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 40.02800
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 47.49400
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 37.83700
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 40.02800
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 MET A 946
REMARK 465 HIS A 947
REMARK 465 HIS A 948
REMARK 465 HIS A 949
REMARK 465 HIS A 950
REMARK 465 HIS A 951
REMARK 465 HIS A 952
REMARK 465 SER A 953
REMARK 465 SER A 954
REMARK 465 GLY A 955
REMARK 465 LEU A 956
REMARK 465 GLU A 957
REMARK 465 VAL A 958
REMARK 465 LEU A 959
REMARK 465 PHE A 960
REMARK 465 GLN A 961
REMARK 465 GLY A 962
REMARK 465 PRO A 963
REMARK 465 THR A 1080
REMARK 465 GLU A 1081
REMARK 465 ASP A 1082
REMARK 465 GLU A 1083
REMARK 465 LEU A 1084
REMARK 465 ASN A 1085
REMARK 465 GLU A 1086
REMARK 465 ILE A 1087
REMARK 465 LEU A 1088
REMARK 465 ASN A 1089
REMARK 465 LYS A 1361
REMARK 465 SER A 1362
REMARK 465 GLY A 1363
REMARK 465 LYS A 1402
REMARK 465 SER A 1403
REMARK 465 THR A 1404
REMARK 465 ARG A 1405
REMARK 465 GLY A 1406
REMARK 465 LEU A 1407
REMARK 465 VAL A 1408
REMARK 465 LYS A 1424
REMARK 465 GLU A 1425
REMARK 465 SER A 1426
REMARK 465 GLU A 1427
REMARK 465 SER A 1428
REMARK 465 ASP A 1429
REMARK 465 GLN A 1430
REMARK 465 GLU A 1431
REMARK 465 GLN A 1432
REMARK 465 GLU A 1433
REMARK 465 GLU A 1434
REMARK 465 GLU A 1435
REMARK 465 ILE A 1436
REMARK 465 ASP A 1437
REMARK 465 MET A 1438
REMARK 465 THR A 1439
REMARK 465 SER A 1440
REMARK 465 GLU A 1441
REMARK 465 LYS A 1442
REMARK 465 ASN A 1443
REMARK 465 PRO A 1444
REMARK 465 GLN A 1445
REMARK 465 ASP A 1446
REMARK 465 GLU A 1447
REMARK 465 GLN A 1448
REMARK 465 GLU A 1449
REMARK 465 ARG A 1450
REMARK 465 ILE A 1451
REMARK 465 LEU A 1530
REMARK 465 MET A 1531
REMARK 465 GLU A 1532
REMARK 465 THR A 1533
REMARK 465 ASN A 1534
REMARK 465 THR A 1535
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 ARG A1011 CG CD NE CZ NH1 NH2
REMARK 470 LYS A1057 CG CD CE NZ
REMARK 470 ASP A1078 CG OD1 OD2
REMARK 470 GLU A1171 CG CD OE1 OE2
REMARK 470 LYS A1175 CG CD CE NZ
REMARK 470 ILE A1307 CG1 CG2 CD1
REMARK 470 LYS A1323 CG CD CE NZ
REMARK 470 GLU A1326 CG CD OE1 OE2
REMARK 470 GLN A1327 CG CD OE1 NE2
REMARK 470 GLN A1364 CG CD OE1 NE2
REMARK 470 GLU A1390 CG CD OE1 OE2
REMARK 470 GLU A1452 CG CD OE1 OE2
REMARK 470 GLU A1453 CG CD OE1 OE2
REMARK 470 LEU A1455 CG CD1 CD2
REMARK 470 GLU A1468 CG CD OE1 OE2
REMARK 470 LYS A1508 CG CD CE NZ
REMARK 470 GLU A1517 CG CD OE1 OE2
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 SER A 971 111.42 -161.84
REMARK 500 ASP A 975 -150.29 -140.59
REMARK 500 ARG A 985 -81.39 -115.75
REMARK 500 PHE A1051 21.08 -141.69
REMARK 500 ASP A1070 -70.85 -81.93
REMARK 500 ARG A1193 51.34 71.03
REMARK 500 SER A1210 -165.67 -103.32
REMARK 500 GLU A1254 25.73 46.22
REMARK 500 ALA A1264 -168.50 -162.59
REMARK 500 ASP A1305 -170.76 -171.95
REMARK 500 LYS A1320 -1.40 74.29
REMARK 500 GLN A1328 45.96 -96.92
REMARK 500 ASN A1330 -12.25 89.77
REMARK 500 ALA A1335 149.27 -172.04
REMARK 500 ALA A1510 70.39 -103.11
REMARK 500 ARG A1524 51.49 -116.76
REMARK 500
REMARK 500 REMARK: NULL
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 A PART OF RESIDUES 1211-1219 IN Q01484 HAS BEEN DELETED.
REMARK 999 THE SEQUENCE OF RESIDUES 1220-1535 IS FROM
REMARK 999 ISOFORM 2 OF ANKYRIN-2 (Q01484-2).
DBREF 4D8O A 966 1210 UNP Q01484 ANK2_HUMAN 966 1210
DBREF 4D8O A 1220 1535 UNP Q01484 ANK2_HUMAN 1253 1568
SEQADV 4D8O MET A 946 UNP Q01484 EXPRESSION TAG
SEQADV 4D8O HIS A 947 UNP Q01484 EXPRESSION TAG
SEQADV 4D8O HIS A 948 UNP Q01484 EXPRESSION TAG
SEQADV 4D8O HIS A 949 UNP Q01484 EXPRESSION TAG
SEQADV 4D8O HIS A 950 UNP Q01484 EXPRESSION TAG
SEQADV 4D8O HIS A 951 UNP Q01484 EXPRESSION TAG
SEQADV 4D8O HIS A 952 UNP Q01484 EXPRESSION TAG
SEQADV 4D8O SER A 953 UNP Q01484 EXPRESSION TAG
SEQADV 4D8O SER A 954 UNP Q01484 EXPRESSION TAG
SEQADV 4D8O GLY A 955 UNP Q01484 EXPRESSION TAG
SEQADV 4D8O LEU A 956 UNP Q01484 EXPRESSION TAG
SEQADV 4D8O GLU A 957 UNP Q01484 EXPRESSION TAG
SEQADV 4D8O VAL A 958 UNP Q01484 EXPRESSION TAG
SEQADV 4D8O LEU A 959 UNP Q01484 EXPRESSION TAG
SEQADV 4D8O PHE A 960 UNP Q01484 EXPRESSION TAG
SEQADV 4D8O GLN A 961 UNP Q01484 EXPRESSION TAG
SEQADV 4D8O GLY A 962 UNP Q01484 EXPRESSION TAG
SEQADV 4D8O PRO A 963 UNP Q01484 EXPRESSION TAG
SEQADV 4D8O GLU A 964 UNP Q01484 EXPRESSION TAG
SEQADV 4D8O PHE A 965 UNP Q01484 EXPRESSION TAG
SEQRES 1 A 581 MET HIS HIS HIS HIS HIS HIS SER SER GLY LEU GLU VAL
SEQRES 2 A 581 LEU PHE GLN GLY PRO GLU PHE SER GLY PHE LEU VAL SER
SEQRES 3 A 581 PHE MET VAL ASP ALA ARG GLY GLY ALA MET ARG GLY CYS
SEQRES 4 A 581 ARG HIS ASN GLY LEU ARG ILE ILE ILE PRO PRO ARG LYS
SEQRES 5 A 581 CYS THR ALA PRO THR ARG VAL THR CYS ARG LEU VAL LYS
SEQRES 6 A 581 ARG HIS ARG LEU ALA THR MET PRO PRO MET VAL GLU GLY
SEQRES 7 A 581 GLU GLY LEU ALA SER ARG LEU ILE GLU VAL GLY PRO SER
SEQRES 8 A 581 GLY ALA GLN PHE LEU GLY PRO VAL ILE VAL GLU ILE PRO
SEQRES 9 A 581 HIS PHE ALA ALA LEU ARG GLY LYS GLU ARG GLU LEU VAL
SEQRES 10 A 581 VAL LEU ARG SER GLU ASN GLY ASP SER TRP LYS GLU HIS
SEQRES 11 A 581 PHE CYS ASP TYR THR GLU ASP GLU LEU ASN GLU ILE LEU
SEQRES 12 A 581 ASN GLY MET ASP GLU VAL LEU ASP SER PRO GLU ASP LEU
SEQRES 13 A 581 GLU LYS LYS ARG ILE CYS ARG ILE ILE THR ARG ASP PHE
SEQRES 14 A 581 PRO GLN TYR PHE ALA VAL VAL SER ARG ILE LYS GLN ASP
SEQRES 15 A 581 SER ASN LEU ILE GLY PRO GLU GLY GLY VAL LEU SER SER
SEQRES 16 A 581 THR VAL VAL PRO GLN VAL GLN ALA VAL PHE PRO GLU GLY
SEQRES 17 A 581 ALA LEU THR LYS ARG ILE ARG VAL GLY LEU GLN ALA GLN
SEQRES 18 A 581 PRO MET HIS SER GLU LEU VAL LYS LYS ILE LEU GLY ASN
SEQRES 19 A 581 LYS ALA THR PHE SER PRO ILE VAL THR LEU GLU PRO ARG
SEQRES 20 A 581 ARG ARG LYS PHE HIS LYS PRO ILE THR MET THR ILE PRO
SEQRES 21 A 581 VAL PRO LYS ALA SER GLY ASP ALA PRO THR LEU ARG LEU
SEQRES 22 A 581 LEU CYS SER ILE THR GLY GLY THR THR PRO ALA GLN TRP
SEQRES 23 A 581 GLU ASP ILE THR GLY THR THR PRO LEU THR PHE VAL ASN
SEQRES 24 A 581 GLU CYS VAL SER PHE THR THR ASN VAL SER ALA ARG PHE
SEQRES 25 A 581 TRP LEU ILE ASP CYS ARG GLN ILE GLN GLU SER VAL THR
SEQRES 26 A 581 PHE ALA SER GLN VAL TYR ARG GLU ILE ILE CYS VAL PRO
SEQRES 27 A 581 TYR MET ALA LYS PHE VAL VAL PHE ALA LYS SER HIS ASP
SEQRES 28 A 581 PRO ILE GLU ALA ARG LEU ARG CYS PHE CYS MET THR ASP
SEQRES 29 A 581 ASP LYS VAL ASP LYS THR LEU GLU GLN GLN GLU ASN PHE
SEQRES 30 A 581 ALA GLU VAL ALA ARG SER ARG ASP VAL GLU VAL LEU GLU
SEQRES 31 A 581 GLY LYS PRO ILE TYR VAL ASP CYS PHE GLY ASN LEU VAL
SEQRES 32 A 581 PRO LEU THR LYS SER GLY GLN HIS HIS ILE PHE SER PHE
SEQRES 33 A 581 PHE ALA PHE LYS GLU ASN ARG LEU PRO LEU PHE VAL LYS
SEQRES 34 A 581 VAL ARG ASP THR THR GLN GLU PRO CYS GLY ARG LEU SER
SEQRES 35 A 581 PHE MET LYS GLU PRO LYS SER THR ARG GLY LEU VAL HIS
SEQRES 36 A 581 GLN ALA ILE CYS ASN LEU ASN ILE THR LEU PRO ILE TYR
SEQRES 37 A 581 THR LYS GLU SER GLU SER ASP GLN GLU GLN GLU GLU GLU
SEQRES 38 A 581 ILE ASP MET THR SER GLU LYS ASN PRO GLN ASP GLU GLN
SEQRES 39 A 581 GLU ARG ILE GLU GLU ARG LEU ALA TYR ILE ALA ASP HIS
SEQRES 40 A 581 LEU GLY PHE SER TRP THR GLU LEU ALA ARG GLU LEU ASP
SEQRES 41 A 581 PHE THR GLU GLU GLN ILE HIS GLN ILE ARG ILE GLU ASN
SEQRES 42 A 581 PRO ASN SER LEU GLN ASP GLN SER HIS ALA LEU LEU LYS
SEQRES 43 A 581 TYR TRP LEU GLU ARG ASP GLY LYS HIS ALA THR ASP THR
SEQRES 44 A 581 ASN LEU VAL GLU CYS LEU THR LYS ILE ASN ARG MET ASP
SEQRES 45 A 581 ILE VAL HIS LEU MET GLU THR ASN THR
FORMUL 2 HOH *101(H2 O)
HELIX 1 1 SER A 1097 ARG A 1105 1 9
HELIX 2 2 HIS A 1169 GLY A 1178 1 10
HELIX 3 3 THR A 1244 THR A 1247 5 4
HELIX 4 4 GLN A 1273 GLN A 1275 5 3
HELIX 5 5 GLU A 1276 ILE A 1289 1 14
HELIX 6 6 LYS A 1323 GLN A 1327 5 5
HELIX 7 7 GLU A 1453 GLY A 1463 1 11
HELIX 8 8 PHE A 1464 LEU A 1473 1 10
HELIX 9 9 THR A 1476 ASN A 1487 1 12
HELIX 10 10 SER A 1490 GLY A 1507 1 18
HELIX 11 11 LYS A 1508 ALA A 1510 5 3
HELIX 12 12 THR A 1511 ILE A 1522 1 12
HELIX 13 13 ARG A 1524 HIS A 1529 1 6
SHEET 1 A 3 VAL A 970 VAL A 974 0
SHEET 2 A 3 THR A1002 LEU A1008 -1 O THR A1002 N VAL A 974
SHEET 3 A 3 ILE A1031 GLY A1034 -1 O GLU A1032 N ARG A1007
SHEET 1 B 4 GLY A 979 ARG A 982 0
SHEET 2 B 4 ARG A 990 ILE A 993 -1 O ILE A 993 N GLY A 979
SHEET 3 B 4 GLN A1039 PRO A1049 -1 O GLU A1047 N ARG A 990
SHEET 4 B 4 ILE A1106 ASP A1113 -1 O CYS A1107 N ILE A1048
SHEET 1 C 4 GLY A1025 LEU A1026 0
SHEET 2 C 4 TYR A1117 ILE A1124 -1 O SER A1122 N GLY A1025
SHEET 3 C 4 ARG A1059 SER A1066 -1 N LEU A1064 O ALA A1119
SHEET 4 C 4 LYS A1073 GLU A1074 -1 O LYS A1073 N ARG A1065
SHEET 1 D 5 GLN A1126 ILE A1131 0
SHEET 2 D 5 ILE A1159 GLN A1166 -1 O LEU A1163 N ASP A1127
SHEET 3 D 5 ILE A1186 GLU A1190 -1 O GLU A1190 N GLY A1162
SHEET 4 D 5 ARG A1265 CYS A1271 -1 O PHE A1266 N VAL A1187
SHEET 5 D 5 ALA A1181 PHE A1183 -1 N THR A1182 O ASP A1270
SHEET 1 E 6 GLN A1126 ILE A1131 0
SHEET 2 E 6 ILE A1159 GLN A1166 -1 O LEU A1163 N ASP A1127
SHEET 3 E 6 ILE A1186 GLU A1190 -1 O GLU A1190 N GLY A1162
SHEET 4 E 6 ARG A1265 CYS A1271 -1 O PHE A1266 N VAL A1187
SHEET 5 E 6 LEU A1225 SER A1230 -1 N ARG A1226 O ILE A1269
SHEET 6 E 6 GLU A1241 ASP A1242 -1 O GLU A1241 N CYS A1229
SHEET 1 F 5 GLY A1136 SER A1139 0
SHEET 2 F 5 GLN A1147 PHE A1150 -1 O ALA A1148 N LEU A1138
SHEET 3 F 5 LYS A1195 PRO A1205 -1 O THR A1203 N GLN A1147
SHEET 4 F 5 CYS A1255 VAL A1262 -1 O VAL A1256 N ILE A1204
SHEET 5 F 5 THR A1250 VAL A1252 -1 N THR A1250 O SER A1257
SHEET 1 G 3 ALA A1332 ARG A1336 0
SHEET 2 G 3 PRO A1292 LYS A1302 -1 N VAL A1299 O VAL A1334
SHEET 3 G 3 VAL A1340 LEU A1343 -1 O VAL A1340 N ALA A1295
SHEET 1 H 5 ALA A1332 ARG A1336 0
SHEET 2 H 5 PRO A1292 LYS A1302 -1 N VAL A1299 O VAL A1334
SHEET 3 H 5 GLU A1308 MET A1316 -1 O ARG A1310 N LYS A1302
SHEET 4 H 5 ARG A1377 VAL A1384 -1 O LEU A1380 N LEU A1311
SHEET 5 H 5 LEU A1356 PRO A1358 -1 N VAL A1357 O LYS A1383
SHEET 1 I 4 HIS A1366 SER A1369 0
SHEET 2 I 4 PRO A1347 GLY A1354 -1 N ILE A1348 O PHE A1368
SHEET 3 I 4 CYS A1392 MET A1398 -1 O MET A1398 N TYR A1349
SHEET 4 I 4 CYS A1413 THR A1418 -1 O LEU A1415 N LEU A1395
CISPEP 1 GLY A 1034 PRO A 1035 0 1.95
CISPEP 2 GLU A 1190 PRO A 1191 0 0.03
CRYST1 75.674 80.056 94.988 90.00 90.00 90.00 P 21 21 21 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 0.013215 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012491 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010528 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
