HEADER STRUCTURAL PROTEIN 18-OCT-14 4RLY
TITLE CRYSTAL STRUCTURE OF ANKB ANKYRIN REPEATS (R1-R9) IN COMPLEX WITH
TITLE 2 NAV1.2 ANKYRIN BINDING DOMAIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: NAV1.2 - ANKB CHIMERA;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS, HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: MOUSE, HUMAN;
SOURCE 4 ORGANISM_TAXID: 10090, 9606;
SOURCE 5 GENE: ANK2, SCN2A, SCN2A1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET32M
KEYWDS ANK REPEAT, PROTEIN-PROTEIN INTERACTION, STRUCTURAL PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR Z.WEI,C.WANG,M.ZHANG
REVDAT 6 28-FEB-24 4RLY 1 REMARK SEQADV
REVDAT 5 22-NOV-17 4RLY 1 REMARK
REVDAT 4 02-AUG-17 4RLY 1 SOURCE REMARK
REVDAT 3 20-MAY-15 4RLY 1 JRNL
REVDAT 2 14-JAN-15 4RLY 1 REMARK
REVDAT 1 26-NOV-14 4RLY 0
JRNL AUTH C.WANG,Z.WEI,K.CHEN,F.YE,C.YU,V.BENNETT,M.ZHANG
JRNL TITL STRUCTURAL BASIS OF DIVERSE MEMBRANE TARGET RECOGNITIONS BY
JRNL TITL 2 ANKYRINS.
JRNL REF ELIFE V. 3 04353 2014
JRNL REFN ESSN 2050-084X
JRNL PMID 25383926
JRNL DOI 10.7554/ELIFE.04353
REMARK 2
REMARK 2 RESOLUTION. 2.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX
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) : 2.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 34.23
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.2
REMARK 3 NUMBER OF REFLECTIONS : 19832
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.190
REMARK 3 R VALUE (WORKING SET) : 0.188
REMARK 3 FREE R VALUE : 0.238
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.090
REMARK 3 FREE R VALUE TEST SET COUNT : 1009
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 34.2326 - 4.7846 0.96 2804 134 0.1877 0.2226
REMARK 3 2 4.7846 - 3.7993 0.99 2717 137 0.1532 0.2021
REMARK 3 3 3.7993 - 3.3195 1.00 2712 134 0.1849 0.2424
REMARK 3 4 3.3195 - 3.0162 1.00 2659 156 0.1997 0.2671
REMARK 3 5 3.0162 - 2.8001 1.00 2665 142 0.2302 0.2978
REMARK 3 6 2.8001 - 2.6351 1.00 2637 157 0.2287 0.2974
REMARK 3 7 2.6351 - 2.5032 1.00 2629 149 0.2272 0.2453
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.10
REMARK 3 SHRINKAGE RADIUS : 0.83
REMARK 3 K_SOL : 0.34
REMARK 3 B_SOL : 57.21
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.650
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 23.700
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 53.21
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 69.27
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 10.59500
REMARK 3 B22 (A**2) : 10.59500
REMARK 3 B33 (A**2) : -21.19000
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 : 0.015 2318
REMARK 3 ANGLE : 1.543 3151
REMARK 3 CHIRALITY : 0.098 380
REMARK 3 PLANARITY : 0.006 410
REMARK 3 DIHEDRAL : 17.041 811
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 10
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESSEQ 2029:2086)
REMARK 3 ORIGIN FOR THE GROUP (A): 40.9904 -23.5263 58.6885
REMARK 3 T TENSOR
REMARK 3 T11: 0.4383 T22: 0.3059
REMARK 3 T33: 0.4453 T12: -0.0305
REMARK 3 T13: 0.0064 T23: 0.0400
REMARK 3 L TENSOR
REMARK 3 L11: 2.2584 L22: 1.5564
REMARK 3 L33: 0.6523 L12: -0.9824
REMARK 3 L13: 0.7696 L23: -0.2811
REMARK 3 S TENSOR
REMARK 3 S11: 0.0283 S12: -0.6322 S13: -0.3590
REMARK 3 S21: 0.6907 S22: 0.0262 S23: 0.2961
REMARK 3 S31: 0.1587 S32: -0.1544 S33: 0.0499
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESSEQ 2087:2152)
REMARK 3 ORIGIN FOR THE GROUP (A): 37.4855 -12.9409 43.2483
REMARK 3 T TENSOR
REMARK 3 T11: 0.3427 T22: 0.4506
REMARK 3 T33: 0.4577 T12: 0.0031
REMARK 3 T13: -0.0116 T23: -0.0623
REMARK 3 L TENSOR
REMARK 3 L11: 0.3395 L22: 0.5096
REMARK 3 L33: 0.4619 L12: -0.3727
REMARK 3 L13: 0.4468 L23: -0.3223
REMARK 3 S TENSOR
REMARK 3 S11: 0.0076 S12: 0.2931 S13: 0.0042
REMARK 3 S21: -0.2723 S22: 0.0125 S23: 0.0048
REMARK 3 S31: 0.3585 S32: -0.1460 S33: -0.0002
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESSEQ 2153:2183)
REMARK 3 ORIGIN FOR THE GROUP (A): 34.4303 -0.6067 36.9452
REMARK 3 T TENSOR
REMARK 3 T11: 0.3085 T22: 0.5235
REMARK 3 T33: 0.4778 T12: 0.0544
REMARK 3 T13: 0.0222 T23: 0.0260
REMARK 3 L TENSOR
REMARK 3 L11: 0.2332 L22: 1.5951
REMARK 3 L33: 3.6671 L12: -0.1879
REMARK 3 L13: 0.6544 L23: 1.1805
REMARK 3 S TENSOR
REMARK 3 S11: 0.4860 S12: 0.1717 S13: 0.3065
REMARK 3 S21: 0.0757 S22: -0.6265 S23: 0.5043
REMARK 3 S31: 0.2880 S32: -1.1529 S33: -0.0477
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESSEQ 2184:2204)
REMARK 3 ORIGIN FOR THE GROUP (A): 34.6617 1.8962 25.3009
REMARK 3 T TENSOR
REMARK 3 T11: 0.8482 T22: 0.6381
REMARK 3 T33: 0.4331 T12: 0.2515
REMARK 3 T13: -0.0121 T23: 0.0379
REMARK 3 L TENSOR
REMARK 3 L11: 0.4426 L22: 0.5328
REMARK 3 L33: 0.0204 L12: 0.2199
REMARK 3 L13: 0.0964 L23: 0.0272
REMARK 3 S TENSOR
REMARK 3 S11: 0.3327 S12: 0.5707 S13: -0.0248
REMARK 3 S21: -0.1411 S22: -0.1351 S23: 0.2424
REMARK 3 S31: 1.3344 S32: 0.4260 S33: -0.0146
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' AND (RESSEQ 2205:2227)
REMARK 3 ORIGIN FOR THE GROUP (A): 29.3344 15.1325 30.8628
REMARK 3 T TENSOR
REMARK 3 T11: 0.4230 T22: 0.6124
REMARK 3 T33: 0.4099 T12: 0.0930
REMARK 3 T13: -0.0335 T23: 0.0355
REMARK 3 L TENSOR
REMARK 3 L11: 0.8728 L22: 0.3579
REMARK 3 L33: 4.4035 L12: -0.0094
REMARK 3 L13: 0.7957 L23: -1.0352
REMARK 3 S TENSOR
REMARK 3 S11: -0.0682 S12: -0.2423 S13: 0.3022
REMARK 3 S21: 0.6543 S22: -0.1773 S23: -0.0859
REMARK 3 S31: -1.0005 S32: -0.1046 S33: -0.1522
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'A' AND (RESSEQ 2228:2268)
REMARK 3 ORIGIN FOR THE GROUP (A): 26.1786 10.3923 19.7096
REMARK 3 T TENSOR
REMARK 3 T11: 0.6387 T22: 0.4906
REMARK 3 T33: 0.2952 T12: 0.1849
REMARK 3 T13: 0.0612 T23: 0.0235
REMARK 3 L TENSOR
REMARK 3 L11: 0.4877 L22: 0.6346
REMARK 3 L33: 0.3082 L12: -0.3061
REMARK 3 L13: 0.2376 L23: -0.3284
REMARK 3 S TENSOR
REMARK 3 S11: 0.2322 S12: 0.1950 S13: 0.1092
REMARK 3 S21: -0.4589 S22: -0.1260 S23: 0.1771
REMARK 3 S31: 0.1312 S32: 0.4670 S33: -0.0010
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'A' AND (RESSEQ 2269:2287)
REMARK 3 ORIGIN FOR THE GROUP (A): 17.6740 5.7240 15.4184
REMARK 3 T TENSOR
REMARK 3 T11: 0.7971 T22: 0.6192
REMARK 3 T33: 0.3626 T12: 0.1551
REMARK 3 T13: -0.0789 T23: -0.0241
REMARK 3 L TENSOR
REMARK 3 L11: 0.0238 L22: 0.0252
REMARK 3 L33: 0.0854 L12: -0.0655
REMARK 3 L13: -0.0388 L23: -0.0040
REMARK 3 S TENSOR
REMARK 3 S11: 0.2135 S12: 0.5616 S13: -0.4993
REMARK 3 S21: -0.8505 S22: -0.2652 S23: 0.4161
REMARK 3 S31: 1.2610 S32: -0.2574 S33: 0.0013
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'A' AND (RESSEQ 2288:2301)
REMARK 3 ORIGIN FOR THE GROUP (A): 19.4650 14.0375 7.3215
REMARK 3 T TENSOR
REMARK 3 T11: 1.0478 T22: 0.8182
REMARK 3 T33: 0.4876 T12: 0.2388
REMARK 3 T13: 0.0145 T23: 0.0207
REMARK 3 L TENSOR
REMARK 3 L11: 0.4193 L22: 0.6267
REMARK 3 L33: 0.5886 L12: -0.1809
REMARK 3 L13: 0.3700 L23: 0.0735
REMARK 3 S TENSOR
REMARK 3 S11: 0.3097 S12: 0.1730 S13: 0.6768
REMARK 3 S21: -1.1351 S22: 0.0144 S23: -0.3025
REMARK 3 S31: -0.6460 S32: 0.8451 S33: 0.2649
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'A' AND (RESSEQ 2302:2322)
REMARK 3 ORIGIN FOR THE GROUP (A): 13.2323 3.6435 6.8579
REMARK 3 T TENSOR
REMARK 3 T11: 1.5177 T22: 0.9130
REMARK 3 T33: 0.3577 T12: 0.1229
REMARK 3 T13: -0.2036 T23: -0.2350
REMARK 3 L TENSOR
REMARK 3 L11: 0.3101 L22: 1.1644
REMARK 3 L33: 0.2328 L12: 0.1776
REMARK 3 L13: -0.2361 L23: -0.3378
REMARK 3 S TENSOR
REMARK 3 S11: 0.8245 S12: 0.4076 S13: -0.0819
REMARK 3 S21: -0.3720 S22: -0.2140 S23: 0.5597
REMARK 3 S31: 0.6920 S32: -0.0598 S33: 1.0307
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN 'A' AND (RESSEQ 1113:1132)
REMARK 3 ORIGIN FOR THE GROUP (A): 34.9676 -4.6336 57.1305
REMARK 3 T TENSOR
REMARK 3 T11: 0.5724 T22: 0.4609
REMARK 3 T33: 0.4244 T12: 0.0241
REMARK 3 T13: 0.0572 T23: -0.0278
REMARK 3 L TENSOR
REMARK 3 L11: 2.0331 L22: 1.8716
REMARK 3 L33: 2.7395 L12: -0.0088
REMARK 3 L13: -0.1431 L23: -1.2058
REMARK 3 S TENSOR
REMARK 3 S11: -0.3260 S12: -0.2316 S13: 0.0462
REMARK 3 S21: 0.8038 S22: -0.0654 S23: -0.3871
REMARK 3 S31: -0.4753 S32: -0.3354 S33: -0.1117
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 4RLY COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-OCT-14.
REMARK 100 THE DEPOSITION ID IS D_1000087509.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-JUN-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
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) : NULL
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO, HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK, HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 19914
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.500
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 : 9.500
REMARK 200 R MERGE (I) : 0.07700
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.54
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 9.70
REMARK 200 R MERGE FOR SHELL (I) : 0.74800
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: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 69.12
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.98
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.8 M AMMONIUM SULFATE, 6-8% DIOXANE,
REMARK 280 AND 0.1 M MES , PH 6.5, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 289K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 42 2 2
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 -Y,X,Z+1/2
REMARK 290 4555 Y,-X,Z+1/2
REMARK 290 5555 -X,Y,-Z
REMARK 290 6555 X,-Y,-Z
REMARK 290 7555 Y,X,-Z+1/2
REMARK 290 8555 -Y,-X,-Z+1/2
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 53.00400
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 53.00400
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 53.00400
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 53.00400
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2460 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 26500 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -7.0 KCAL/MOL
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 350 BIOMT1 2 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 106.00800
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 S SO4 A2403 LIES ON A SPECIAL POSITION.
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 GLY A 1112
REMARK 465 GLY A 2020
REMARK 465 SER A 2021
REMARK 465 LEU A 2022
REMARK 465 VAL A 2023
REMARK 465 PRO A 2024
REMARK 465 ARG A 2025
REMARK 465 GLY A 2026
REMARK 465 SER A 2027
REMARK 465 LYS A 2028
REMARK 465 GLY A 2189
REMARK 465 LYS A 2190
REMARK 465 VAL A 2191
REMARK 465 ALA A 2218
REMARK 465 ASP A 2219
REMARK 465 VAL A 2220
REMARK 465 GLU A 2323
REMARK 465 GLU A 2324
REMARK 465 VAL A 2325
REMARK 465 THR A 2326
REMARK 465 THR A 2327
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 SER A1113 OG
REMARK 470 ASP A2186 CG OD1 OD2
REMARK 470 LYS A2188 CG CD CE NZ
REMARK 470 ARG A2192 CG CD NE CZ NH1 NH2
REMARK 470 ASN A2217 CG OD1 ND2
REMARK 470 LYS A2223 CG CD CE NZ
REMARK 470 GLU A2231 CG CD OE1 OE2
REMARK 470 ARG A2264 CG CD NE CZ NH1 NH2
REMARK 470 LYS A2319 CG CD CE NZ
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 THR A2059 124.10 -38.99
REMARK 500 ARG A2264 127.07 -31.37
REMARK 500 ARG A2308 -3.74 -51.24
REMARK 500 GLU A2316 -72.08 -43.70
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 2401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 2402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 2403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 2404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 2405
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 2406
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 2407
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4RLV RELATED DB: PDB
DBREF 4RLY A 1114 1132 UNP A9JQD3 A9JQD3_MOUSE 74 92
DBREF 4RLY A 2028 2318 UNP Q01484 ANK2_HUMAN 28 318
SEQADV 4RLY GLY A 1112 UNP A9JQD3 EXPRESSION TAG
SEQADV 4RLY SER A 1113 UNP A9JQD3 EXPRESSION TAG
SEQADV 4RLY GLY A 2020 UNP A9JQD3 LINKER
SEQADV 4RLY SER A 2021 UNP A9JQD3 LINKER
SEQADV 4RLY LEU A 2022 UNP A9JQD3 LINKER
SEQADV 4RLY VAL A 2023 UNP A9JQD3 LINKER
SEQADV 4RLY PRO A 2024 UNP A9JQD3 LINKER
SEQADV 4RLY ARG A 2025 UNP A9JQD3 LINKER
SEQADV 4RLY GLY A 2026 UNP Q01484 LINKER
SEQADV 4RLY SER A 2027 UNP Q01484 LINKER
SEQADV 4RLY LYS A 2319 UNP Q01484 EXPRESSION TAG
SEQADV 4RLY VAL A 2320 UNP Q01484 EXPRESSION TAG
SEQADV 4RLY VAL A 2321 UNP Q01484 EXPRESSION TAG
SEQADV 4RLY THR A 2322 UNP Q01484 EXPRESSION TAG
SEQADV 4RLY GLU A 2323 UNP Q01484 EXPRESSION TAG
SEQADV 4RLY GLU A 2324 UNP Q01484 EXPRESSION TAG
SEQADV 4RLY VAL A 2325 UNP Q01484 EXPRESSION TAG
SEQADV 4RLY THR A 2326 UNP Q01484 EXPRESSION TAG
SEQADV 4RLY THR A 2327 UNP Q01484 EXPRESSION TAG
SEQRES 1 A 329 GLY SER THR VAL THR VAL PRO ILE ALA VAL GLY GLU SER
SEQRES 2 A 329 ASP PHE GLU ASN LEU ASN THR GLU GLY SER LEU VAL PRO
SEQRES 3 A 329 ARG GLY SER LYS SER ASP SER ASN ALA SER PHE LEU ARG
SEQRES 4 A 329 ALA ALA ARG ALA GLY ASN LEU ASP LYS VAL VAL GLU TYR
SEQRES 5 A 329 LEU LYS GLY GLY ILE ASP ILE ASN THR CYS ASN GLN ASN
SEQRES 6 A 329 GLY LEU ASN ALA LEU HIS LEU ALA ALA LYS GLU GLY HIS
SEQRES 7 A 329 VAL GLY LEU VAL GLN GLU LEU LEU GLY ARG GLY SER SER
SEQRES 8 A 329 VAL ASP SER ALA THR LYS LYS GLY ASN THR ALA LEU HIS
SEQRES 9 A 329 ILE ALA SER LEU ALA GLY GLN ALA GLU VAL VAL LYS VAL
SEQRES 10 A 329 LEU VAL LYS GLU GLY ALA ASN ILE ASN ALA GLN SER GLN
SEQRES 11 A 329 ASN GLY PHE THR PRO LEU TYR MET ALA ALA GLN GLU ASN
SEQRES 12 A 329 HIS ILE ASP VAL VAL LYS TYR LEU LEU GLU ASN GLY ALA
SEQRES 13 A 329 ASN GLN SER THR ALA THR GLU ASP GLY PHE THR PRO LEU
SEQRES 14 A 329 ALA VAL ALA LEU GLN GLN GLY HIS ASN GLN ALA VAL ALA
SEQRES 15 A 329 ILE LEU LEU GLU ASN ASP THR LYS GLY LYS VAL ARG LEU
SEQRES 16 A 329 PRO ALA LEU HIS ILE ALA ALA ARG LYS ASP ASP THR LYS
SEQRES 17 A 329 SER ALA ALA LEU LEU LEU GLN ASN ASP HIS ASN ALA ASP
SEQRES 18 A 329 VAL GLN SER LYS MET MET VAL ASN ARG THR THR GLU SER
SEQRES 19 A 329 GLY PHE THR PRO LEU HIS ILE ALA ALA HIS TYR GLY ASN
SEQRES 20 A 329 VAL ASN VAL ALA THR LEU LEU LEU ASN ARG GLY ALA ALA
SEQRES 21 A 329 VAL ASP PHE THR ALA ARG ASN GLY ILE THR PRO LEU HIS
SEQRES 22 A 329 VAL ALA SER LYS ARG GLY ASN THR ASN MET VAL LYS LEU
SEQRES 23 A 329 LEU LEU ASP ARG GLY GLY GLN ILE ASP ALA LYS THR ARG
SEQRES 24 A 329 ASP GLY LEU THR PRO LEU HIS CYS ALA ALA ARG SER GLY
SEQRES 25 A 329 HIS ASP GLN VAL VAL GLU LEU LEU LYS VAL VAL THR GLU
SEQRES 26 A 329 GLU VAL THR THR
HET SO4 A2401 5
HET SO4 A2402 5
HET SO4 A2403 5
HET SO4 A2404 5
HET SO4 A2405 5
HET SO4 A2406 5
HET SO4 A2407 5
HETNAM SO4 SULFATE ION
FORMUL 2 SO4 7(O4 S 2-)
FORMUL 9 HOH *74(H2 O)
HELIX 1 1 ASP A 1125 LEU A 1129 5 5
HELIX 2 2 ASP A 2030 GLY A 2042 1 13
HELIX 3 3 ASN A 2043 GLY A 2053 1 11
HELIX 4 4 ASN A 2066 GLY A 2075 1 10
HELIX 5 5 HIS A 2076 GLY A 2087 1 12
HELIX 6 6 THR A 2099 ALA A 2107 1 9
HELIX 7 7 GLN A 2109 GLU A 2119 1 11
HELIX 8 8 THR A 2132 GLU A 2140 1 9
HELIX 9 9 HIS A 2142 GLU A 2151 1 10
HELIX 10 10 THR A 2165 GLN A 2173 1 9
HELIX 11 11 HIS A 2175 GLU A 2184 1 10
HELIX 12 12 PRO A 2194 ASP A 2203 1 10
HELIX 13 13 ASP A 2204 LEU A 2212 1 9
HELIX 14 14 GLN A 2213 ASP A 2215 5 3
HELIX 15 15 MET A 2224 ARG A 2228 5 5
HELIX 16 16 THR A 2235 GLY A 2244 1 10
HELIX 17 17 ASN A 2245 ARG A 2255 1 11
HELIX 18 18 ALA A 2263 ILE A 2267 5 5
HELIX 19 19 THR A 2268 ARG A 2276 1 9
HELIX 20 20 ASN A 2278 ARG A 2288 1 11
HELIX 21 21 THR A 2301 ARG A 2308 1 8
HELIX 22 22 HIS A 2311 THR A 2322 1 12
SITE 1 AC1 6 ASN A1128 ASN A2141 GLY A2174 ASN A2176
SITE 2 AC1 6 GLN A2177 HOH A2521
SITE 1 AC2 7 VAL A1121 GLY A1122 LYS A2096 ASN A2129
SITE 2 AC2 7 PHE A2131 HOH A2511 HOH A2535
SITE 1 AC3 4 HIS A2076 VAL A2077 GLY A2078 LEU A2079
SITE 1 AC4 6 GLY A2108 GLN A2109 ALA A2110 GLU A2111
SITE 2 AC4 6 HOH A2514 HOH A2574
SITE 1 AC5 5 ASN A2141 HIS A2142 ILE A2143 ASP A2144
SITE 2 AC5 5 HOH A2558
SITE 1 AC6 3 LEU A2251 ASN A2254 GLY A2289
SITE 1 AC7 4 ASN A2278 THR A2279 ASN A2280 MET A2281
CRYST1 102.295 102.295 106.008 90.00 90.00 90.00 P 42 2 2 8
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.009776 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009776 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009433 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
