HEADER TRANSFERASE 11-NOV-07 3BBW
TITLE CRYSTAL STRUCTURE OF THE ERBB4 KINASE IN ITS INACTIVE CONFORMATION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: RECEPTOR TYROSINE-PROTEIN KINASE ERBB-4;
COMPND 3 CHAIN: B, A;
COMPND 4 SYNONYM: P180ERBB4, TYROSINE KINASE-TYPE CELL SURFACE RECEPTOR HER4;
COMPND 5 EC: 2.7.10.1;
COMPND 6 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: ERBB4, HER4;
SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: SF9;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PFASTBAC
KEYWDS INACTIVE KINASE CONFORMATION, ALTERNATIVE SPLICING, ATP-BINDING,
KEYWDS 2 GLYCOPROTEIN, MEMBRANE, NUCLEOTIDE-BINDING, PHOSPHORYLATION,
KEYWDS 3 RECEPTOR, TRANSFERASE, TRANSMEMBRANE, TYROSINE-PROTEIN KINASE
EXPDTA X-RAY DIFFRACTION
AUTHOR C.QIU
REVDAT 5 21-FEB-24 3BBW 1 REMARK
REVDAT 4 25-OCT-17 3BBW 1 REMARK
REVDAT 3 24-FEB-09 3BBW 1 VERSN
REVDAT 2 25-MAR-08 3BBW 1 JRNL
REVDAT 1 12-FEB-08 3BBW 0
JRNL AUTH C.QIU,M.K.TARRANT,S.H.CHOI,A.SATHYAMURTHY,R.BOSE,S.BANJADE,
JRNL AUTH 2 A.PAL,W.G.BORNMANN,M.A.LEMMON,P.A.COLE,D.J.LEAHY
JRNL TITL MECHANISM OF ACTIVATION AND INHIBITION OF THE HER4/ERBB4
JRNL TITL 2 KINASE.
JRNL REF STRUCTURE V. 16 460 2008
JRNL REFN ISSN 0969-2126
JRNL PMID 18334220
JRNL DOI 10.1016/J.STR.2007.12.016
REMARK 2
REMARK 2 RESOLUTION. 4.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
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) : 4.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.2
REMARK 3 NUMBER OF REFLECTIONS : 9034
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) : 0.305
REMARK 3 R VALUE (WORKING SET) : 0.302
REMARK 3 FREE R VALUE : 0.354
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.700
REMARK 3 FREE R VALUE TEST SET COUNT : 428
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) : 4.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 4.10
REMARK 3 REFLECTION IN BIN (WORKING SET) : 592
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 91.54
REMARK 3 BIN R VALUE (WORKING SET) : 0.3380
REMARK 3 BIN FREE R VALUE SET COUNT : 25
REMARK 3 BIN FREE R VALUE : 0.2850
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4354
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 0
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 63.66
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -8.46000
REMARK 3 B22 (A**2) : -8.46000
REMARK 3 B33 (A**2) : 12.69000
REMARK 3 B12 (A**2) : -4.23000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 1.030
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 1.216
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 90.276
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.759
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.667
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4454 ; 0.012 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 6024 ; 1.639 ; 1.975
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 537 ; 8.146 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 185 ;32.893 ;23.405
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 823 ;19.019 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 31 ;15.000 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 676 ; 0.088 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3261 ; 0.006 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 2099 ; 0.244 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 2943 ; 0.316 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 144 ; 0.182 ; 0.200
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): 35 ; 0.307 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 2 ; 0.144 ; 0.200
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): 2791 ; 0.320 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 4398 ; 0.561 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1918 ; 0.505 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1626 ; 0.827 ; 4.500
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 : 1
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
REMARK 3 CHAIN NAMES : B A
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 B 683 B 966 1
REMARK 3 1 A 683 A 966 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 1 B (A): 2149 ; 0.050 ; 0.050
REMARK 3 TIGHT THERMAL 1 B (A**2): 2149 ; 0.060 ; 0.500
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 : 1.40
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
REMARK 4
REMARK 4 3BBW COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-NOV-07.
REMARK 100 THE DEPOSITION ID IS D_1000045331.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 08-MAY-07
REMARK 200 TEMPERATURE (KELVIN) : NULL
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : CAMD
REMARK 200 BEAMLINE : GCPCC
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 : MAR CCD 165 MM
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO, HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK, HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 9061
REMARK 200 RESOLUTION RANGE HIGH (A) : 4.000
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.6
REMARK 200 DATA REDUNDANCY : 7.500
REMARK 200 R MERGE (I) : 0.25300
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 4.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 4.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 4.14
REMARK 200 COMPLETENESS FOR SHELL (%) : 93.3
REMARK 200 DATA REDUNDANCY IN SHELL : 5.30
REMARK 200 R MERGE FOR SHELL (I) : 0.66700
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 (%): 70.42
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.68
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 2.2 M NACL, 0.2 M MGCL2, 0.1 M HEPES,
REMARK 280 PH 7.0, 2% HEXAFLUOROISOPROPANOL, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+5/6
REMARK 290 6555 X-Y,X,Z+1/6
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 60.44500
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 120.89000
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 90.66750
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 151.11250
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 30.22250
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 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 B 677
REMARK 465 THR B 678
REMARK 465 ALA B 679
REMARK 465 PRO B 680
REMARK 465 ASN B 681
REMARK 465 GLN B 682
REMARK 465 THR B 731
REMARK 465 THR B 732
REMARK 465 GLU B 844
REMARK 465 GLY B 845
REMARK 465 ASP B 846
REMARK 465 GLU B 847
REMARK 465 LYS B 848
REMARK 465 GLU B 849
REMARK 465 TYR B 850
REMARK 465 ASN B 851
REMARK 465 ALA B 852
REMARK 465 ASP B 853
REMARK 465 GLY B 854
REMARK 465 GLY B 855
REMARK 465 LYS B 856
REMARK 465 MET B 857
REMARK 465 ASN B 974
REMARK 465 ASP B 975
REMARK 465 SER B 976
REMARK 465 LYS B 977
REMARK 465 PHE B 978
REMARK 465 PHE B 979
REMARK 465 GLN B 980
REMARK 465 ASN B 981
REMARK 465 LEU B 982
REMARK 465 LEU B 983
REMARK 465 ASP B 984
REMARK 465 GLU B 985
REMARK 465 GLU B 986
REMARK 465 ASP B 987
REMARK 465 LEU B 988
REMARK 465 GLU B 989
REMARK 465 ASP B 990
REMARK 465 MET B 991
REMARK 465 MET B 992
REMARK 465 ASP B 993
REMARK 465 ALA B 994
REMARK 465 GLU B 995
REMARK 465 GLU B 996
REMARK 465 TYR B 997
REMARK 465 LEU B 998
REMARK 465 VAL B 999
REMARK 465 PRO B 1000
REMARK 465 GLN B 1001
REMARK 465 ALA B 1002
REMARK 465 PHE B 1003
REMARK 465 ASN B 1004
REMARK 465 GLY A 677
REMARK 465 THR A 678
REMARK 465 ALA A 679
REMARK 465 PRO A 680
REMARK 465 ASN A 681
REMARK 465 GLN A 682
REMARK 465 THR A 731
REMARK 465 THR A 732
REMARK 465 GLU A 844
REMARK 465 GLY A 845
REMARK 465 ASP A 846
REMARK 465 GLU A 847
REMARK 465 LYS A 848
REMARK 465 GLU A 849
REMARK 465 TYR A 850
REMARK 465 ASN A 851
REMARK 465 ALA A 852
REMARK 465 ASP A 853
REMARK 465 GLY A 854
REMARK 465 GLY A 855
REMARK 465 LYS A 856
REMARK 465 MET A 857
REMARK 465 ARG A 967
REMARK 465 MET A 968
REMARK 465 LYS A 969
REMARK 465 LEU A 970
REMARK 465 PRO A 971
REMARK 465 SER A 972
REMARK 465 PRO A 973
REMARK 465 ASN A 974
REMARK 465 ASP A 975
REMARK 465 SER A 976
REMARK 465 LYS A 977
REMARK 465 PHE A 978
REMARK 465 PHE A 979
REMARK 465 GLN A 980
REMARK 465 ASN A 981
REMARK 465 LEU A 982
REMARK 465 LEU A 983
REMARK 465 ASP A 984
REMARK 465 GLU A 985
REMARK 465 GLU A 986
REMARK 465 ASP A 987
REMARK 465 LEU A 988
REMARK 465 GLU A 989
REMARK 465 ASP A 990
REMARK 465 MET A 991
REMARK 465 MET A 992
REMARK 465 ASP A 993
REMARK 465 ALA A 994
REMARK 465 GLU A 995
REMARK 465 GLU A 996
REMARK 465 TYR A 997
REMARK 465 LEU A 998
REMARK 465 VAL A 999
REMARK 465 PRO A 1000
REMARK 465 GLN A 1001
REMARK 465 ALA A 1002
REMARK 465 PHE A 1003
REMARK 465 ASN A 1004
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 PRO B 722 C - N - CD ANGL. DEV. = -18.1 DEGREES
REMARK 500 PRO B 918 C - N - CA ANGL. DEV. = 9.3 DEGREES
REMARK 500 PRO A 722 C - N - CD ANGL. DEV. = -18.2 DEGREES
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 VAL B 696 -77.72 -104.05
REMARK 500 GLU B 715 135.61 -39.26
REMARK 500 GLU B 717 53.60 -148.81
REMARK 500 PRO B 722 99.89 -3.83
REMARK 500 ALA B 736 74.18 -61.14
REMARK 500 PRO B 753 97.70 -43.84
REMARK 500 HIS B 754 17.86 102.82
REMARK 500 LYS B 787 -45.34 -20.95
REMARK 500 ARG B 817 -13.68 84.17
REMARK 500 ASP B 818 52.41 -150.95
REMARK 500 ARG B 870 39.88 30.44
REMARK 500 PHE B 891 16.77 86.12
REMARK 500 ARG B 902 2.52 -65.08
REMARK 500 PRO B 918 -48.46 -28.34
REMARK 500 ALA B 946 -70.18 -56.80
REMARK 500 ASP B 965 21.11 86.31
REMARK 500 ASP B 966 -7.28 66.20
REMARK 500 SER B 972 -131.74 -119.68
REMARK 500 VAL A 696 -75.17 -104.18
REMARK 500 GLU A 717 51.54 -145.45
REMARK 500 PRO A 722 98.74 -3.47
REMARK 500 ALA A 736 74.42 -62.57
REMARK 500 PRO A 753 98.92 -44.17
REMARK 500 HIS A 754 17.15 106.95
REMARK 500 LYS A 787 -43.53 -23.14
REMARK 500 ARG A 817 -11.24 83.05
REMARK 500 ASP A 818 52.07 -151.09
REMARK 500 ARG A 870 38.47 30.92
REMARK 500 PRO A 918 -50.66 -26.94
REMARK 500 ALA A 946 -71.20 -56.81
REMARK 500 ASP A 965 22.52 81.71
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 ILE B 721 PRO B 722 114.40
REMARK 500 HIS B 752 PRO B 753 120.77
REMARK 500 ILE A 721 PRO A 722 114.54
REMARK 500 HIS A 752 PRO A 753 118.30
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3BBT RELATED DB: PDB
REMARK 900 RELATED ID: 3BCE RELATED DB: PDB
DBREF 3BBW B 677 1004 UNP Q15303 ERBB4_HUMAN 702 1029
DBREF 3BBW A 677 1004 UNP Q15303 ERBB4_HUMAN 702 1029
SEQRES 1 B 328 GLY THR ALA PRO ASN GLN ALA GLN LEU ARG ILE LEU LYS
SEQRES 2 B 328 GLU THR GLU LEU LYS ARG VAL LYS VAL LEU GLY SER GLY
SEQRES 3 B 328 ALA PHE GLY THR VAL TYR LYS GLY ILE TRP VAL PRO GLU
SEQRES 4 B 328 GLY GLU THR VAL LYS ILE PRO VAL ALA ILE LYS ILE LEU
SEQRES 5 B 328 ASN GLU THR THR GLY PRO LYS ALA ASN VAL GLU PHE MET
SEQRES 6 B 328 ASP GLU ALA LEU ILE MET ALA SER MET ASP HIS PRO HIS
SEQRES 7 B 328 LEU VAL ARG LEU LEU GLY VAL CYS LEU SER PRO THR ILE
SEQRES 8 B 328 GLN LEU VAL THR GLN LEU MET PRO HIS GLY CYS LEU LEU
SEQRES 9 B 328 GLU TYR VAL HIS GLU HIS LYS ASP ASN ILE GLY SER GLN
SEQRES 10 B 328 LEU LEU LEU ASN TRP CYS VAL GLN ILE ALA LYS GLY MET
SEQRES 11 B 328 MET TYR LEU GLU GLU ARG ARG LEU VAL HIS ARG ASP LEU
SEQRES 12 B 328 ALA ALA ARG ASN VAL LEU VAL LYS SER PRO ASN HIS VAL
SEQRES 13 B 328 LYS ILE THR ASP PHE GLY LEU ALA ARG LEU LEU GLU GLY
SEQRES 14 B 328 ASP GLU LYS GLU TYR ASN ALA ASP GLY GLY LYS MET PRO
SEQRES 15 B 328 ILE LYS TRP MET ALA LEU GLU CYS ILE HIS TYR ARG LYS
SEQRES 16 B 328 PHE THR HIS GLN SER ASP VAL TRP SER TYR GLY VAL THR
SEQRES 17 B 328 ILE TRP GLU LEU MET THR PHE GLY GLY LYS PRO TYR ASP
SEQRES 18 B 328 GLY ILE PRO THR ARG GLU ILE PRO ASP LEU LEU GLU LYS
SEQRES 19 B 328 GLY GLU ARG LEU PRO GLN PRO PRO ILE CYS THR ILE ASP
SEQRES 20 B 328 VAL TYR MET VAL MET VAL LYS CYS TRP MET ILE ASP ALA
SEQRES 21 B 328 ASP SER ARG PRO LYS PHE LYS GLU LEU ALA ALA GLU PHE
SEQRES 22 B 328 SER ARG MET ALA ARG ASP PRO GLN ARG TYR LEU VAL ILE
SEQRES 23 B 328 GLN GLY ASP ASP ARG MET LYS LEU PRO SER PRO ASN ASP
SEQRES 24 B 328 SER LYS PHE PHE GLN ASN LEU LEU ASP GLU GLU ASP LEU
SEQRES 25 B 328 GLU ASP MET MET ASP ALA GLU GLU TYR LEU VAL PRO GLN
SEQRES 26 B 328 ALA PHE ASN
SEQRES 1 A 328 GLY THR ALA PRO ASN GLN ALA GLN LEU ARG ILE LEU LYS
SEQRES 2 A 328 GLU THR GLU LEU LYS ARG VAL LYS VAL LEU GLY SER GLY
SEQRES 3 A 328 ALA PHE GLY THR VAL TYR LYS GLY ILE TRP VAL PRO GLU
SEQRES 4 A 328 GLY GLU THR VAL LYS ILE PRO VAL ALA ILE LYS ILE LEU
SEQRES 5 A 328 ASN GLU THR THR GLY PRO LYS ALA ASN VAL GLU PHE MET
SEQRES 6 A 328 ASP GLU ALA LEU ILE MET ALA SER MET ASP HIS PRO HIS
SEQRES 7 A 328 LEU VAL ARG LEU LEU GLY VAL CYS LEU SER PRO THR ILE
SEQRES 8 A 328 GLN LEU VAL THR GLN LEU MET PRO HIS GLY CYS LEU LEU
SEQRES 9 A 328 GLU TYR VAL HIS GLU HIS LYS ASP ASN ILE GLY SER GLN
SEQRES 10 A 328 LEU LEU LEU ASN TRP CYS VAL GLN ILE ALA LYS GLY MET
SEQRES 11 A 328 MET TYR LEU GLU GLU ARG ARG LEU VAL HIS ARG ASP LEU
SEQRES 12 A 328 ALA ALA ARG ASN VAL LEU VAL LYS SER PRO ASN HIS VAL
SEQRES 13 A 328 LYS ILE THR ASP PHE GLY LEU ALA ARG LEU LEU GLU GLY
SEQRES 14 A 328 ASP GLU LYS GLU TYR ASN ALA ASP GLY GLY LYS MET PRO
SEQRES 15 A 328 ILE LYS TRP MET ALA LEU GLU CYS ILE HIS TYR ARG LYS
SEQRES 16 A 328 PHE THR HIS GLN SER ASP VAL TRP SER TYR GLY VAL THR
SEQRES 17 A 328 ILE TRP GLU LEU MET THR PHE GLY GLY LYS PRO TYR ASP
SEQRES 18 A 328 GLY ILE PRO THR ARG GLU ILE PRO ASP LEU LEU GLU LYS
SEQRES 19 A 328 GLY GLU ARG LEU PRO GLN PRO PRO ILE CYS THR ILE ASP
SEQRES 20 A 328 VAL TYR MET VAL MET VAL LYS CYS TRP MET ILE ASP ALA
SEQRES 21 A 328 ASP SER ARG PRO LYS PHE LYS GLU LEU ALA ALA GLU PHE
SEQRES 22 A 328 SER ARG MET ALA ARG ASP PRO GLN ARG TYR LEU VAL ILE
SEQRES 23 A 328 GLN GLY ASP ASP ARG MET LYS LEU PRO SER PRO ASN ASP
SEQRES 24 A 328 SER LYS PHE PHE GLN ASN LEU LEU ASP GLU GLU ASP LEU
SEQRES 25 A 328 GLU ASP MET MET ASP ALA GLU GLU TYR LEU VAL PRO GLN
SEQRES 26 A 328 ALA PHE ASN
HELIX 1 1 ASN B 737 MET B 750 1 14
HELIX 2 2 CYS B 778 HIS B 786 1 9
HELIX 3 3 GLY B 791 ARG B 813 1 23
HELIX 4 4 GLY B 838 LEU B 843 1 6
HELIX 5 5 PRO B 858 MET B 862 5 5
HELIX 6 6 ALA B 863 ARG B 870 1 8
HELIX 7 7 THR B 873 THR B 890 1 18
HELIX 8 8 GLU B 903 GLY B 911 1 9
HELIX 9 9 THR B 921 TRP B 932 1 12
HELIX 10 10 LYS B 941 ALA B 953 1 13
HELIX 11 11 ARG B 954 TYR B 959 5 6
HELIX 12 12 ASN A 737 MET A 750 1 14
HELIX 13 13 CYS A 778 HIS A 786 1 9
HELIX 14 14 GLY A 791 ARG A 813 1 23
HELIX 15 15 GLY A 838 LEU A 843 1 6
HELIX 16 16 PRO A 858 MET A 862 5 5
HELIX 17 17 ALA A 863 ARG A 870 1 8
HELIX 18 18 THR A 873 THR A 890 1 18
HELIX 19 19 GLU A 903 GLY A 911 1 9
HELIX 20 20 THR A 921 TRP A 932 1 12
HELIX 21 21 LYS A 941 ALA A 953 1 13
HELIX 22 22 ARG A 954 TYR A 959 5 6
SHEET 1 A 6 ARG B 686 ILE B 687 0
SHEET 2 A 6 LEU B 758 CYS B 762 1 O VAL B 761 N ARG B 686
SHEET 3 A 6 GLN B 768 GLN B 772 -1 O VAL B 770 N GLY B 760
SHEET 4 A 6 ILE B 721 LEU B 728 -1 N ALA B 724 O THR B 771
SHEET 5 A 6 GLY B 705 TRP B 712 -1 N GLY B 710 O VAL B 723
SHEET 6 A 6 LEU B 693 SER B 701 -1 N GLY B 700 O VAL B 707
SHEET 1 B 2 VAL B 824 SER B 828 0
SHEET 2 B 2 HIS B 831 ILE B 834 -1 O LYS B 833 N LEU B 825
SHEET 1 C 6 ARG A 686 ILE A 687 0
SHEET 2 C 6 LEU A 758 CYS A 762 1 O VAL A 761 N ARG A 686
SHEET 3 C 6 GLN A 768 GLN A 772 -1 O VAL A 770 N GLY A 760
SHEET 4 C 6 ILE A 721 LEU A 728 -1 N ALA A 724 O THR A 771
SHEET 5 C 6 GLY A 705 TRP A 712 -1 N TYR A 708 O ILE A 725
SHEET 6 C 6 LEU A 693 SER A 701 -1 N GLY A 700 O VAL A 707
SHEET 1 D 2 VAL A 824 SER A 828 0
SHEET 2 D 2 HIS A 831 ILE A 834 -1 O HIS A 831 N SER A 828
CISPEP 1 GLY B 733 PRO B 734 0 -4.62
CISPEP 2 SER B 972 PRO B 973 0 0.35
CISPEP 3 GLY A 733 PRO A 734 0 -1.87
CRYST1 102.746 102.746 181.335 90.00 90.00 120.00 P 61 12
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 0.009733 0.005619 0.000000 0.00000
SCALE2 0.000000 0.011238 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005515 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
