HEADER PROTEIN BINDING 02-SEP-17 5YAY
TITLE CRYSTAL STRUCTURE OF KANK1/KIF21A COMPLEX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: KN MOTIF AND ANKYRIN REPEAT DOMAINS 1;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 1088-1338;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: KINESIN-LIKE PROTEIN KIF21A;
COMPND 8 CHAIN: B;
COMPND 9 FRAGMENT: UNP RESIDUES 1142-1169;
COMPND 10 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: MOUSE;
SOURCE 4 ORGANISM_TAXID: 10090;
SOURCE 5 GENE: KANK1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(C PLUS);
SOURCE 9 MOL_ID: 2;
SOURCE 10 SYNTHETIC: YES;
SOURCE 11 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 12 ORGANISM_COMMON: MOUSE;
SOURCE 13 ORGANISM_TAXID: 10090
KEYWDS SCAFFOLD PROTEIN, ANK REPEAT, PROTEIN BINDING
EXPDTA X-RAY DIFFRACTION
AUTHOR Z.WEI,W.PAN
REVDAT 4 22-NOV-23 5YAY 1 REMARK
REVDAT 3 07-MAR-18 5YAY 1 JRNL
REVDAT 2 27-DEC-17 5YAY 1 JRNL
REVDAT 1 20-DEC-17 5YAY 0
JRNL AUTH W.PAN,K.SUN,K.TANG,Q.XIAO,C.MA,C.YU,Z.WEI
JRNL TITL STRUCTURAL INSIGHTS INTO ANKYRIN REPEAT-MEDIATED RECOGNITION
JRNL TITL 2 OF THE KINESIN MOTOR PROTEIN KIF21A BY KANK1, A SCAFFOLD
JRNL TITL 3 PROTEIN IN FOCAL ADHESION.
JRNL REF J. BIOL. CHEM. V. 293 1944 2018
JRNL REFN ESSN 1083-351X
JRNL PMID 29217769
JRNL DOI 10.1074/JBC.M117.815779
REMARK 2
REMARK 2 RESOLUTION. 1.55 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.8.4_1496
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) : 1.55
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 28.48
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.2
REMARK 3 NUMBER OF REFLECTIONS : 39518
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.184
REMARK 3 R VALUE (WORKING SET) : 0.183
REMARK 3 FREE R VALUE : 0.200
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1976
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 28.4888 - 3.7327 0.85 2489 131 0.1788 0.1816
REMARK 3 2 3.7327 - 2.9637 0.97 2712 143 0.1745 0.1931
REMARK 3 3 2.9637 - 2.5894 0.98 2713 142 0.1880 0.2025
REMARK 3 4 2.5894 - 2.3528 0.99 2694 143 0.1812 0.2055
REMARK 3 5 2.3528 - 2.1842 0.99 2729 143 0.1795 0.1960
REMARK 3 6 2.1842 - 2.0555 1.00 2698 142 0.1688 0.1884
REMARK 3 7 2.0555 - 1.9525 1.00 2693 142 0.1792 0.2030
REMARK 3 8 1.9525 - 1.8676 1.00 2714 143 0.1877 0.2118
REMARK 3 9 1.8676 - 1.7957 1.00 2666 140 0.1946 0.2009
REMARK 3 10 1.7957 - 1.7337 1.00 2693 141 0.1933 0.2107
REMARK 3 11 1.7337 - 1.6795 1.00 2701 143 0.2052 0.2258
REMARK 3 12 1.6795 - 1.6315 1.00 2688 142 0.2133 0.2744
REMARK 3 13 1.6315 - 1.5886 1.00 2661 140 0.2296 0.2506
REMARK 3 14 1.5886 - 1.5498 0.99 2691 141 0.2458 0.2979
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.140
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 19.640
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 22.36
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 35.42
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 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 : 0.012 2022
REMARK 3 ANGLE : 1.353 2742
REMARK 3 CHIRALITY : 0.060 321
REMARK 3 PLANARITY : 0.006 357
REMARK 3 DIHEDRAL : 13.481 748
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 9
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 1090 THROUGH 1107 )
REMARK 3 ORIGIN FOR THE GROUP (A): -2.0133 1.4637 59.7579
REMARK 3 T TENSOR
REMARK 3 T11: 0.7803 T22: 0.4808
REMARK 3 T33: 0.2586 T12: 0.1512
REMARK 3 T13: 0.0389 T23: -0.0473
REMARK 3 L TENSOR
REMARK 3 L11: 5.0489 L22: 5.0904
REMARK 3 L33: 4.5822 L12: 2.0032
REMARK 3 L13: 0.6431 L23: 0.5131
REMARK 3 S TENSOR
REMARK 3 S11: -0.3320 S12: -0.8767 S13: 0.1909
REMARK 3 S21: 1.2242 S22: 0.2827 S23: 0.2312
REMARK 3 S31: -0.6551 S32: -0.6273 S33: 0.0334
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 1108 THROUGH 1134 )
REMARK 3 ORIGIN FOR THE GROUP (A): 8.2468 -0.1132 55.8785
REMARK 3 T TENSOR
REMARK 3 T11: 0.6021 T22: 0.3674
REMARK 3 T33: 0.3099 T12: -0.0142
REMARK 3 T13: -0.1020 T23: -0.0371
REMARK 3 L TENSOR
REMARK 3 L11: 0.5929 L22: 0.5418
REMARK 3 L33: 0.7285 L12: -0.5747
REMARK 3 L13: -0.3727 L23: -0.1976
REMARK 3 S TENSOR
REMARK 3 S11: 0.0311 S12: -0.3848 S13: 0.3478
REMARK 3 S21: 0.7235 S22: -0.1331 S23: -0.2404
REMARK 3 S31: -0.1437 S32: 0.3708 S33: 0.1750
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 1135 THROUGH 1172 )
REMARK 3 ORIGIN FOR THE GROUP (A): -0.5439 0.3122 48.1089
REMARK 3 T TENSOR
REMARK 3 T11: 0.3448 T22: 0.1888
REMARK 3 T33: 0.1803 T12: 0.0718
REMARK 3 T13: -0.0272 T23: 0.0051
REMARK 3 L TENSOR
REMARK 3 L11: 3.4753 L22: 2.5662
REMARK 3 L33: 3.7562 L12: 0.5270
REMARK 3 L13: -0.2249 L23: 0.1378
REMARK 3 S TENSOR
REMARK 3 S11: -0.1807 S12: -0.3564 S13: 0.3241
REMARK 3 S21: 0.6108 S22: 0.1449 S23: 0.1459
REMARK 3 S31: -0.3374 S32: -0.1164 S33: 0.0290
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 1173 THROUGH 1206 )
REMARK 3 ORIGIN FOR THE GROUP (A): 2.0987 -0.1631 37.7063
REMARK 3 T TENSOR
REMARK 3 T11: 0.1819 T22: 0.1380
REMARK 3 T33: 0.1547 T12: 0.0185
REMARK 3 T13: -0.0320 T23: 0.0339
REMARK 3 L TENSOR
REMARK 3 L11: 3.5300 L22: 3.6286
REMARK 3 L33: 3.6859 L12: -0.7148
REMARK 3 L13: -0.9096 L23: 0.1694
REMARK 3 S TENSOR
REMARK 3 S11: -0.0175 S12: -0.0687 S13: 0.2482
REMARK 3 S21: 0.3226 S22: 0.0714 S23: -0.1521
REMARK 3 S31: -0.3655 S32: -0.0468 S33: -0.0623
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 1207 THROUGH 1231 )
REMARK 3 ORIGIN FOR THE GROUP (A): -2.8298 0.2063 28.7897
REMARK 3 T TENSOR
REMARK 3 T11: 0.1177 T22: 0.2451
REMARK 3 T33: 0.2065 T12: 0.0072
REMARK 3 T13: -0.0049 T23: 0.0466
REMARK 3 L TENSOR
REMARK 3 L11: 6.3887 L22: 6.2563
REMARK 3 L33: 4.4184 L12: -0.7428
REMARK 3 L13: -0.7883 L23: -0.2220
REMARK 3 S TENSOR
REMARK 3 S11: 0.0703 S12: 0.4438 S13: 0.0809
REMARK 3 S21: -0.1804 S22: 0.1041 S23: 0.7310
REMARK 3 S31: -0.1319 S32: -0.7099 S33: -0.1353
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 1232 THROUGH 1321 )
REMARK 3 ORIGIN FOR THE GROUP (A): 10.4547 -0.0660 15.5480
REMARK 3 T TENSOR
REMARK 3 T11: 0.2384 T22: 0.2276
REMARK 3 T33: 0.2315 T12: 0.0502
REMARK 3 T13: 0.0913 T23: 0.0404
REMARK 3 L TENSOR
REMARK 3 L11: 2.1276 L22: 4.4843
REMARK 3 L33: 4.6077 L12: 0.5299
REMARK 3 L13: -0.5283 L23: -1.2643
REMARK 3 S TENSOR
REMARK 3 S11: -0.0544 S12: 0.2700 S13: -0.0705
REMARK 3 S21: -0.7376 S22: -0.1620 S23: -0.6047
REMARK 3 S31: 0.3450 S32: 0.3667 S33: 0.1705
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 1322 THROUGH 1333 )
REMARK 3 ORIGIN FOR THE GROUP (A): 9.6476 -0.0135 0.4063
REMARK 3 T TENSOR
REMARK 3 T11: 0.9393 T22: 0.3986
REMARK 3 T33: 0.3094 T12: 0.0128
REMARK 3 T13: 0.1917 T23: 0.0180
REMARK 3 L TENSOR
REMARK 3 L11: 3.3300 L22: 3.9005
REMARK 3 L33: 5.5371 L12: 0.5284
REMARK 3 L13: -1.6232 L23: -2.2517
REMARK 3 S TENSOR
REMARK 3 S11: -0.2232 S12: 0.0523 S13: 0.1114
REMARK 3 S21: -0.3601 S22: 0.2521 S23: 0.8236
REMARK 3 S31: 0.0960 S32: 0.1264 S33: 0.1114
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 1154 THROUGH 1161 )
REMARK 3 ORIGIN FOR THE GROUP (A): 15.5144 -9.5380 19.8682
REMARK 3 T TENSOR
REMARK 3 T11: 0.4512 T22: 0.4899
REMARK 3 T33: 0.4936 T12: 0.0526
REMARK 3 T13: 0.2103 T23: 0.0270
REMARK 3 L TENSOR
REMARK 3 L11: 6.8943 L22: 3.0394
REMARK 3 L33: 2.0557 L12: 4.5372
REMARK 3 L13: -8.2544 L23: -5.6306
REMARK 3 S TENSOR
REMARK 3 S11: -0.2545 S12: 0.5735 S13: -0.5952
REMARK 3 S21: -1.0967 S22: -0.4500 S23: -1.2490
REMARK 3 S31: 0.6289 S32: 0.4412 S33: 0.5704
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 1162 THROUGH 1168 )
REMARK 3 ORIGIN FOR THE GROUP (A): 9.3450 -11.0657 33.6898
REMARK 3 T TENSOR
REMARK 3 T11: 0.2459 T22: 0.2035
REMARK 3 T33: 0.2915 T12: 0.0412
REMARK 3 T13: 0.0156 T23: -0.0219
REMARK 3 L TENSOR
REMARK 3 L11: 2.0554 L22: 7.7692
REMARK 3 L33: 9.1172 L12: 1.6420
REMARK 3 L13: -0.6223 L23: -1.7460
REMARK 3 S TENSOR
REMARK 3 S11: -0.1569 S12: 0.3333 S13: -0.4946
REMARK 3 S21: 0.3396 S22: 0.2886 S23: -0.6397
REMARK 3 S31: 0.6341 S32: -0.0139 S33: -0.1512
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 5YAY COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 04-SEP-17.
REMARK 100 THE DEPOSITION ID IS D_1300004965.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 02-APR-16
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 : SSRF
REMARK 200 BEAMLINE : BL17U1
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 : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 39577
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.550
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 (%) : 98.2
REMARK 200 DATA REDUNDANCY : 5.400
REMARK 200 R MERGE (I) : 0.05700
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 15.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.55
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.58
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 5.50
REMARK 200 R MERGE FOR SHELL (I) : 0.83500
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: 4HBD
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 43.42
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.17
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M AMMONIUM FORMATE AND 20% W/V
REMARK 280 POLYETHYLENE GLYCOL 3350, VAPOR DIFFUSION, SITTING 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 19.02150
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 68.04750
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 26.04000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 68.04750
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 19.02150
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 26.04000
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1740 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 12210 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -5.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
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 GLY A 1082
REMARK 465 PRO A 1083
REMARK 465 GLY A 1084
REMARK 465 SER A 1085
REMARK 465 GLU A 1086
REMARK 465 PHE A 1087
REMARK 465 ARG A 1088
REMARK 465 GLU A 1089
REMARK 465 PHE A 1334
REMARK 465 SER A 1335
REMARK 465 LYS A 1336
REMARK 465 ALA A 1337
REMARK 465 GLN A 1338
REMARK 465 LEU B 1142
REMARK 465 MET B 1143
REMARK 465 LYS B 1144
REMARK 465 LEU B 1145
REMARK 465 CYS B 1146
REMARK 465 GLY B 1147
REMARK 465 GLU B 1148
REMARK 465 VAL B 1149
REMARK 465 LYS B 1150
REMARK 465 PRO B 1151
REMARK 465 LYS B 1152
REMARK 465 ASN B 1153
REMARK 465 ASP B 1169
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 A1155 142.11 -175.91
REMARK 500 HIS A1321 68.87 -119.45
REMARK 500
REMARK 500 REMARK: NULL
DBREF 5YAY A 1088 1338 UNP E9Q238 E9Q238_MOUSE 1088 1338
DBREF 5YAY B 1142 1169 UNP Q9QXL2 KI21A_MOUSE 1142 1169
SEQADV 5YAY GLY A 1082 UNP E9Q238 EXPRESSION TAG
SEQADV 5YAY PRO A 1083 UNP E9Q238 EXPRESSION TAG
SEQADV 5YAY GLY A 1084 UNP E9Q238 EXPRESSION TAG
SEQADV 5YAY SER A 1085 UNP E9Q238 EXPRESSION TAG
SEQADV 5YAY GLU A 1086 UNP E9Q238 EXPRESSION TAG
SEQADV 5YAY PHE A 1087 UNP E9Q238 EXPRESSION TAG
SEQRES 1 A 257 GLY PRO GLY SER GLU PHE ARG GLU ARG TYR GLU LEU SER
SEQRES 2 A 257 GLU LYS MET LEU SER ALA CYS ASN LEU LEU LYS TYR ASN
SEQRES 3 A 257 ILE LYS ASP PRO LYS ALA LEU ALA SER LYS ASP MET ARG
SEQRES 4 A 257 ILE CYS LEU ASN THR LEU GLN HIS ASP TRP PHE ARG VAL
SEQRES 5 A 257 SER SER GLN LYS SER ALA VAL PRO ALA MET VAL GLY ASP
SEQRES 6 A 257 TYR ILE ALA ALA PHE GLU ALA VAL SER PRO ASP VAL LEU
SEQRES 7 A 257 ARG TYR ILE ILE ASN MET ALA ASP GLY ASN GLY ASN THR
SEQRES 8 A 257 ALA LEU HIS TYR SER VAL SER HIS SER ASN PHE GLN ILE
SEQRES 9 A 257 VAL LYS LEU LEU LEU ASP ALA ASP VAL CYS ASN VAL ASP
SEQRES 10 A 257 HIS GLN ASN LYS ALA GLY TYR THR PRO ILE MET LEU ALA
SEQRES 11 A 257 ALA LEU ALA ALA VAL GLU ALA GLU LYS ASP MET GLN VAL
SEQRES 12 A 257 VAL GLU GLU LEU PHE SER CYS GLY ASP VAL ASN ALA LYS
SEQRES 13 A 257 ALA SER GLN ALA GLY GLN THR ALA LEU MET LEU ALA VAL
SEQRES 14 A 257 SER HIS GLY ARG ILE ASP MET VAL LYS GLY LEU LEU ALA
SEQRES 15 A 257 CYS GLY ALA ASP VAL ASN ILE GLN ASP ASP GLU GLY SER
SEQRES 16 A 257 THR ALA LEU MET CYS ALA SER GLU HIS GLY HIS VAL GLU
SEQRES 17 A 257 ILE VAL LYS LEU LEU LEU ALA GLN PRO GLY CYS ASN GLY
SEQRES 18 A 257 HIS LEU GLU ASP ASN ASP GLY SER THR ALA LEU SER ILE
SEQRES 19 A 257 ALA LEU GLU ALA GLY HIS LYS ASP ILE ALA VAL LEU LEU
SEQRES 20 A 257 TYR ALA HIS LEU ASN PHE SER LYS ALA GLN
SEQRES 1 B 28 LEU MET LYS LEU CYS GLY GLU VAL LYS PRO LYS ASN LYS
SEQRES 2 B 28 ALA ARG ARG ARG THR THR THR GLN MET GLU LEU LEU TYR
SEQRES 3 B 28 ALA ASP
FORMUL 3 HOH *121(H2 O)
HELIX 1 AA1 SER A 1094 ILE A 1108 1 15
HELIX 2 AA2 ASP A 1110 ALA A 1115 1 6
HELIX 3 AA3 SER A 1116 SER A 1135 1 20
HELIX 4 AA4 VAL A 1140 SER A 1155 1 16
HELIX 5 AA5 SER A 1155 ASN A 1164 1 10
HELIX 6 AA6 THR A 1172 HIS A 1180 1 9
HELIX 7 AA7 ASN A 1182 ALA A 1192 1 11
HELIX 8 AA8 THR A 1206 ALA A 1214 1 9
HELIX 9 AA9 ALA A 1218 GLY A 1232 1 15
HELIX 10 AB1 THR A 1244 HIS A 1252 1 9
HELIX 11 AB2 ARG A 1254 CYS A 1264 1 11
HELIX 12 AB3 THR A 1277 GLY A 1286 1 10
HELIX 13 AB4 HIS A 1287 ALA A 1296 1 10
HELIX 14 AB5 THR A 1311 ALA A 1319 1 9
HELIX 15 AB6 HIS A 1321 ASN A 1333 1 13
HELIX 16 AB7 LYS B 1154 ARG B 1158 5 5
HELIX 17 AB8 THR B 1161 TYR B 1167 1 7
CRYST1 38.043 52.080 136.095 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 0.026286 0.000000 0.000000 0.00000
SCALE2 0.000000 0.019201 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007348 0.00000
(ATOM LINES ARE NOT SHOWN.)
END