HEADER IMMUNE SYSTEM 17-DEC-14 4XC2
TITLE CRYSTAL STRUCTURE OF GABARAP IN COMPLEX WITH KBTBD6 LIR PEPTIDE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GABA(A) RECEPTOR-ASSOCIATED PROTEIN;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 FRAGMENT: UNP RESIDUES 3-116;
COMPND 5 SYNONYM: GABARAP PROTEIN,HCG1987397,ISOFORM CRA_B;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: KELCH REPEAT AND BTB DOMAIN-CONTAINING PROTEIN 6;
COMPND 9 CHAIN: E, F, G, H;
COMPND 10 FRAGMENT: UNP RESIDUES 663-673;
COMPND 11 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: GABARAP, HCG_1987397;
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: HOMO SAPIENS;
SOURCE 11 ORGANISM_COMMON: HUMAN;
SOURCE 12 ORGANISM_TAXID: 9606
KEYWDS AUTOPHAGY, COMPLEX, IMMUNE SYSTEM
EXPDTA X-RAY DIFFRACTION
AUTHOR J.HUBER,H.M.GENAU,F.BASCHIERI,V.DOETSCH,H.FARHAN,V.V.ROGOV,
AUTHOR 2 C.BEHRENDS,M.AKUTSU
REVDAT 5 10-JAN-24 4XC2 1 REMARK
REVDAT 4 06-SEP-17 4XC2 1 ATOM
REVDAT 3 26-OCT-16 4XC2 1 AUTHOR
REVDAT 2 01-APR-15 4XC2 1 JRNL
REVDAT 1 04-MAR-15 4XC2 0
JRNL AUTH H.M.GENAU,J.HUBER,F.BASCHIERI,M.AKUTSU,V.DOTSCH,H.FARHAN,
JRNL AUTH 2 V.ROGOV,C.BEHRENDS
JRNL TITL CUL3-KBTBD6/KBTBD7 UBIQUITIN LIGASE COOPERATES WITH GABARAP
JRNL TITL 2 PROTEINS TO SPATIALLY RESTRICT TIAM1-RAC1 SIGNALING.
JRNL REF MOL.CELL V. 57 995 2015
JRNL REFN ISSN 1097-2765
JRNL PMID 25684205
JRNL DOI 10.1016/J.MOLCEL.2014.12.040
REMARK 2
REMARK 2 RESOLUTION. 1.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.7.0029
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 32.73
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 92.7
REMARK 3 NUMBER OF REFLECTIONS : 35614
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.201
REMARK 3 R VALUE (WORKING SET) : 0.198
REMARK 3 FREE R VALUE : 0.258
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1881
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.90
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.95
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2632
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 91.62
REMARK 3 BIN R VALUE (WORKING SET) : 0.3480
REMARK 3 BIN FREE R VALUE SET COUNT : 134
REMARK 3 BIN FREE R VALUE : 0.3660
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4254
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 187
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 33.19
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 5.04000
REMARK 3 B22 (A**2) : -1.19000
REMARK 3 B33 (A**2) : -2.04000
REMARK 3 B12 (A**2) : 0.47000
REMARK 3 B13 (A**2) : 0.75000
REMARK 3 B23 (A**2) : 0.96000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.197
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.181
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.153
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.492
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.966
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.940
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4393 ; 0.009 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 4142 ; 0.000 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 5927 ; 1.162 ; 1.957
REMARK 3 BOND ANGLES OTHERS (DEGREES): 9549 ; 0.635 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 504 ; 7.857 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 234 ;29.437 ;22.991
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 757 ;17.586 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 36 ;15.396 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 602 ; 0.079 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4878 ; 0.014 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 1074 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS U VALUES : REFINED INDIVIDUALLY
REMARK 4
REMARK 4 4XC2 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 18-DEC-14.
REMARK 100 THE DEPOSITION ID IS D_1000205417.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 14-JUL-14
REMARK 200 TEMPERATURE (KELVIN) : 77
REMARK 200 PH : 8.0
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 : PSI PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 37496
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900
REMARK 200 RESOLUTION RANGE LOW (A) : 37.750
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 92.7
REMARK 200 DATA REDUNDANCY : 2.500
REMARK 200 R MERGE (I) : 0.04300
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 12.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.00
REMARK 200 COMPLETENESS FOR SHELL (%) : 91.0
REMARK 200 DATA REDUNDANCY IN SHELL : 2.40
REMARK 200 R MERGE FOR SHELL (I) : 0.36500
REMARK 200 R SYM FOR SHELL (I) : NULL
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: 3D32
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 43.75
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.19
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M AMMONIUM ACETATE, 0.01 M
REMARK 280 MAGNESIUM ACETATE TETRAHYDRATE, 30% POLY ETHYLENE GLYCOL 8000,
REMARK 280 0.1 M TRIS-HCL, PH 8.0, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,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
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4
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: 1400 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 7230 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -6.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, E
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1450 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 7170 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -5.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, 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 350
REMARK 350 BIOMOLECULE: 3
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: 1460 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 7190 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -6.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, G
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: 4
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: 1430 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 7040 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -5.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, H
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 ALA A 0
REMARK 465 ALA C 0
REMARK 465 MET C 1
REMARK 465 ALA D 0
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 MET D 1 CG SD CE
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 HIS B 69 43.18 73.62
REMARK 500 ASN B 81 43.85 35.02
REMARK 500 ASN B 82 17.76 80.28
REMARK 500 LYS C 38 6.62 81.56
REMARK 500 ASP G 664 118.10 -39.19
REMARK 500
REMARK 500 REMARK: NULL
DBREF 4XC2 A 3 116 UNP Q6IAW1 Q6IAW1_HUMAN 3 116
DBREF 4XC2 B 3 116 UNP Q6IAW1 Q6IAW1_HUMAN 3 116
DBREF 4XC2 C 3 116 UNP Q6IAW1 Q6IAW1_HUMAN 3 116
DBREF 4XC2 D 3 116 UNP Q6IAW1 Q6IAW1_HUMAN 3 116
DBREF 4XC2 E 663 673 UNP Q86V97 KBTB6_HUMAN 663 673
DBREF 4XC2 F 663 673 UNP Q86V97 KBTB6_HUMAN 663 673
DBREF 4XC2 G 663 673 UNP Q86V97 KBTB6_HUMAN 663 673
DBREF 4XC2 H 663 673 UNP Q86V97 KBTB6_HUMAN 663 673
SEQADV 4XC2 ALA A 0 UNP Q6IAW1 EXPRESSION TAG
SEQADV 4XC2 MET A 1 UNP Q6IAW1 EXPRESSION TAG
SEQADV 4XC2 GLY A 2 UNP Q6IAW1 EXPRESSION TAG
SEQADV 4XC2 ALA B 0 UNP Q6IAW1 EXPRESSION TAG
SEQADV 4XC2 MET B 1 UNP Q6IAW1 EXPRESSION TAG
SEQADV 4XC2 GLY B 2 UNP Q6IAW1 EXPRESSION TAG
SEQADV 4XC2 ALA C 0 UNP Q6IAW1 EXPRESSION TAG
SEQADV 4XC2 MET C 1 UNP Q6IAW1 EXPRESSION TAG
SEQADV 4XC2 GLY C 2 UNP Q6IAW1 EXPRESSION TAG
SEQADV 4XC2 ALA D 0 UNP Q6IAW1 EXPRESSION TAG
SEQADV 4XC2 MET D 1 UNP Q6IAW1 EXPRESSION TAG
SEQADV 4XC2 GLY D 2 UNP Q6IAW1 EXPRESSION TAG
SEQRES 1 A 117 ALA MET GLY PHE VAL TYR LYS GLU GLU HIS PRO PHE GLU
SEQRES 2 A 117 LYS ARG ARG SER GLU GLY GLU LYS ILE ARG LYS LYS TYR
SEQRES 3 A 117 PRO ASP ARG VAL PRO VAL ILE VAL GLU LYS ALA PRO LYS
SEQRES 4 A 117 ALA ARG ILE GLY ASP LEU ASP LYS LYS LYS TYR LEU VAL
SEQRES 5 A 117 PRO SER ASP LEU THR VAL GLY GLN PHE TYR PHE LEU ILE
SEQRES 6 A 117 ARG LYS ARG ILE HIS LEU ARG ALA GLU ASP ALA LEU PHE
SEQRES 7 A 117 PHE PHE VAL ASN ASN VAL ILE PRO PRO THR SER ALA THR
SEQRES 8 A 117 MET GLY GLN LEU TYR GLN GLU HIS HIS GLU GLU ASP PHE
SEQRES 9 A 117 PHE LEU TYR ILE ALA TYR SER ASP GLU SER VAL TYR GLY
SEQRES 1 B 117 ALA MET GLY PHE VAL TYR LYS GLU GLU HIS PRO PHE GLU
SEQRES 2 B 117 LYS ARG ARG SER GLU GLY GLU LYS ILE ARG LYS LYS TYR
SEQRES 3 B 117 PRO ASP ARG VAL PRO VAL ILE VAL GLU LYS ALA PRO LYS
SEQRES 4 B 117 ALA ARG ILE GLY ASP LEU ASP LYS LYS LYS TYR LEU VAL
SEQRES 5 B 117 PRO SER ASP LEU THR VAL GLY GLN PHE TYR PHE LEU ILE
SEQRES 6 B 117 ARG LYS ARG ILE HIS LEU ARG ALA GLU ASP ALA LEU PHE
SEQRES 7 B 117 PHE PHE VAL ASN ASN VAL ILE PRO PRO THR SER ALA THR
SEQRES 8 B 117 MET GLY GLN LEU TYR GLN GLU HIS HIS GLU GLU ASP PHE
SEQRES 9 B 117 PHE LEU TYR ILE ALA TYR SER ASP GLU SER VAL TYR GLY
SEQRES 1 C 117 ALA MET GLY PHE VAL TYR LYS GLU GLU HIS PRO PHE GLU
SEQRES 2 C 117 LYS ARG ARG SER GLU GLY GLU LYS ILE ARG LYS LYS TYR
SEQRES 3 C 117 PRO ASP ARG VAL PRO VAL ILE VAL GLU LYS ALA PRO LYS
SEQRES 4 C 117 ALA ARG ILE GLY ASP LEU ASP LYS LYS LYS TYR LEU VAL
SEQRES 5 C 117 PRO SER ASP LEU THR VAL GLY GLN PHE TYR PHE LEU ILE
SEQRES 6 C 117 ARG LYS ARG ILE HIS LEU ARG ALA GLU ASP ALA LEU PHE
SEQRES 7 C 117 PHE PHE VAL ASN ASN VAL ILE PRO PRO THR SER ALA THR
SEQRES 8 C 117 MET GLY GLN LEU TYR GLN GLU HIS HIS GLU GLU ASP PHE
SEQRES 9 C 117 PHE LEU TYR ILE ALA TYR SER ASP GLU SER VAL TYR GLY
SEQRES 1 D 117 ALA MET GLY PHE VAL TYR LYS GLU GLU HIS PRO PHE GLU
SEQRES 2 D 117 LYS ARG ARG SER GLU GLY GLU LYS ILE ARG LYS LYS TYR
SEQRES 3 D 117 PRO ASP ARG VAL PRO VAL ILE VAL GLU LYS ALA PRO LYS
SEQRES 4 D 117 ALA ARG ILE GLY ASP LEU ASP LYS LYS LYS TYR LEU VAL
SEQRES 5 D 117 PRO SER ASP LEU THR VAL GLY GLN PHE TYR PHE LEU ILE
SEQRES 6 D 117 ARG LYS ARG ILE HIS LEU ARG ALA GLU ASP ALA LEU PHE
SEQRES 7 D 117 PHE PHE VAL ASN ASN VAL ILE PRO PRO THR SER ALA THR
SEQRES 8 D 117 MET GLY GLN LEU TYR GLN GLU HIS HIS GLU GLU ASP PHE
SEQRES 9 D 117 PHE LEU TYR ILE ALA TYR SER ASP GLU SER VAL TYR GLY
SEQRES 1 E 11 SER ASP ASP ASP PHE TRP VAL ARG VAL ALA PRO
SEQRES 1 F 11 SER ASP ASP ASP PHE TRP VAL ARG VAL ALA PRO
SEQRES 1 G 11 SER ASP ASP ASP PHE TRP VAL ARG VAL ALA PRO
SEQRES 1 H 11 SER ASP ASP ASP PHE TRP VAL ARG VAL ALA PRO
FORMUL 9 HOH *187(H2 O)
HELIX 1 AA1 PHE A 3 HIS A 9 1 7
HELIX 2 AA2 PRO A 10 TYR A 25 1 16
HELIX 3 AA3 THR A 56 HIS A 69 1 14
HELIX 4 AA4 THR A 90 HIS A 99 1 10
HELIX 5 AA5 PHE B 3 HIS B 9 1 7
HELIX 6 AA6 PRO B 10 TYR B 25 1 16
HELIX 7 AA7 THR B 56 ILE B 68 1 13
HELIX 8 AA8 THR B 90 HIS B 99 1 10
HELIX 9 AA9 PHE C 3 HIS C 9 1 7
HELIX 10 AB1 PRO C 10 TYR C 25 1 16
HELIX 11 AB2 THR C 56 HIS C 69 1 14
HELIX 12 AB3 THR C 90 HIS C 99 1 10
HELIX 13 AB4 PHE D 3 HIS D 9 1 7
HELIX 14 AB5 PRO D 10 TYR D 25 1 16
HELIX 15 AB6 THR D 56 ILE D 68 1 13
HELIX 16 AB7 THR D 90 HIS D 99 1 10
SHEET 1 AA1 5 PHE A 77 PHE A 79 0
SHEET 2 AA1 5 LEU A 105 SER A 110 -1 O ALA A 108 N PHE A 79
SHEET 3 AA1 5 ARG A 28 LYS A 35 1 N ILE A 32 O ILE A 107
SHEET 4 AA1 5 LYS A 48 PRO A 52 -1 O TYR A 49 N VAL A 31
SHEET 5 AA1 5 VAL E 669 ARG E 670 1 O VAL E 669 N LYS A 48
SHEET 1 AA2 6 VAL A 114 TYR A 115 0
SHEET 2 AA2 6 TRP H 668 ARG H 670 1 O ARG H 670 N TYR A 115
SHEET 3 AA2 6 LYS D 48 PRO D 52 1 N LEU D 50 O VAL H 669
SHEET 4 AA2 6 ARG D 28 LYS D 35 -1 N VAL D 31 O TYR D 49
SHEET 5 AA2 6 LEU D 105 SER D 110 1 O ILE D 107 N ILE D 32
SHEET 6 AA2 6 PHE D 77 PHE D 79 -1 N PHE D 79 O ALA D 108
SHEET 1 AA3 5 PHE B 77 PHE B 79 0
SHEET 2 AA3 5 LEU B 105 SER B 110 -1 O ALA B 108 N PHE B 79
SHEET 3 AA3 5 ARG B 28 LYS B 35 1 N ILE B 32 O LEU B 105
SHEET 4 AA3 5 LYS B 48 PRO B 52 -1 O TYR B 49 N VAL B 31
SHEET 5 AA3 5 VAL F 669 ARG F 670 1 O VAL F 669 N LYS B 48
SHEET 1 AA4 6 VAL B 114 TYR B 115 0
SHEET 2 AA4 6 TRP G 668 ARG G 670 1 O TRP G 668 N TYR B 115
SHEET 3 AA4 6 LYS C 48 PRO C 52 1 N LYS C 48 O VAL G 669
SHEET 4 AA4 6 ARG C 28 LYS C 35 -1 N VAL C 29 O VAL C 51
SHEET 5 AA4 6 LEU C 105 SER C 110 1 O LEU C 105 N ILE C 32
SHEET 6 AA4 6 PHE C 77 PHE C 79 -1 N PHE C 79 O ALA C 108
CRYST1 38.893 57.353 67.310 65.30 77.34 89.95 P 1 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 0.025712 -0.000021 -0.006379 0.00000
SCALE2 0.000000 0.017436 -0.008260 0.00000
SCALE3 0.000000 0.000000 0.016849 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
