HEADER DE NOVO PROTEIN 01-DEC-17 6F5E
TITLE CRYSTAL STRUCTURE OF DARPIN-DARPIN RIGID FUSION, VARIANT DD_D12_10_47
TITLE 2 IN COMPLEX JNK1A1 AND JIP1 PEPTIDE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DD_D12_10_47;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: MITOGEN-ACTIVATED PROTEIN KINASE 8;
COMPND 7 CHAIN: B;
COMPND 8 SYNONYM: MAPK 8,JNK-46,STRESS-ACTIVATED PROTEIN KINASE 1C,SAPK1C,
COMPND 9 STRESS-ACTIVATED PROTEIN KINASE JNK1,C-JUN N-TERMINAL KINASE 1;
COMPND 10 EC: 2.7.11.24;
COMPND 11 ENGINEERED: YES;
COMPND 12 MOL_ID: 3;
COMPND 13 MOLECULE: C-JUN-AMINO-TERMINAL KINASE-INTERACTING PROTEIN 1;
COMPND 14 CHAIN: C;
COMPND 15 SYNONYM: JNK-INTERACTING PROTEIN 1,ISLET-BRAIN-1,IB-1,JNK MAP KINASE
COMPND 16 SCAFFOLD PROTEIN 1,MITOGEN-ACTIVATED PROTEIN KINASE 8-INTERACTING
COMPND 17 PROTEIN 1;
COMPND 18 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;
SOURCE 3 ORGANISM_TAXID: 32630;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI K-12;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 83333;
SOURCE 6 EXPRESSION_SYSTEM_VARIANT: XL1-BLUE;
SOURCE 7 MOL_ID: 2;
SOURCE 8 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 9 ORGANISM_COMMON: HUMAN;
SOURCE 10 ORGANISM_TAXID: 9606;
SOURCE 11 GENE: MAPK8, JNK1, PRKM8, SAPK1, SAPK1C;
SOURCE 12 EXPRESSION_SYSTEM: ESCHERICHIA COLI K-12;
SOURCE 13 EXPRESSION_SYSTEM_TAXID: 83333;
SOURCE 14 EXPRESSION_SYSTEM_VARIANT: XL1-BLUE;
SOURCE 15 MOL_ID: 3;
SOURCE 16 SYNTHETIC: YES;
SOURCE 17 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 18 ORGANISM_COMMON: MOUSE;
SOURCE 19 ORGANISM_TAXID: 10090
KEYWDS X-RAY CRYSTALLOGRAPHY; DESIGNED ANKYRIN REPEAT PROTEINS; PROTEIN
KEYWDS 2 DESIGN; PROTEIN ENGINEERING; RIGID DOMAIN FUSIONS, TRANSFERASE, DE
KEYWDS 3 NOVO PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.WU,P.R.MITTL,A.HONEGGER,A.BATYUK,A.PLUECKTHUN
REVDAT 2 08-MAY-24 6F5E 1 REMARK
REVDAT 1 13-DEC-17 6F5E 0
SPRSDE 13-DEC-17 6F5E 5LEN
JRNL AUTH Y.WU,P.R.MITTL,A.HONEGGER,A.BATYUK,A.PLUECKTHUN
JRNL TITL CRYSTAL STRUCTURE OF DARPIN-DARPIN RIGID FUSION, VARIANT
JRNL TITL 2 DD_D12_10_47 IN COMPLEX JNK1A1 AND JIP1 PEPTIDE
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.12_2829: ???)
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) : 2.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 46.96
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 30221
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.202
REMARK 3 R VALUE (WORKING SET) : 0.201
REMARK 3 FREE R VALUE : 0.226
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.060
REMARK 3 FREE R VALUE TEST SET COUNT : 1528
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 46.9665 - 6.0011 1.00 2608 157 0.1602 0.1728
REMARK 3 2 6.0011 - 4.7647 1.00 2622 129 0.1917 0.2114
REMARK 3 3 4.7647 - 4.1629 1.00 2629 136 0.1750 0.2056
REMARK 3 4 4.1629 - 3.7824 1.00 2620 145 0.1968 0.2434
REMARK 3 5 3.7824 - 3.5114 1.00 2569 128 0.2304 0.2590
REMARK 3 6 3.5114 - 3.3044 1.00 2635 160 0.2436 0.3192
REMARK 3 7 3.3044 - 3.1390 0.99 2601 133 0.2587 0.2672
REMARK 3 8 3.1390 - 3.0024 0.99 2579 150 0.2976 0.3898
REMARK 3 9 3.0024 - 2.8868 0.99 2624 123 0.3439 0.3496
REMARK 3 10 2.8868 - 2.7872 1.00 2599 125 0.3525 0.4086
REMARK 3 11 2.7872 - 2.7001 0.99 2607 142 0.3747 0.4116
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) : 0.500
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 32.480
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
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 : 0.002 5385
REMARK 3 ANGLE : 0.463 7298
REMARK 3 CHIRALITY : 0.037 831
REMARK 3 PLANARITY : 0.002 940
REMARK 3 DIHEDRAL : 11.973 3252
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 6
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 11 THROUGH 180 )
REMARK 3 ORIGIN FOR THE GROUP (A): 90.8249 54.8275 66.1711
REMARK 3 T TENSOR
REMARK 3 T11: 0.8800 T22: 1.6965
REMARK 3 T33: 1.2623 T12: 0.3135
REMARK 3 T13: -0.0646 T23: 0.0809
REMARK 3 L TENSOR
REMARK 3 L11: 3.2956 L22: 2.5084
REMARK 3 L33: 5.4356 L12: 1.0924
REMARK 3 L13: -1.0847 L23: -0.8069
REMARK 3 S TENSOR
REMARK 3 S11: -0.2432 S12: -0.5249 S13: -0.1532
REMARK 3 S21: 0.1041 S22: 0.1242 S23: 0.4673
REMARK 3 S31: 0.0421 S32: -0.9025 S33: 0.0644
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 181 THROUGH 325 )
REMARK 3 ORIGIN FOR THE GROUP (A): 92.6240 53.8949 27.3860
REMARK 3 T TENSOR
REMARK 3 T11: 0.7129 T22: 1.8993
REMARK 3 T33: 1.1221 T12: -0.1609
REMARK 3 T13: 0.0017 T23: 0.0244
REMARK 3 L TENSOR
REMARK 3 L11: 3.5176 L22: 2.7825
REMARK 3 L33: 6.9245 L12: 0.5530
REMARK 3 L13: 2.5615 L23: 1.3758
REMARK 3 S TENSOR
REMARK 3 S11: -0.3993 S12: 1.4144 S13: -0.0976
REMARK 3 S21: -0.2429 S22: 0.4756 S23: -0.0435
REMARK 3 S31: 0.1623 S32: 0.2082 S33: -0.0652
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 7 THROUGH 164 )
REMARK 3 ORIGIN FOR THE GROUP (A): 56.2847 65.6347 9.1709
REMARK 3 T TENSOR
REMARK 3 T11: 0.9015 T22: 1.3194
REMARK 3 T33: 1.1171 T12: -0.4961
REMARK 3 T13: -0.0430 T23: 0.1745
REMARK 3 L TENSOR
REMARK 3 L11: 1.4789 L22: 2.2937
REMARK 3 L33: 5.2998 L12: -0.3031
REMARK 3 L13: 2.0693 L23: 0.7034
REMARK 3 S TENSOR
REMARK 3 S11: -0.1313 S12: 0.6642 S13: 0.3635
REMARK 3 S21: -0.8010 S22: 0.1381 S23: 0.0517
REMARK 3 S31: -0.7628 S32: 1.0748 S33: -0.0439
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 165 THROUGH 335 )
REMARK 3 ORIGIN FOR THE GROUP (A): 65.2545 65.3300 33.7727
REMARK 3 T TENSOR
REMARK 3 T11: 0.8486 T22: 1.1844
REMARK 3 T33: 0.9505 T12: -0.3802
REMARK 3 T13: -0.0221 T23: -0.0021
REMARK 3 L TENSOR
REMARK 3 L11: 4.9940 L22: 1.3733
REMARK 3 L33: 3.0546 L12: -1.1744
REMARK 3 L13: 0.9244 L23: -0.8861
REMARK 3 S TENSOR
REMARK 3 S11: -0.3383 S12: -0.2889 S13: 0.2854
REMARK 3 S21: 0.1655 S22: 0.2024 S23: -0.1538
REMARK 3 S31: -0.2691 S32: 0.4163 S33: 0.1309
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 336 THROUGH 362 )
REMARK 3 ORIGIN FOR THE GROUP (A): 62.2051 47.2164 3.8551
REMARK 3 T TENSOR
REMARK 3 T11: 1.1652 T22: 1.4724
REMARK 3 T33: 1.3742 T12: -0.2663
REMARK 3 T13: -0.0662 T23: -0.0915
REMARK 3 L TENSOR
REMARK 3 L11: 9.4131 L22: 3.6822
REMARK 3 L33: 6.6848 L12: -2.4928
REMARK 3 L13: -3.9648 L23: 2.5503
REMARK 3 S TENSOR
REMARK 3 S11: -0.4419 S12: 1.0992 S13: -0.7465
REMARK 3 S21: -0.7660 S22: -0.1353 S23: -0.3177
REMARK 3 S31: 1.3075 S32: 0.2595 S33: 0.3315
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 154 THROUGH 163 )
REMARK 3 ORIGIN FOR THE GROUP (A): 46.4013 78.6597 24.6974
REMARK 3 T TENSOR
REMARK 3 T11: 1.0936 T22: 1.4169
REMARK 3 T33: 1.4596 T12: -0.0627
REMARK 3 T13: -0.2039 T23: -0.0477
REMARK 3 L TENSOR
REMARK 3 L11: 1.3973 L22: 9.6878
REMARK 3 L33: 9.9817 L12: -1.9193
REMARK 3 L13: -1.2196 L23: -6.2570
REMARK 3 S TENSOR
REMARK 3 S11: 0.3018 S12: 0.1873 S13: 0.7039
REMARK 3 S21: -0.0393 S22: 0.1108 S23: 0.8142
REMARK 3 S31: -0.7991 S32: 0.8124 S33: -0.4271
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 6F5E COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 01-DEC-17.
REMARK 100 THE DEPOSITION ID IS D_1200007772.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 05-SEP-14
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.8
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SLS
REMARK 200 BEAMLINE : X06SA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 30294
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.700
REMARK 200 RESOLUTION RANGE LOW (A) : 46.959
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 41.10
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 22.9900
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.77
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.100
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 (%): 65.40
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.55
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 10000 3% W/V HEPES 0.1 M, PH 6.8
REMARK 280 ADDITIVES (0.033% W/V) 1,5-NAPHTHALENE- DISULFONIC ACID DISODIUM
REMARK 280 SALT 2,5-PYRIDINEDICARBOXYLIC ACID 3,5-DINITROSALICYLIC ACID,
REMARK 280 VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 65
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+1/6
REMARK 290 6555 X-Y,X,Z+5/6
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 220.48333
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 110.24167
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 165.36250
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 55.12083
REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 275.60417
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3510 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 30460 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -16.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C
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 1
REMARK 465 ARG A 2
REMARK 465 GLY A 3
REMARK 465 SER A 4
REMARK 465 HIS A 5
REMARK 465 HIS A 6
REMARK 465 HIS A 7
REMARK 465 HIS A 8
REMARK 465 HIS A 9
REMARK 465 HIS A 10
REMARK 465 MET B -9
REMARK 465 ARG B -8
REMARK 465 GLY B -7
REMARK 465 SER B -6
REMARK 465 HIS B -5
REMARK 465 HIS B -4
REMARK 465 HIS B -3
REMARK 465 HIS B -2
REMARK 465 HIS B -1
REMARK 465 HIS B 0
REMARK 465 GLY B 1
REMARK 465 SER B 2
REMARK 465 ARG B 3
REMARK 465 SER B 4
REMARK 465 LYS B 5
REMARK 465 ARG B 6
REMARK 465 GLY B 33
REMARK 465 SER B 34
REMARK 465 GLY B 35
REMARK 465 ALA B 36
REMARK 465 GLN B 37
REMARK 465 GLY B 38
REMARK 465 MET B 182
REMARK 465 THR B 183
REMARK 465 PRO B 184
REMARK 465 TYR B 185
REMARK 465 LEU B 363
REMARK 465 ARG C 153
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 PHE B 225 HE22 GLN B 233 1.60
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 ASP A 77 -166.88 -123.19
REMARK 500 ALA A 180 34.46 -158.13
REMARK 500 ASN A 230 41.60 -108.60
REMARK 500 ASN B 9 32.23 -87.52
REMARK 500 ASN B 28 71.15 59.20
REMARK 500 GLN B 102 -64.83 -141.20
REMARK 500 ASP B 151 42.37 -157.58
REMARK 500 SER B 179 -71.56 -72.34
REMARK 500 LYS B 203 -169.89 -116.75
REMARK 500 ASP B 283 57.94 -150.51
REMARK 500 SER B 284 161.03 176.89
REMARK 500 GLU B 344 38.35 -83.50
REMARK 500 LEU C 160 106.01 -161.80
REMARK 500
REMARK 500 REMARK: NULL
DBREF 6F5E A 1 325 PDB 6F5E 6F5E 1 325
DBREF 6F5E B 2 363 UNP P45983 MK08_HUMAN 2 363
DBREF 6F5E C 153 163 UNP Q9WVI9 JIP1_MOUSE 153 163
SEQADV 6F5E MET B -9 UNP P45983 INITIATING METHIONINE
SEQADV 6F5E ARG B -8 UNP P45983 EXPRESSION TAG
SEQADV 6F5E GLY B -7 UNP P45983 EXPRESSION TAG
SEQADV 6F5E SER B -6 UNP P45983 EXPRESSION TAG
SEQADV 6F5E HIS B -5 UNP P45983 EXPRESSION TAG
SEQADV 6F5E HIS B -4 UNP P45983 EXPRESSION TAG
SEQADV 6F5E HIS B -3 UNP P45983 EXPRESSION TAG
SEQADV 6F5E HIS B -2 UNP P45983 EXPRESSION TAG
SEQADV 6F5E HIS B -1 UNP P45983 EXPRESSION TAG
SEQADV 6F5E HIS B 0 UNP P45983 EXPRESSION TAG
SEQADV 6F5E GLY B 1 UNP P45983 EXPRESSION TAG
SEQRES 1 A 325 MET ARG GLY SER HIS HIS HIS HIS HIS HIS GLY SER ASP
SEQRES 2 A 325 LEU GLY LYS LYS LEU LEU GLU ALA ALA ARG ALA GLY GLN
SEQRES 3 A 325 ASP ASP GLU VAL ARG ILE LEU LEU ALA ASN GLY ALA ASP
SEQRES 4 A 325 VAL ASN THR ALA ASP GLU THR GLY PHE THR PRO LEU HIS
SEQRES 5 A 325 LEU ALA ALA TRP GLU GLY HIS LEU GLY ILE VAL GLU VAL
SEQRES 6 A 325 LEU LEU LYS ASN GLY ALA ASP VAL ASN ALA ASN ASP GLU
SEQRES 7 A 325 ARG GLY HIS THR PRO LEU HIS LEU ALA ALA TYR THR GLY
SEQRES 8 A 325 HIS LEU GLU ILE VAL GLU VAL LEU LEU LYS ASN GLY ALA
SEQRES 9 A 325 GLY VAL ASN ALA THR ASP VAL ILE GLY THR ALA PRO LEU
SEQRES 10 A 325 HIS LEU ALA ALA MET TRP GLY HIS LEU GLU ILE VAL GLU
SEQRES 11 A 325 VAL LEU LEU LYS ASN GLY ALA ASP VAL ASN ALA GLN ASP
SEQRES 12 A 325 LYS PHE GLY LYS THR PRO TYR ASP LEU ALA THR ASP ASN
SEQRES 13 A 325 GLY ASN GLN TRP ILE ALA GLU LEU LEU LYS ARG ALA ALA
SEQRES 14 A 325 LEU ARG ARG LYS LEU LEU GLU ALA ALA ARG ALA GLY HIS
SEQRES 15 A 325 ARG ASP GLU VAL GLU ASP LEU ILE LYS ASN GLY ALA ASP
SEQRES 16 A 325 VAL ASN ALA ILE ASP ALA MET GLY LEU THR PRO LEU HIS
SEQRES 17 A 325 LEU ALA ALA MET ARG GLY HIS LEU GLU ILE VAL GLU VAL
SEQRES 18 A 325 LEU LEU LYS TYR GLY ALA ASP VAL ASN ALA GLU ASP TYR
SEQRES 19 A 325 TYR GLY THR THR PRO LEU ARG LEU ALA ALA TYR ILE GLY
SEQRES 20 A 325 HIS LEU GLU ILE VAL GLU VAL LEU LEU LYS TYR GLY ALA
SEQRES 21 A 325 ASP VAL ASN ALA TYR ASP ILE SER GLY THR THR PRO LEU
SEQRES 22 A 325 HIS LEU ALA ALA VAL LEU GLY HIS LEU GLU ILE VAL GLU
SEQRES 23 A 325 VAL LEU LEU LYS TYR GLY ALA ASP VAL ASN ALA GLN ASP
SEQRES 24 A 325 LYS PHE GLY LYS THR ALA PHE ASP ILE SER ILE ASP ASN
SEQRES 25 A 325 GLY ASN GLU ASP LEU ALA GLU ILE LEU GLN LYS LEU ASN
SEQRES 1 B 373 MET ARG GLY SER HIS HIS HIS HIS HIS HIS GLY SER ARG
SEQRES 2 B 373 SER LYS ARG ASP ASN ASN PHE TYR SER VAL GLU ILE GLY
SEQRES 3 B 373 ASP SER THR PHE THR VAL LEU LYS ARG TYR GLN ASN LEU
SEQRES 4 B 373 LYS PRO ILE GLY SER GLY ALA GLN GLY ILE VAL CYS ALA
SEQRES 5 B 373 ALA TYR ASP ALA ILE LEU GLU ARG ASN VAL ALA ILE LYS
SEQRES 6 B 373 LYS LEU SER ARG PRO PHE GLN ASN GLN THR HIS ALA LYS
SEQRES 7 B 373 ARG ALA TYR ARG GLU LEU VAL LEU MET LYS CYS VAL ASN
SEQRES 8 B 373 HIS LYS ASN ILE ILE GLY LEU LEU ASN VAL PHE THR PRO
SEQRES 9 B 373 GLN LYS SER LEU GLU GLU PHE GLN ASP VAL TYR ILE VAL
SEQRES 10 B 373 MET GLU LEU MET ASP ALA ASN LEU CYS GLN VAL ILE GLN
SEQRES 11 B 373 MET GLU LEU ASP HIS GLU ARG MET SER TYR LEU LEU TYR
SEQRES 12 B 373 GLN MET LEU CYS GLY ILE LYS HIS LEU HIS SER ALA GLY
SEQRES 13 B 373 ILE ILE HIS ARG ASP LEU LYS PRO SER ASN ILE VAL VAL
SEQRES 14 B 373 LYS SER ASP CYS THR LEU LYS ILE LEU ASP PHE GLY LEU
SEQRES 15 B 373 ALA ARG THR ALA GLY THR SER PHE MET MET THR PRO TYR
SEQRES 16 B 373 VAL VAL THR ARG TYR TYR ARG ALA PRO GLU VAL ILE LEU
SEQRES 17 B 373 GLY MET GLY TYR LYS GLU ASN VAL ASP LEU TRP SER VAL
SEQRES 18 B 373 GLY CYS ILE MET GLY GLU MET VAL CYS HIS LYS ILE LEU
SEQRES 19 B 373 PHE PRO GLY ARG ASP TYR ILE ASP GLN TRP ASN LYS VAL
SEQRES 20 B 373 ILE GLU GLN LEU GLY THR PRO CYS PRO GLU PHE MET LYS
SEQRES 21 B 373 LYS LEU GLN PRO THR VAL ARG THR TYR VAL GLU ASN ARG
SEQRES 22 B 373 PRO LYS TYR ALA GLY TYR SER PHE GLU LYS LEU PHE PRO
SEQRES 23 B 373 ASP VAL LEU PHE PRO ALA ASP SER GLU HIS ASN LYS LEU
SEQRES 24 B 373 LYS ALA SER GLN ALA ARG ASP LEU LEU SER LYS MET LEU
SEQRES 25 B 373 VAL ILE ASP ALA SER LYS ARG ILE SER VAL ASP GLU ALA
SEQRES 26 B 373 LEU GLN HIS PRO TYR ILE ASN VAL TRP TYR ASP PRO SER
SEQRES 27 B 373 GLU ALA GLU ALA PRO PRO PRO LYS ILE PRO ASP LYS GLN
SEQRES 28 B 373 LEU ASP GLU ARG GLU HIS THR ILE GLU GLU TRP LYS GLU
SEQRES 29 B 373 LEU ILE TYR LYS GLU VAL MET ASP LEU
SEQRES 1 C 11 ARG PRO LYS ARG PRO THR THR LEU ASN LEU PHE
HELIX 1 AA1 SER A 12 GLY A 25 1 14
HELIX 2 AA2 GLN A 26 GLY A 37 1 12
HELIX 3 AA3 THR A 49 GLY A 58 1 10
HELIX 4 AA4 HIS A 59 ASN A 69 1 11
HELIX 5 AA5 THR A 82 GLY A 91 1 10
HELIX 6 AA6 HIS A 92 ASN A 102 1 11
HELIX 7 AA7 ALA A 115 TRP A 123 1 9
HELIX 8 AA8 HIS A 125 ASN A 135 1 11
HELIX 9 AA9 THR A 148 ASN A 156 1 9
HELIX 10 AB1 ASN A 158 GLY A 181 1 24
HELIX 11 AB2 HIS A 182 ASN A 192 1 11
HELIX 12 AB3 THR A 205 GLY A 214 1 10
HELIX 13 AB4 HIS A 215 TYR A 225 1 11
HELIX 14 AB5 THR A 238 GLY A 247 1 10
HELIX 15 AB6 HIS A 248 TYR A 258 1 11
HELIX 16 AB7 THR A 271 GLY A 280 1 10
HELIX 17 AB8 HIS A 281 TYR A 291 1 11
HELIX 18 AB9 THR A 304 ASN A 312 1 9
HELIX 19 AC1 ASN A 314 ASN A 325 1 12
HELIX 20 AC2 PRO B 60 GLN B 62 5 3
HELIX 21 AC3 ASN B 63 VAL B 80 1 18
HELIX 22 AC4 LEU B 115 ILE B 119 1 5
HELIX 23 AC5 ASP B 124 ALA B 145 1 22
HELIX 24 AC6 LYS B 153 SER B 155 5 3
HELIX 25 AC7 THR B 188 ARG B 192 5 5
HELIX 26 AC8 ALA B 193 LEU B 198 1 6
HELIX 27 AC9 ASN B 205 HIS B 221 1 17
HELIX 28 AD1 ASP B 229 GLY B 242 1 14
HELIX 29 AD2 CYS B 245 LYS B 250 1 6
HELIX 30 AD3 GLN B 253 GLU B 261 1 9
HELIX 31 AD4 SER B 270 PHE B 275 1 6
HELIX 32 AD5 SER B 284 LEU B 302 1 19
HELIX 33 AD6 SER B 311 GLN B 317 1 7
HELIX 34 AD7 ILE B 321 TYR B 325 5 5
HELIX 35 AD8 ASP B 326 GLU B 331 1 6
HELIX 36 AD9 THR B 348 MET B 361 1 14
SHEET 1 AA1 2 PHE B 10 ILE B 15 0
SHEET 2 AA1 2 SER B 18 LEU B 23 -1 O PHE B 20 N VAL B 13
SHEET 1 AA2 5 TYR B 26 PRO B 31 0
SHEET 2 AA2 5 VAL B 40 ASP B 45 -1 O ALA B 42 N LYS B 30
SHEET 3 AA2 5 ARG B 50 SER B 58 -1 O VAL B 52 N ALA B 43
SHEET 4 AA2 5 ASP B 103 GLU B 109 -1 O MET B 108 N ALA B 53
SHEET 5 AA2 5 LEU B 88 PHE B 92 -1 N LEU B 89 O VAL B 107
SHEET 1 AA3 3 ALA B 113 ASN B 114 0
SHEET 2 AA3 3 ILE B 157 VAL B 159 -1 O VAL B 159 N ALA B 113
SHEET 3 AA3 3 LEU B 165 ILE B 167 -1 O LYS B 166 N VAL B 158
CRYST1 76.995 76.995 330.725 90.00 90.00 120.00 P 65 6
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 0.012988 0.007499 0.000000 0.00000
SCALE2 0.000000 0.014997 0.000000 0.00000
SCALE3 0.000000 0.000000 0.003024 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
