HEADER SIGNALING PROTEIN 20-DEC-17 6BYJ
TITLE STRUCTURE OF HUMAN 14-3-3 GAMMA BOUND TO O-GLCNAC PEPTIDE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 14-3-3 PROTEIN GAMMA;
COMPND 3 CHAIN: A, B, C, D, E, F;
COMPND 4 SYNONYM: PROTEIN KINASE C INHIBITOR PROTEIN 1,KCIP-1;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: TSTTATPPVSQASSTTTSTW O-GLCNAC PEPTIDE;
COMPND 8 CHAIN: G, P, T;
COMPND 9 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: YWHAG;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 MOL_ID: 2;
SOURCE 9 SYNTHETIC: YES;
SOURCE 10 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;
SOURCE 11 ORGANISM_TAXID: 32630
KEYWDS 14-3-3 GAMMA, O-GLCNAC, SIGNALLING, SIGNALING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR M.A.SCHUMACHER
REVDAT 4 04-OCT-23 6BYJ 1 HETSYN
REVDAT 3 29-JUL-20 6BYJ 1 COMPND REMARK HETNAM LINK
REVDAT 3 2 1 SITE
REVDAT 2 22-MAY-19 6BYJ 1 JRNL
REVDAT 1 09-MAY-18 6BYJ 0
JRNL AUTH C.A.TOLEMAN,M.A.SCHUMACHER,S.H.YU,W.ZENG,N.J.COX,T.J.SMITH,
JRNL AUTH 2 E.J.SODERBLOM,A.M.WANDS,J.J.KOHLER,M.BOYCE
JRNL TITL STRUCTURAL BASIS OF O-GLCNAC RECOGNITION BY MAMMALIAN 14-3-3
JRNL TITL 2 PROTEINS.
JRNL REF PROC.NATL.ACAD.SCI.USA V. 115 5956 2018
JRNL REFN ESSN 1091-6490
JRNL PMID 29784830
JRNL DOI 10.1073/PNAS.1722437115
REMARK 2
REMARK 2 RESOLUTION. 2.90 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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 113.94
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 53764
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.229
REMARK 3 R VALUE (WORKING SET) : 0.228
REMARK 3 FREE R VALUE : 0.269
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 3.720
REMARK 3 FREE R VALUE TEST SET COUNT : 1999
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1114.0295 - 6.9890 1.00 4006 155 0.2053 0.2217
REMARK 3 2 6.9890 - 5.5474 1.00 3791 147 0.2314 0.2835
REMARK 3 3 5.5474 - 4.8461 1.00 3746 144 0.2239 0.2892
REMARK 3 4 4.8461 - 4.4030 1.00 3708 143 0.2011 0.2758
REMARK 3 5 4.4030 - 4.0874 1.00 3701 142 0.2179 0.2445
REMARK 3 6 4.0874 - 3.8464 1.00 3668 143 0.2210 0.2467
REMARK 3 7 3.8464 - 3.6538 1.00 3673 141 0.2387 0.2721
REMARK 3 8 3.6538 - 3.4947 1.00 3637 140 0.2466 0.2952
REMARK 3 9 3.4947 - 3.3602 1.00 3674 142 0.2433 0.2974
REMARK 3 10 3.3602 - 3.2442 1.00 3639 141 0.2559 0.3143
REMARK 3 11 3.2442 - 3.1428 1.00 3609 140 0.2747 0.3235
REMARK 3 12 3.1428 - 3.0529 1.00 3661 140 0.2910 0.3483
REMARK 3 13 3.0529 - 2.9726 1.00 3619 141 0.3064 0.3935
REMARK 3 14 2.9726 - 2.9000 1.00 3633 140 0.3418 0.4124
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
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) : 0.440
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 29.850
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 91.24
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 109.5
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 : 0.003 11893
REMARK 3 ANGLE : 0.544 16056
REMARK 3 CHIRALITY : 0.024 1799
REMARK 3 PLANARITY : 0.002 2084
REMARK 3 DIHEDRAL : 15.067 4535
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
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 6BYJ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 21-DEC-17.
REMARK 100 THE DEPOSITION ID IS D_1000231794.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-JUL-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 : ALS
REMARK 200 BEAMLINE : 8.3.1
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 : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 53876
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.900
REMARK 200 RESOLUTION RANGE LOW (A) : 113.942
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 8.800
REMARK 200 R MERGE (I) : 0.06700
REMARK 200 R SYM (I) : 0.06200
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 18.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.06
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 7.00
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.76400
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.500
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: 3UZD
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 64.65
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.48
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 29% PEG 4000, 200 MM SODIUM ACETATE,
REMARK 280 0.1 M TRIS PH 8.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE
REMARK 280 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y+1/2,X+1/2,Z+1/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+3/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+1/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+3/4
REMARK 290 7555 Y,X,-Z
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 157.05000
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 61.13500
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 61.13500
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 78.52500
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 61.13500
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 61.13500
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 235.57500
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 61.13500
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 61.13500
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 78.52500
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 61.13500
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 61.13500
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 235.57500
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 0.00000
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 157.05000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3
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: TETRAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, D, G, P
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: TRIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, C, T
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 APPLY THE FOLLOWING TO CHAINS: E, 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 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 ASP B 240
REMARK 465 ASP B 241
REMARK 465 ASP C 240
REMARK 465 ASP C 241
REMARK 465 ASP D 240
REMARK 465 ASP D 241
REMARK 465 ASP E 239
REMARK 465 ASP E 240
REMARK 465 ASP E 241
REMARK 465 VAL F 2
REMARK 465 SER F 235
REMARK 465 ASP F 236
REMARK 465 GLN F 237
REMARK 465 GLN F 238
REMARK 465 ASP F 239
REMARK 465 ASP F 240
REMARK 465 ASP F 241
REMARK 465 THR G 496
REMARK 465 SER G 497
REMARK 465 THR G 498
REMARK 465 THR G 499
REMARK 465 SER G 513
REMARK 465 THR G 514
REMARK 465 TRP G 515
REMARK 465 THR P 496
REMARK 465 SER P 497
REMARK 465 THR P 498
REMARK 465 THR P 499
REMARK 465 ALA P 500
REMARK 465 THR P 501
REMARK 465 SER P 509
REMARK 465 THR P 510
REMARK 465 THR P 511
REMARK 465 THR P 512
REMARK 465 SER P 513
REMARK 465 THR P 514
REMARK 465 TRP P 515
REMARK 465 THR T 496
REMARK 465 SER T 497
REMARK 465 THR T 498
REMARK 465 THR T 499
REMARK 465 ALA T 500
REMARK 465 THR T 501
REMARK 465 PRO T 502
REMARK 465 PRO T 503
REMARK 465 THR T 511
REMARK 465 THR T 512
REMARK 465 SER T 513
REMARK 465 THR T 514
REMARK 465 TRP T 515
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 OG SER G 505 C2 NAG G 601 2.18
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 OE2 GLU C 114 OG1 THR F 139 3555 2.19
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 ARG A 19 77.60 -110.52
REMARK 500 TYR A 107 -46.13 -137.49
REMARK 500 GLN A 116 58.43 -103.36
REMARK 500 SER A 215 29.34 -151.42
REMARK 500 ARG B 19 75.31 -107.36
REMARK 500 TYR B 107 -49.99 -139.45
REMARK 500 TYR C 107 -61.00 -138.62
REMARK 500 GLN C 116 50.43 -105.88
REMARK 500 ILE C 186 -60.93 -92.71
REMARK 500 ARG D 19 79.81 -115.33
REMARK 500 TYR D 107 -41.40 -139.53
REMARK 500 LEU D 108 -64.69 -96.71
REMARK 500 ASN D 111 39.06 -90.93
REMARK 500 GLN D 116 52.22 -95.80
REMARK 500 ALA D 189 76.87 -110.53
REMARK 500 GLU D 207 47.11 -104.89
REMARK 500 THR D 210 36.00 -91.04
REMARK 500 TYR E 107 -51.04 -142.55
REMARK 500 ALA E 189 79.38 -111.28
REMARK 500 GLU E 207 34.60 -97.42
REMARK 500 TYR F 107 -48.38 -142.65
REMARK 500 CYS F 112 108.48 -56.89
REMARK 500 GLU F 207 56.75 -106.30
REMARK 500 ALA G 507 70.54 -155.77
REMARK 500 THR G 511 -88.23 -80.59
REMARK 500 SER T 505 -156.48 -157.82
REMARK 500
REMARK 500 REMARK: NULL
DBREF 6BYJ A 2 241 UNP P61981 1433G_HUMAN 2 241
DBREF 6BYJ B 2 241 UNP P61981 1433G_HUMAN 2 241
DBREF 6BYJ C 2 241 UNP P61981 1433G_HUMAN 2 241
DBREF 6BYJ D 2 241 UNP P61981 1433G_HUMAN 2 241
DBREF 6BYJ E 2 241 UNP P61981 1433G_HUMAN 2 241
DBREF 6BYJ F 2 241 UNP P61981 1433G_HUMAN 2 241
DBREF 6BYJ G 496 515 PDB 6BYJ 6BYJ 496 515
DBREF 6BYJ P 496 515 PDB 6BYJ 6BYJ 496 515
DBREF 6BYJ T 496 515 PDB 6BYJ 6BYJ 496 515
SEQRES 1 A 240 VAL ASP ARG GLU GLN LEU VAL GLN LYS ALA ARG LEU ALA
SEQRES 2 A 240 GLU GLN ALA GLU ARG TYR ASP ASP MET ALA ALA ALA MET
SEQRES 3 A 240 LYS ASN VAL THR GLU LEU ASN GLU PRO LEU SER ASN GLU
SEQRES 4 A 240 GLU ARG ASN LEU LEU SER VAL ALA TYR LYS ASN VAL VAL
SEQRES 5 A 240 GLY ALA ARG ARG SER SER TRP ARG VAL ILE SER SER ILE
SEQRES 6 A 240 GLU GLN LYS THR SER ALA ASP GLY ASN GLU LYS LYS ILE
SEQRES 7 A 240 GLU MET VAL ARG ALA TYR ARG GLU LYS ILE GLU LYS GLU
SEQRES 8 A 240 LEU GLU ALA VAL CYS GLN ASP VAL LEU SER LEU LEU ASP
SEQRES 9 A 240 ASN TYR LEU ILE LYS ASN CYS SER GLU THR GLN TYR GLU
SEQRES 10 A 240 SER LYS VAL PHE TYR LEU LYS MET LYS GLY ASP TYR TYR
SEQRES 11 A 240 ARG TYR LEU ALA GLU VAL ALA THR GLY GLU LYS ARG ALA
SEQRES 12 A 240 THR VAL VAL GLU SER SER GLU LYS ALA TYR SER GLU ALA
SEQRES 13 A 240 HIS GLU ILE SER LYS GLU HIS MET GLN PRO THR HIS PRO
SEQRES 14 A 240 ILE ARG LEU GLY LEU ALA LEU ASN TYR SER VAL PHE TYR
SEQRES 15 A 240 TYR GLU ILE GLN ASN ALA PRO GLU GLN ALA CYS HIS LEU
SEQRES 16 A 240 ALA LYS THR ALA PHE ASP ASP ALA ILE ALA GLU LEU ASP
SEQRES 17 A 240 THR LEU ASN GLU ASP SER TYR LYS ASP SER THR LEU ILE
SEQRES 18 A 240 MET GLN LEU LEU ARG ASP ASN LEU THR LEU TRP THR SER
SEQRES 19 A 240 ASP GLN GLN ASP ASP ASP
SEQRES 1 B 240 VAL ASP ARG GLU GLN LEU VAL GLN LYS ALA ARG LEU ALA
SEQRES 2 B 240 GLU GLN ALA GLU ARG TYR ASP ASP MET ALA ALA ALA MET
SEQRES 3 B 240 LYS ASN VAL THR GLU LEU ASN GLU PRO LEU SER ASN GLU
SEQRES 4 B 240 GLU ARG ASN LEU LEU SER VAL ALA TYR LYS ASN VAL VAL
SEQRES 5 B 240 GLY ALA ARG ARG SER SER TRP ARG VAL ILE SER SER ILE
SEQRES 6 B 240 GLU GLN LYS THR SER ALA ASP GLY ASN GLU LYS LYS ILE
SEQRES 7 B 240 GLU MET VAL ARG ALA TYR ARG GLU LYS ILE GLU LYS GLU
SEQRES 8 B 240 LEU GLU ALA VAL CYS GLN ASP VAL LEU SER LEU LEU ASP
SEQRES 9 B 240 ASN TYR LEU ILE LYS ASN CYS SER GLU THR GLN TYR GLU
SEQRES 10 B 240 SER LYS VAL PHE TYR LEU LYS MET LYS GLY ASP TYR TYR
SEQRES 11 B 240 ARG TYR LEU ALA GLU VAL ALA THR GLY GLU LYS ARG ALA
SEQRES 12 B 240 THR VAL VAL GLU SER SER GLU LYS ALA TYR SER GLU ALA
SEQRES 13 B 240 HIS GLU ILE SER LYS GLU HIS MET GLN PRO THR HIS PRO
SEQRES 14 B 240 ILE ARG LEU GLY LEU ALA LEU ASN TYR SER VAL PHE TYR
SEQRES 15 B 240 TYR GLU ILE GLN ASN ALA PRO GLU GLN ALA CYS HIS LEU
SEQRES 16 B 240 ALA LYS THR ALA PHE ASP ASP ALA ILE ALA GLU LEU ASP
SEQRES 17 B 240 THR LEU ASN GLU ASP SER TYR LYS ASP SER THR LEU ILE
SEQRES 18 B 240 MET GLN LEU LEU ARG ASP ASN LEU THR LEU TRP THR SER
SEQRES 19 B 240 ASP GLN GLN ASP ASP ASP
SEQRES 1 C 240 VAL ASP ARG GLU GLN LEU VAL GLN LYS ALA ARG LEU ALA
SEQRES 2 C 240 GLU GLN ALA GLU ARG TYR ASP ASP MET ALA ALA ALA MET
SEQRES 3 C 240 LYS ASN VAL THR GLU LEU ASN GLU PRO LEU SER ASN GLU
SEQRES 4 C 240 GLU ARG ASN LEU LEU SER VAL ALA TYR LYS ASN VAL VAL
SEQRES 5 C 240 GLY ALA ARG ARG SER SER TRP ARG VAL ILE SER SER ILE
SEQRES 6 C 240 GLU GLN LYS THR SER ALA ASP GLY ASN GLU LYS LYS ILE
SEQRES 7 C 240 GLU MET VAL ARG ALA TYR ARG GLU LYS ILE GLU LYS GLU
SEQRES 8 C 240 LEU GLU ALA VAL CYS GLN ASP VAL LEU SER LEU LEU ASP
SEQRES 9 C 240 ASN TYR LEU ILE LYS ASN CYS SER GLU THR GLN TYR GLU
SEQRES 10 C 240 SER LYS VAL PHE TYR LEU LYS MET LYS GLY ASP TYR TYR
SEQRES 11 C 240 ARG TYR LEU ALA GLU VAL ALA THR GLY GLU LYS ARG ALA
SEQRES 12 C 240 THR VAL VAL GLU SER SER GLU LYS ALA TYR SER GLU ALA
SEQRES 13 C 240 HIS GLU ILE SER LYS GLU HIS MET GLN PRO THR HIS PRO
SEQRES 14 C 240 ILE ARG LEU GLY LEU ALA LEU ASN TYR SER VAL PHE TYR
SEQRES 15 C 240 TYR GLU ILE GLN ASN ALA PRO GLU GLN ALA CYS HIS LEU
SEQRES 16 C 240 ALA LYS THR ALA PHE ASP ASP ALA ILE ALA GLU LEU ASP
SEQRES 17 C 240 THR LEU ASN GLU ASP SER TYR LYS ASP SER THR LEU ILE
SEQRES 18 C 240 MET GLN LEU LEU ARG ASP ASN LEU THR LEU TRP THR SER
SEQRES 19 C 240 ASP GLN GLN ASP ASP ASP
SEQRES 1 D 240 VAL ASP ARG GLU GLN LEU VAL GLN LYS ALA ARG LEU ALA
SEQRES 2 D 240 GLU GLN ALA GLU ARG TYR ASP ASP MET ALA ALA ALA MET
SEQRES 3 D 240 LYS ASN VAL THR GLU LEU ASN GLU PRO LEU SER ASN GLU
SEQRES 4 D 240 GLU ARG ASN LEU LEU SER VAL ALA TYR LYS ASN VAL VAL
SEQRES 5 D 240 GLY ALA ARG ARG SER SER TRP ARG VAL ILE SER SER ILE
SEQRES 6 D 240 GLU GLN LYS THR SER ALA ASP GLY ASN GLU LYS LYS ILE
SEQRES 7 D 240 GLU MET VAL ARG ALA TYR ARG GLU LYS ILE GLU LYS GLU
SEQRES 8 D 240 LEU GLU ALA VAL CYS GLN ASP VAL LEU SER LEU LEU ASP
SEQRES 9 D 240 ASN TYR LEU ILE LYS ASN CYS SER GLU THR GLN TYR GLU
SEQRES 10 D 240 SER LYS VAL PHE TYR LEU LYS MET LYS GLY ASP TYR TYR
SEQRES 11 D 240 ARG TYR LEU ALA GLU VAL ALA THR GLY GLU LYS ARG ALA
SEQRES 12 D 240 THR VAL VAL GLU SER SER GLU LYS ALA TYR SER GLU ALA
SEQRES 13 D 240 HIS GLU ILE SER LYS GLU HIS MET GLN PRO THR HIS PRO
SEQRES 14 D 240 ILE ARG LEU GLY LEU ALA LEU ASN TYR SER VAL PHE TYR
SEQRES 15 D 240 TYR GLU ILE GLN ASN ALA PRO GLU GLN ALA CYS HIS LEU
SEQRES 16 D 240 ALA LYS THR ALA PHE ASP ASP ALA ILE ALA GLU LEU ASP
SEQRES 17 D 240 THR LEU ASN GLU ASP SER TYR LYS ASP SER THR LEU ILE
SEQRES 18 D 240 MET GLN LEU LEU ARG ASP ASN LEU THR LEU TRP THR SER
SEQRES 19 D 240 ASP GLN GLN ASP ASP ASP
SEQRES 1 E 240 VAL ASP ARG GLU GLN LEU VAL GLN LYS ALA ARG LEU ALA
SEQRES 2 E 240 GLU GLN ALA GLU ARG TYR ASP ASP MET ALA ALA ALA MET
SEQRES 3 E 240 LYS ASN VAL THR GLU LEU ASN GLU PRO LEU SER ASN GLU
SEQRES 4 E 240 GLU ARG ASN LEU LEU SER VAL ALA TYR LYS ASN VAL VAL
SEQRES 5 E 240 GLY ALA ARG ARG SER SER TRP ARG VAL ILE SER SER ILE
SEQRES 6 E 240 GLU GLN LYS THR SER ALA ASP GLY ASN GLU LYS LYS ILE
SEQRES 7 E 240 GLU MET VAL ARG ALA TYR ARG GLU LYS ILE GLU LYS GLU
SEQRES 8 E 240 LEU GLU ALA VAL CYS GLN ASP VAL LEU SER LEU LEU ASP
SEQRES 9 E 240 ASN TYR LEU ILE LYS ASN CYS SER GLU THR GLN TYR GLU
SEQRES 10 E 240 SER LYS VAL PHE TYR LEU LYS MET LYS GLY ASP TYR TYR
SEQRES 11 E 240 ARG TYR LEU ALA GLU VAL ALA THR GLY GLU LYS ARG ALA
SEQRES 12 E 240 THR VAL VAL GLU SER SER GLU LYS ALA TYR SER GLU ALA
SEQRES 13 E 240 HIS GLU ILE SER LYS GLU HIS MET GLN PRO THR HIS PRO
SEQRES 14 E 240 ILE ARG LEU GLY LEU ALA LEU ASN TYR SER VAL PHE TYR
SEQRES 15 E 240 TYR GLU ILE GLN ASN ALA PRO GLU GLN ALA CYS HIS LEU
SEQRES 16 E 240 ALA LYS THR ALA PHE ASP ASP ALA ILE ALA GLU LEU ASP
SEQRES 17 E 240 THR LEU ASN GLU ASP SER TYR LYS ASP SER THR LEU ILE
SEQRES 18 E 240 MET GLN LEU LEU ARG ASP ASN LEU THR LEU TRP THR SER
SEQRES 19 E 240 ASP GLN GLN ASP ASP ASP
SEQRES 1 F 240 VAL ASP ARG GLU GLN LEU VAL GLN LYS ALA ARG LEU ALA
SEQRES 2 F 240 GLU GLN ALA GLU ARG TYR ASP ASP MET ALA ALA ALA MET
SEQRES 3 F 240 LYS ASN VAL THR GLU LEU ASN GLU PRO LEU SER ASN GLU
SEQRES 4 F 240 GLU ARG ASN LEU LEU SER VAL ALA TYR LYS ASN VAL VAL
SEQRES 5 F 240 GLY ALA ARG ARG SER SER TRP ARG VAL ILE SER SER ILE
SEQRES 6 F 240 GLU GLN LYS THR SER ALA ASP GLY ASN GLU LYS LYS ILE
SEQRES 7 F 240 GLU MET VAL ARG ALA TYR ARG GLU LYS ILE GLU LYS GLU
SEQRES 8 F 240 LEU GLU ALA VAL CYS GLN ASP VAL LEU SER LEU LEU ASP
SEQRES 9 F 240 ASN TYR LEU ILE LYS ASN CYS SER GLU THR GLN TYR GLU
SEQRES 10 F 240 SER LYS VAL PHE TYR LEU LYS MET LYS GLY ASP TYR TYR
SEQRES 11 F 240 ARG TYR LEU ALA GLU VAL ALA THR GLY GLU LYS ARG ALA
SEQRES 12 F 240 THR VAL VAL GLU SER SER GLU LYS ALA TYR SER GLU ALA
SEQRES 13 F 240 HIS GLU ILE SER LYS GLU HIS MET GLN PRO THR HIS PRO
SEQRES 14 F 240 ILE ARG LEU GLY LEU ALA LEU ASN TYR SER VAL PHE TYR
SEQRES 15 F 240 TYR GLU ILE GLN ASN ALA PRO GLU GLN ALA CYS HIS LEU
SEQRES 16 F 240 ALA LYS THR ALA PHE ASP ASP ALA ILE ALA GLU LEU ASP
SEQRES 17 F 240 THR LEU ASN GLU ASP SER TYR LYS ASP SER THR LEU ILE
SEQRES 18 F 240 MET GLN LEU LEU ARG ASP ASN LEU THR LEU TRP THR SER
SEQRES 19 F 240 ASP GLN GLN ASP ASP ASP
SEQRES 1 G 20 THR SER THR THR ALA THR PRO PRO VAL SER GLN ALA SER
SEQRES 2 G 20 SER THR THR THR SER THR TRP
SEQRES 1 P 20 THR SER THR THR ALA THR PRO PRO VAL SER GLN ALA SER
SEQRES 2 P 20 SER THR THR THR SER THR TRP
SEQRES 1 T 20 THR SER THR THR ALA THR PRO PRO VAL SER GLN ALA SER
SEQRES 2 T 20 SER THR THR THR SER THR TRP
HET NAG G 601 14
HET NAG P 601 14
HET NAG T 601 14
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETSYN NAG N-ACETYL-BETA-D-GLUCOSAMINE; 2-ACETAMIDO-2-DEOXY-BETA-
HETSYN 2 NAG D-GLUCOSE; 2-ACETAMIDO-2-DEOXY-D-GLUCOSE; 2-ACETAMIDO-
HETSYN 3 NAG 2-DEOXY-GLUCOSE; N-ACETYL-D-GLUCOSAMINE
FORMUL 10 NAG 3(C8 H15 N O6)
HELIX 1 AA1 ASP A 3 ALA A 17 1 15
HELIX 2 AA2 ARG A 19 LEU A 33 1 15
HELIX 3 AA3 SER A 38 SER A 71 1 34
HELIX 4 AA4 ASN A 75 TYR A 107 1 33
HELIX 5 AA5 GLN A 116 GLU A 136 1 21
HELIX 6 AA6 THR A 139 MET A 165 1 27
HELIX 7 AA7 HIS A 169 ILE A 186 1 18
HELIX 8 AA8 ALA A 189 GLU A 207 1 19
HELIX 9 AA9 LEU A 208 LEU A 211 5 4
HELIX 10 AB1 SER A 215 ASP A 241 1 27
HELIX 11 AB2 ASP B 3 ALA B 17 1 15
HELIX 12 AB3 ARG B 19 GLU B 32 1 14
HELIX 13 AB4 SER B 38 THR B 70 1 33
HELIX 14 AB5 ASN B 75 TYR B 107 1 33
HELIX 15 AB6 GLN B 116 ALA B 138 1 23
HELIX 16 AB7 GLY B 140 MET B 165 1 26
HELIX 17 AB8 HIS B 169 GLN B 187 1 19
HELIX 18 AB9 ALA B 189 GLU B 207 1 19
HELIX 19 AC1 LEU B 208 LEU B 211 5 4
HELIX 20 AC2 SER B 215 GLN B 237 1 23
HELIX 21 AC3 ASP C 3 ALA C 17 1 15
HELIX 22 AC4 ARG C 19 GLU C 32 1 14
HELIX 23 AC5 SER C 38 THR C 70 1 33
HELIX 24 AC6 SER C 71 GLY C 74 5 4
HELIX 25 AC7 ASN C 75 TYR C 107 1 33
HELIX 26 AC8 GLN C 116 ALA C 138 1 23
HELIX 27 AC9 THR C 139 MET C 165 1 27
HELIX 28 AD1 HIS C 169 ILE C 186 1 18
HELIX 29 AD2 ALA C 189 ALA C 206 1 18
HELIX 30 AD3 GLU C 207 LEU C 211 5 5
HELIX 31 AD4 SER C 215 GLN C 237 1 23
HELIX 32 AD5 ASP D 3 ALA D 17 1 15
HELIX 33 AD6 ARG D 19 GLU D 32 1 14
HELIX 34 AD7 SER D 38 SER D 71 1 34
HELIX 35 AD8 ASN D 75 TYR D 107 1 33
HELIX 36 AD9 GLN D 116 ALA D 138 1 23
HELIX 37 AE1 THR D 139 MET D 165 1 27
HELIX 38 AE2 HIS D 169 ILE D 186 1 18
HELIX 39 AE3 ALA D 189 GLU D 207 1 19
HELIX 40 AE4 ASP D 214 GLN D 238 1 25
HELIX 41 AE5 ASP E 3 ALA E 17 1 15
HELIX 42 AE6 ARG E 19 GLU E 32 1 14
HELIX 43 AE7 SER E 38 GLY E 74 1 37
HELIX 44 AE8 ASN E 75 TYR E 107 1 33
HELIX 45 AE9 TYR E 107 CYS E 112 1 6
HELIX 46 AF1 GLN E 116 GLU E 136 1 21
HELIX 47 AF2 GLY E 140 MET E 165 1 26
HELIX 48 AF3 HIS E 169 ILE E 186 1 18
HELIX 49 AF4 ALA E 189 GLU E 207 1 19
HELIX 50 AF5 SER E 215 SER E 235 1 21
HELIX 51 AF6 ASP E 236 GLN E 238 5 3
HELIX 52 AF7 ARG F 4 ALA F 17 1 14
HELIX 53 AF8 ARG F 19 GLU F 32 1 14
HELIX 54 AF9 SER F 38 GLN F 68 1 31
HELIX 55 AG1 GLN F 68 GLY F 74 1 7
HELIX 56 AG2 GLU F 76 TYR F 107 1 32
HELIX 57 AG3 GLN F 116 ALA F 135 1 20
HELIX 58 AG4 THR F 139 GLU F 159 1 21
HELIX 59 AG5 HIS F 169 GLU F 185 1 17
HELIX 60 AG6 ALA F 189 GLU F 207 1 19
HELIX 61 AG7 LEU F 208 LEU F 211 5 4
HELIX 62 AG8 SER F 215 THR F 231 1 17
LINK OG SER G 505 C1 NAG G 601 1555 1555 1.43
LINK OG SER P 505 C1 NAG P 601 1555 1555 1.45
LINK OG SER T 505 C1 NAG T 601 1555 1555 1.47
CRYST1 122.270 122.270 314.100 90.00 90.00 90.00 P 41 21 2 48
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 0.008179 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008179 0.000000 0.00000
SCALE3 0.000000 0.000000 0.003184 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
