HEADER PROTEIN BINDING 24-JUL-08 3DXC
TITLE CRYSTAL STRUCTURE OF THE INTRACELLULAR DOMAIN OF HUMAN APP IN COMPLEX
TITLE 2 WITH FE65-PTB2
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: AMYLOID BETA A4 PROTEIN-BINDING FAMILY B MEMBER 1;
COMPND 3 CHAIN: A, C;
COMPND 4 FRAGMENT: PTB2 DOMAIN, UNP RESIDUES 534-667;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: AMYLOID BETA A4 PROTEIN;
COMPND 8 CHAIN: B, D;
COMPND 9 FRAGMENT: APP INTRACELLULAR DOMAIN, UNP RESIDUES 739-770;
COMPND 10 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: APBB1, FE65, RIR;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3) RIL;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET21D;
SOURCE 11 MOL_ID: 2;
SOURCE 12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 13 ORGANISM_COMMON: HUMAN;
SOURCE 14 ORGANISM_TAXID: 9606;
SOURCE 15 GENE: APP, A4, AD1;
SOURCE 16 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 17 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 18 EXPRESSION_SYSTEM_STRAIN: BL21(DE3) RIL;
SOURCE 19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 20 EXPRESSION_SYSTEM_PLASMID: PETTRX_1B
KEYWDS ALZHEIMER'S DISEASE, APP, AICD, FE65, PTB DOMAIN, ALZHEIMER DISEASE,
KEYWDS 2 AMYLOID, APOPTOSIS, CELL ADHESION, COATED PIT, DISEASE MUTATION,
KEYWDS 3 ENDOCYTOSIS, GLYCOPROTEIN, HEPARIN-BINDING, IRON, MEMBRANE, METAL-
KEYWDS 4 BINDING, NOTCH SIGNALING PATHWAY, PHOSPHOPROTEIN, PROTEASE
KEYWDS 5 INHIBITOR, PROTEOGLYCAN, SERINE PROTEASE INHIBITOR, TRANSMEMBRANE,
KEYWDS 6 PROTEIN BINDING
EXPDTA X-RAY DIFFRACTION
AUTHOR J.RADZIMANOWSKI,I.SINNING,K.WILD
REVDAT 5 21-FEB-24 3DXC 1 SEQADV
REVDAT 4 01-FEB-17 3DXC 1 JRNL VERSN
REVDAT 3 24-FEB-09 3DXC 1 VERSN
REVDAT 2 18-NOV-08 3DXC 1 JRNL
REVDAT 1 16-SEP-08 3DXC 0
JRNL AUTH J.RADZIMANOWSKI,B.SIMON,M.SATTLER,K.BEYREUTHER,I.SINNING,
JRNL AUTH 2 K.WILD
JRNL TITL STRUCTURE OF THE INTRACELLULAR DOMAIN OF THE AMYLOID
JRNL TITL 2 PRECURSOR PROTEIN IN COMPLEX WITH FE65-PTB2.
JRNL REF EMBO REP. V. 9 1134 2008
JRNL REFN ISSN 1469-221X
JRNL PMID 18833287
JRNL DOI 10.1038/EMBOR.2008.188
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH R.RADZIMANOWSKI,K.BEYREUTHER,I.SINNING,K.WILD
REMARK 1 TITL OVERPRODUCTION, PURIFICATION, CRYSTALLIZATION AND
REMARK 1 TITL 2 PRELIMINARY X-RAY ANALYSIS OF HUMAN FE65-PTB2 IN COMPLEX
REMARK 1 TITL 3 WITH THE AMYLOID PRECURSOR PROTEIN INTRACELLULAR DOMAIN
REMARK 1 REF ACTA CRYSTALLOGR.,SECT.F V. F64 409 2008
REMARK 1 REFN ESSN 1744-3091
REMARK 1 PMID 18453713
REMARK 2
REMARK 2 RESOLUTION. 2.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.3.0008
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) : 2.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 33.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 30579
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) : 0.204
REMARK 3 R VALUE (WORKING SET) : 0.202
REMARK 3 FREE R VALUE : 0.238
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 6.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1997
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) : 2.10
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.15
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2234
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 BIN R VALUE (WORKING SET) : 0.2700
REMARK 3 BIN FREE R VALUE SET COUNT : 142
REMARK 3 BIN FREE R VALUE : 0.3120
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2395
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 236
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 41.32
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.07000
REMARK 3 B22 (A**2) : -0.07000
REMARK 3 B33 (A**2) : 0.10000
REMARK 3 B12 (A**2) : -0.03000
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): 0.158
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.150
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.109
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.055
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.951
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.935
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2477 ; 0.013 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3366 ; 1.312 ; 1.932
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 307 ; 6.377 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 115 ;34.832 ;23.739
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 390 ;14.210 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 14 ;14.396 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 371 ; 0.089 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1908 ; 0.005 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1144 ; 0.206 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 1697 ; 0.297 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 190 ; 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): 47 ; 0.219 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 18 ; 0.191 ; 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): 1585 ; 1.003 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2490 ; 1.710 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1008 ; 2.188 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 876 ; 3.230 ; 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 : 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 : 1.40
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 3DXC COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 25-JUL-08.
REMARK 100 THE DEPOSITION ID IS D_1000048606.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 19-JUL-07
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 4.6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID14-2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.00
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 32612
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100
REMARK 200 RESOLUTION RANGE LOW (A) : 33.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 11.10
REMARK 200 R MERGE (I) : 0.06000
REMARK 200 R SYM (I) : 0.06000
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 28.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.21
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : 11.20
REMARK 200 R MERGE FOR SHELL (I) : 0.46500
REMARK 200 R SYM FOR SHELL (I) : 0.46500
REMARK 200 <I/SIGMA(I)> FOR SHELL : 4.700
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 (%): 65.93
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.61
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 3.2 M NACL,0.1 M SODIUM ACETATE , PH
REMARK 280 4.6, VAPOR DIFFUSION, 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 24.95000
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 49.90000
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 37.42500
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 62.37500
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 12.47500
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 300 REMARK: THE ASYMMETRIC UNIT CONTAINS TWO COPIES OF A PROTEIN
REMARK 300 PROTEIN COMPLEX (ONE BIOMOLECULE 1 BINDS ONE BIOMOLECULE 2).
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: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2100 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 8190 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -16.0 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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2120 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 7690 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -13.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D
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 534
REMARK 465 PRO A 535
REMARK 465 LYS A 536
REMARK 465 GLN A 667
REMARK 465 HIS A 668
REMARK 465 HIS A 669
REMARK 465 HIS A 670
REMARK 465 HIS A 671
REMARK 465 HIS A 672
REMARK 465 HIS A 673
REMARK 465 GLY B 661
REMARK 465 ALA B 662
REMARK 465 MET B 663
REMARK 465 ASP B 664
REMARK 465 ALA B 665
REMARK 465 GLN B 694
REMARK 465 ASN B 695
REMARK 465 ALA C 534
REMARK 465 PRO C 535
REMARK 465 LYS C 536
REMARK 465 ASN C 537
REMARK 465 GLU C 538
REMARK 465 LEU C 539
REMARK 465 VAL C 540
REMARK 465 GLN C 541
REMARK 465 LYS C 542
REMARK 465 SER C 666
REMARK 465 GLN C 667
REMARK 465 HIS C 668
REMARK 465 HIS C 669
REMARK 465 HIS C 670
REMARK 465 HIS C 671
REMARK 465 HIS C 672
REMARK 465 HIS C 673
REMARK 465 GLY D 661
REMARK 465 ALA D 662
REMARK 465 MET D 663
REMARK 465 ASP D 664
REMARK 465 ALA D 665
REMARK 465 ALA D 666
REMARK 465 MET D 693
REMARK 465 GLN D 694
REMARK 465 ASN D 695
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 PHE D 690 2.22 -67.14
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3DXD RELATED DB: PDB
REMARK 900 RELATED ID: 3DXE RELATED DB: PDB
DBREF 3DXC A 534 667 UNP O00213 APBB1_HUMAN 534 667
DBREF 3DXC B 664 695 UNP P05067 A4_HUMAN 739 770
DBREF 3DXC C 534 667 UNP O00213 APBB1_HUMAN 534 667
DBREF 3DXC D 664 695 UNP P05067 A4_HUMAN 739 770
SEQADV 3DXC HIS A 668 UNP O00213 EXPRESSION TAG
SEQADV 3DXC HIS A 669 UNP O00213 EXPRESSION TAG
SEQADV 3DXC HIS A 670 UNP O00213 EXPRESSION TAG
SEQADV 3DXC HIS A 671 UNP O00213 EXPRESSION TAG
SEQADV 3DXC HIS A 672 UNP O00213 EXPRESSION TAG
SEQADV 3DXC HIS A 673 UNP O00213 EXPRESSION TAG
SEQADV 3DXC GLY B 661 UNP P05067 EXPRESSION TAG
SEQADV 3DXC ALA B 662 UNP P05067 EXPRESSION TAG
SEQADV 3DXC MET B 663 UNP P05067 EXPRESSION TAG
SEQADV 3DXC HIS C 668 UNP O00213 EXPRESSION TAG
SEQADV 3DXC HIS C 669 UNP O00213 EXPRESSION TAG
SEQADV 3DXC HIS C 670 UNP O00213 EXPRESSION TAG
SEQADV 3DXC HIS C 671 UNP O00213 EXPRESSION TAG
SEQADV 3DXC HIS C 672 UNP O00213 EXPRESSION TAG
SEQADV 3DXC HIS C 673 UNP O00213 EXPRESSION TAG
SEQADV 3DXC GLY D 661 UNP P05067 EXPRESSION TAG
SEQADV 3DXC ALA D 662 UNP P05067 EXPRESSION TAG
SEQADV 3DXC MET D 663 UNP P05067 EXPRESSION TAG
SEQRES 1 A 140 ALA PRO LYS ASN GLU LEU VAL GLN LYS PHE GLN VAL TYR
SEQRES 2 A 140 TYR LEU GLY ASN VAL PRO VAL ALA LYS PRO VAL GLY VAL
SEQRES 3 A 140 ASP VAL ILE ASN GLY ALA LEU GLU SER VAL LEU SER SER
SEQRES 4 A 140 SER SER ARG GLU GLN TRP THR PRO SER HIS VAL SER VAL
SEQRES 5 A 140 ALA PRO ALA THR LEU THR ILE LEU HIS GLN GLN THR GLU
SEQRES 6 A 140 ALA VAL LEU GLY GLU CYS ARG VAL ARG PHE LEU SER PHE
SEQRES 7 A 140 LEU ALA VAL GLY ARG ASP VAL HIS THR PHE ALA PHE ILE
SEQRES 8 A 140 MET ALA ALA GLY PRO ALA SER PHE CYS CYS HIS MET PHE
SEQRES 9 A 140 TRP CYS GLU PRO ASN ALA ALA SER LEU SER GLU ALA VAL
SEQRES 10 A 140 GLN ALA ALA CYS MET LEU ARG TYR GLN LYS CYS LEU ASP
SEQRES 11 A 140 ALA ARG SER GLN HIS HIS HIS HIS HIS HIS
SEQRES 1 B 35 GLY ALA MET ASP ALA ALA VAL THR PRO GLU GLU ARG HIS
SEQRES 2 B 35 LEU SER LYS MET GLN GLN ASN GLY TYR GLU ASN PRO THR
SEQRES 3 B 35 TYR LYS PHE PHE GLU GLN MET GLN ASN
SEQRES 1 C 140 ALA PRO LYS ASN GLU LEU VAL GLN LYS PHE GLN VAL TYR
SEQRES 2 C 140 TYR LEU GLY ASN VAL PRO VAL ALA LYS PRO VAL GLY VAL
SEQRES 3 C 140 ASP VAL ILE ASN GLY ALA LEU GLU SER VAL LEU SER SER
SEQRES 4 C 140 SER SER ARG GLU GLN TRP THR PRO SER HIS VAL SER VAL
SEQRES 5 C 140 ALA PRO ALA THR LEU THR ILE LEU HIS GLN GLN THR GLU
SEQRES 6 C 140 ALA VAL LEU GLY GLU CYS ARG VAL ARG PHE LEU SER PHE
SEQRES 7 C 140 LEU ALA VAL GLY ARG ASP VAL HIS THR PHE ALA PHE ILE
SEQRES 8 C 140 MET ALA ALA GLY PRO ALA SER PHE CYS CYS HIS MET PHE
SEQRES 9 C 140 TRP CYS GLU PRO ASN ALA ALA SER LEU SER GLU ALA VAL
SEQRES 10 C 140 GLN ALA ALA CYS MET LEU ARG TYR GLN LYS CYS LEU ASP
SEQRES 11 C 140 ALA ARG SER GLN HIS HIS HIS HIS HIS HIS
SEQRES 1 D 35 GLY ALA MET ASP ALA ALA VAL THR PRO GLU GLU ARG HIS
SEQRES 2 D 35 LEU SER LYS MET GLN GLN ASN GLY TYR GLU ASN PRO THR
SEQRES 3 D 35 TYR LYS PHE PHE GLU GLN MET GLN ASN
FORMUL 5 HOH *236(H2 O)
HELIX 1 1 GLY A 558 SER A 572 1 15
HELIX 2 2 SER A 573 TRP A 578 5 6
HELIX 3 3 ALA A 643 SER A 666 1 24
HELIX 4 4 THR B 668 ASN B 680 1 13
HELIX 5 5 ASN B 684 MET B 693 1 10
HELIX 6 6 GLY C 558 SER C 572 1 15
HELIX 7 7 SER C 574 TRP C 578 5 5
HELIX 8 8 ALA C 643 ALA C 664 1 22
HELIX 9 9 THR D 668 ASN D 680 1 13
HELIX 10 10 ASN D 684 PHE D 690 1 7
SHEET 1 A 8 VAL A 600 ARG A 605 0
SHEET 2 A 8 THR A 589 HIS A 594 -1 N ILE A 592 O LEU A 601
SHEET 3 A 8 THR A 579 VAL A 585 -1 N SER A 584 O THR A 591
SHEET 4 A 8 VAL A 540 VAL A 553 -1 N TYR A 547 O THR A 579
SHEET 5 A 8 SER A 631 TRP A 638 -1 O CYS A 634 N VAL A 551
SHEET 6 A 8 THR A 620 GLY A 628 -1 N MET A 625 O CYS A 633
SHEET 7 A 8 LEU A 609 VAL A 614 -1 N PHE A 611 O ILE A 624
SHEET 8 A 8 TYR B 682 GLU B 683 -1 O TYR B 682 N LEU A 612
SHEET 1 B 8 VAL C 600 ARG C 605 0
SHEET 2 B 8 THR C 589 HIS C 594 -1 N ILE C 592 O LEU C 601
SHEET 3 B 8 THR C 579 VAL C 585 -1 N SER C 584 O THR C 591
SHEET 4 B 8 GLN C 544 VAL C 553 -1 N TYR C 547 O THR C 579
SHEET 5 B 8 SER C 631 GLU C 640 -1 O CYS C 634 N VAL C 551
SHEET 6 B 8 THR C 620 GLY C 628 -1 N PHE C 623 O HIS C 635
SHEET 7 B 8 LEU C 609 VAL C 614 -1 N PHE C 611 O ILE C 624
SHEET 8 B 8 TYR D 682 GLU D 683 -1 O TYR D 682 N LEU C 612
CISPEP 1 GLU A 640 PRO A 641 0 5.97
CISPEP 2 GLU C 640 PRO C 641 0 0.85
CRYST1 114.320 114.320 74.850 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 0.008747 0.005050 0.000000 0.00000
SCALE2 0.000000 0.010101 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013360 0.00000
(ATOM LINES ARE NOT SHOWN.)
END