HEADER PROTEIN TRANSPORT/PROTEIN BINDING 23-AUG-13 4MDR
TITLE CRYSTAL STRUCTURE OF ADAPTOR PROTEIN COMPLEX 4 (AP-4) MU4 SUBUNIT C-
TITLE 2 TERMINAL DOMAIN D190A MUTANT, IN COMPLEX WITH A SORTING PEPTIDE FROM
TITLE 3 THE AMYLOID PRECURSOR PROTEIN (APP)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: AP-4 COMPLEX SUBUNIT MU-1;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: C-TERMINUS, RESIDUES 160-453;
COMPND 5 SYNONYM: AP-4 ADAPTER COMPLEX MU SUBUNIT, ADAPTER-RELATED PROTEIN
COMPND 6 COMPLEX 4 MU-1 SUBUNIT, MU SUBUNIT OF AP-4, MU-ADAPTIN-RELATED
COMPND 7 PROTEIN 2, MU-ARP2, MU4-ADAPTIN, MU4;
COMPND 8 ENGINEERED: YES;
COMPND 9 MUTATION: YES;
COMPND 10 MOL_ID: 2;
COMPND 11 MOLECULE: AMYLOID BETA A4 PROTEIN;
COMPND 12 CHAIN: B;
COMPND 13 FRAGMENT: C-TERMINUS, RESIDUES 761-767;
COMPND 14 SYNONYM: ABPP, APPI, APP, ALZHEIMER DISEASE AMYLOID PROTEIN, CEREBRAL
COMPND 15 VASCULAR AMYLOID PEPTIDE, CVAP, PREA4, PROTEASE NEXIN-II, PN-II, N-
COMPND 16 APP, SOLUBLE APP-ALPHA, S-APP-ALPHA, SOLUBLE APP-BETA, S-APP-BETA,
COMPND 17 C99, BETA-AMYLOID PROTEIN 42, BETA-APP42, BETA-AMYLOID PROTEIN 40,
COMPND 18 BETA-APP40, C83, P3(42), P3(40), C80, GAMMA-SECRETASE C-TERMINAL
COMPND 19 FRAGMENT 59, AMYLOID INTRACELLULAR DOMAIN 59, AICD-59, AID(59),
COMPND 20 GAMMA-CTF(59), GAMMA-SECRETASE C-TERMINAL FRAGMENT 57, AMYLOID
COMPND 21 INTRACELLULAR DOMAIN 57, AICD-57, AID(57), GAMMA-CTF(57), GAMMA-
COMPND 22 SECRETASE C-TERMINAL FRAGMENT 50, AMYLOID INTRACELLULAR DOMAIN 50,
COMPND 23 AICD-50, AID(50), GAMMA-CTF(50), C31;
COMPND 24 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: AP4M1, MUARP2;
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;
SOURCE 13 OTHER_DETAILS: THIS SEQUENCE OCCURS NATURALLY IN HUMANS
KEYWDS IMMUNOGLOBULIN-LIKE BETA-SANDWICH, ADAPTOR PROTEIN COMPLEX, GOLGI
KEYWDS 2 APPARATUS, SORTING SIGNAL RECOGNITION, ALZHEIMER'S DISEASE, AMYLOID
KEYWDS 3 PRECURSOR PROTEIN, PROTEIN TRANSPORT-PROTEIN BINDING COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR B.H.ROSS,Y.LIN,E.A.CORALES,P.V.BURGOS,G.A.MARDONES
REVDAT 2 20-SEP-23 4MDR 1 SEQADV
REVDAT 1 12-MAR-14 4MDR 0
JRNL AUTH B.H.ROSS,Y.LIN,E.A.CORALES,P.V.BURGOS,G.A.MARDONES
JRNL TITL STRUCTURAL AND FUNCTIONAL CHARACTERIZATION OF CARGO-BINDING
JRNL TITL 2 SITES ON THE MU 4-SUBUNIT OF ADAPTOR PROTEIN COMPLEX 4.
JRNL REF PLOS ONE V. 9 88147 2014
JRNL REFN ESSN 1932-6203
JRNL PMID 24498434
JRNL DOI 10.1371/JOURNAL.PONE.0088147
REMARK 2
REMARK 2 RESOLUTION. 1.85 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0088
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) : 1.85
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.4
REMARK 3 NUMBER OF REFLECTIONS : 24999
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) : 0.216
REMARK 3 R VALUE (WORKING SET) : 0.214
REMARK 3 FREE R VALUE : 0.260
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1283
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) : 1.85
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.90
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1354
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 75.83
REMARK 3 BIN R VALUE (WORKING SET) : 0.2700
REMARK 3 BIN FREE R VALUE SET COUNT : 77
REMARK 3 BIN FREE R VALUE : 0.3210
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2001
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 97
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 36.57
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.58000
REMARK 3 B22 (A**2) : 0.41000
REMARK 3 B33 (A**2) : -1.21000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 1.38000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.150
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.147
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.109
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.586
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.954
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.926
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2043 ; 0.022 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2759 ; 2.046 ; 1.986
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 248 ; 7.636 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 93 ;33.210 ;22.581
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 359 ;15.224 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 21 ;27.138 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 306 ; 0.143 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1537 ; 0.010 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
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): 1254 ; 1.577 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2019 ; 2.823 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 789 ; 4.019 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 740 ; 6.731 ; 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 U VALUES : REFINED INDIVIDUALLY
REMARK 4
REMARK 4 4MDR COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-SEP-13.
REMARK 100 THE DEPOSITION ID IS D_1000081782.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-NOV-09
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 22-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0000
REMARK 200 MONOCHROMATOR : SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 300 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 25043
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.840
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.1
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.07700
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 15.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.84
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.91
REMARK 200 COMPLETENESS FOR SHELL (%) : 75.5
REMARK 200 DATA REDUNDANCY IN SHELL : 2.90
REMARK 200 R MERGE FOR SHELL (I) : 0.35000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.700
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: PDB ENTRY 3L81
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 44.41
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.21
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 15% PEG 6000, 3% TRIMETHYLAMINE N
REMARK 280 -OXIDE DIHYDRATE, 0.1M HEPES, PH 7.0, VAPOR DIFFUSION, HANGING
REMARK 280 DROP, TEMPERATURE 295.0K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y+1/2,-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 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 28.36450
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
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 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 860 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 13330 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -3.0 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 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 A 153
REMARK 465 ALA A 154
REMARK 465 MET A 155
REMARK 465 ASP A 156
REMARK 465 PRO A 157
REMARK 465 GLU A 158
REMARK 465 PHE A 159
REMARK 465 GLN A 160
REMARK 465 GLN A 161
REMARK 465 SER A 162
REMARK 465 LYS A 163
REMARK 465 VAL A 164
REMARK 465 ALA A 165
REMARK 465 PRO A 166
REMARK 465 SER A 167
REMARK 465 SER A 168
REMARK 465 ALA A 169
REMARK 465 ALA A 170
REMARK 465 SER A 171
REMARK 465 ARG A 172
REMARK 465 PRO A 173
REMARK 465 VAL A 174
REMARK 465 LEU A 175
REMARK 465 SER A 176
REMARK 465 SER A 177
REMARK 465 ARG A 178
REMARK 465 SER A 179
REMARK 465 ASP A 180
REMARK 465 GLN A 181
REMARK 465 SER A 182
REMARK 465 GLN A 183
REMARK 465 LYS A 184
REMARK 465 GLY A 384
REMARK 465 PRO A 385
REMARK 465 PRO A 386
REMARK 465 GLY A 387
REMARK 465 PRO A 388
REMARK 465 PRO A 389
REMARK 465 SER A 390
REMARK 465 HIS A 391
REMARK 465 GLY A 392
REMARK 465 LEU A 393
REMARK 465 SER A 394
REMARK 465 THR A 395
REMARK 465 SER A 396
REMARK 465 ALA A 397
REMARK 465 SER A 398
REMARK 465 PRO A 399
REMARK 465 PHE A 428
REMARK 465 ARG A 429
REMARK 465 PRO A 430
REMARK 465 SER A 431
REMARK 465 GLY A 432
REMARK 465 ASN A 433
REMARK 465 ALA A 434
REMARK 465 ASN A 435
REMARK 465 GLU B 683
REMARK 465 ASN B 684
REMARK 465 PRO B 685
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 A 246 C - N - CA ANGL. DEV. = -9.8 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 THR A 231 122.97 -34.87
REMARK 500 ALA A 448 56.35 -146.34
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN B OF AMYLOID BETA A4
REMARK 800 PROTEIN
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3L81 RELATED DB: PDB
REMARK 900 WILD-TYPE PROTEIN COMPLEXED WITH THE SAME PEPTIDE
DBREF 4MDR A 160 453 UNP O00189 AP4M1_HUMAN 160 453
DBREF 4MDR B 683 692 UNP P05067 A4_HUMAN 758 767
SEQADV 4MDR GLY A 153 UNP O00189 EXPRESSION TAG
SEQADV 4MDR ALA A 154 UNP O00189 EXPRESSION TAG
SEQADV 4MDR MET A 155 UNP O00189 EXPRESSION TAG
SEQADV 4MDR ASP A 156 UNP O00189 EXPRESSION TAG
SEQADV 4MDR PRO A 157 UNP O00189 EXPRESSION TAG
SEQADV 4MDR GLU A 158 UNP O00189 EXPRESSION TAG
SEQADV 4MDR PHE A 159 UNP O00189 EXPRESSION TAG
SEQADV 4MDR ALA A 190 UNP O00189 ASP 190 ENGINEERED MUTATION
SEQADV 4MDR SER A 235 UNP O00189 CYS 235 ENGINEERED MUTATION
SEQADV 4MDR SER A 431 UNP O00189 CYS 431 ENGINEERED MUTATION
SEQRES 1 A 301 GLY ALA MET ASP PRO GLU PHE GLN GLN SER LYS VAL ALA
SEQRES 2 A 301 PRO SER SER ALA ALA SER ARG PRO VAL LEU SER SER ARG
SEQRES 3 A 301 SER ASP GLN SER GLN LYS ASN GLU VAL PHE LEU ALA VAL
SEQRES 4 A 301 VAL GLU ARG LEU SER VAL LEU ILE ALA SER ASN GLY SER
SEQRES 5 A 301 LEU LEU LYS VAL ASP VAL GLN GLY GLU ILE ARG LEU LYS
SEQRES 6 A 301 SER PHE LEU PRO SER GLY SER GLU MET ARG ILE GLY LEU
SEQRES 7 A 301 THR GLU GLU PHE SER VAL GLY LYS SER GLU LEU ARG GLY
SEQRES 8 A 301 TYR GLY PRO GLY ILE ARG VAL ASP GLU VAL SER PHE HIS
SEQRES 9 A 301 SER SER VAL ASN LEU ASP GLU PHE GLU SER HIS ARG ILE
SEQRES 10 A 301 LEU ARG LEU GLN PRO PRO GLN GLY GLU LEU THR VAL MET
SEQRES 11 A 301 ARG TYR GLN LEU SER ASP ASP LEU PRO SER PRO LEU PRO
SEQRES 12 A 301 PHE ARG LEU PHE PRO SER VAL GLN TRP ASP ARG GLY SER
SEQRES 13 A 301 GLY ARG LEU GLN VAL TYR LEU LYS LEU ARG CYS ASP LEU
SEQRES 14 A 301 LEU SER LYS SER GLN ALA LEU ASN VAL ARG LEU HIS LEU
SEQRES 15 A 301 PRO LEU PRO ARG GLY VAL VAL SER LEU SER GLN GLU LEU
SEQRES 16 A 301 SER SER PRO GLU GLN LYS ALA GLU LEU ALA GLU GLY ALA
SEQRES 17 A 301 LEU ARG TRP ASP LEU PRO ARG VAL GLN GLY GLY SER GLN
SEQRES 18 A 301 LEU SER GLY LEU PHE GLN MET ASP VAL PRO GLY PRO PRO
SEQRES 19 A 301 GLY PRO PRO SER HIS GLY LEU SER THR SER ALA SER PRO
SEQRES 20 A 301 LEU GLY LEU GLY PRO ALA SER LEU SER PHE GLU LEU PRO
SEQRES 21 A 301 ARG HIS THR CYS SER GLY LEU GLN VAL ARG PHE LEU ARG
SEQRES 22 A 301 LEU ALA PHE ARG PRO SER GLY ASN ALA ASN PRO HIS LYS
SEQRES 23 A 301 TRP VAL ARG HIS LEU SER HIS SER ASP ALA TYR VAL ILE
SEQRES 24 A 301 ARG ILE
SEQRES 1 B 10 GLU ASN PRO THR TYR LYS PHE PHE GLU GLN
FORMUL 3 HOH *97(H2 O)
HELIX 1 1 GLU A 263 ARG A 268 1 6
SHEET 1 A 4 LYS A 353 ALA A 357 0
SHEET 2 A 4 ALA A 360 LEU A 365 -1 O ASP A 364 N LYS A 353
SHEET 3 A 4 GLN A 326 PRO A 335 -1 N LEU A 332 O TRP A 363
SHEET 4 A 4 VAL A 368 GLN A 369 -1 O VAL A 368 N ALA A 327
SHEET 1 B10 LYS A 353 ALA A 357 0
SHEET 2 B10 ALA A 360 LEU A 365 -1 O ASP A 364 N LYS A 353
SHEET 3 B10 GLN A 326 PRO A 335 -1 N LEU A 332 O TRP A 363
SHEET 4 B10 ALA A 405 PRO A 412 -1 O GLU A 410 N LEU A 328
SHEET 5 B10 HIS A 437 ILE A 451 -1 O SER A 444 N LEU A 411
SHEET 6 B10 GLU A 186 ILE A 199 1 N LEU A 195 O HIS A 445
SHEET 7 B10 LEU A 205 SER A 218 -1 O LEU A 206 N LEU A 198
SHEET 8 B10 GLY A 277 LEU A 286 -1 O LEU A 279 N LEU A 216
SHEET 9 B10 GLU A 252 HIS A 256 -1 N HIS A 256 O VAL A 281
SHEET 10 B10 LYS B 688 PHE B 690 1 O LYS B 688 N PHE A 255
SHEET 1 C 3 ILE A 269 LEU A 272 0
SHEET 2 C 3 MET A 226 LEU A 230 -1 N MET A 226 O LEU A 272
SHEET 3 C 3 VAL A 421 LEU A 426 -1 O ARG A 422 N GLY A 229
SHEET 1 D 2 SER A 235 VAL A 236 0
SHEET 2 D 2 ARG A 249 VAL A 250 1 O VAL A 250 N SER A 235
SHEET 1 E 4 PHE A 296 TRP A 304 0
SHEET 2 E 4 ARG A 310 CYS A 319 -1 O LYS A 316 N PHE A 299
SHEET 3 E 4 GLN A 373 ASP A 381 -1 O PHE A 378 N VAL A 313
SHEET 4 E 4 VAL A 341 LEU A 347 -1 N LEU A 343 O GLN A 379
CISPEP 1 ARG A 306 GLY A 307 0 15.93
CISPEP 2 LEU A 400 GLY A 401 0 16.86
CISPEP 3 GLY A 403 PRO A 404 0 1.77
SITE 1 AC1 14 SER A 254 PHE A 255 HIS A 256 SER A 257
SITE 2 AC1 14 LEU A 261 GLU A 265 THR A 280 ARG A 283
SITE 3 AC1 14 ARG A 297 PHE A 299 HOH B 701 HOH B 702
SITE 4 AC1 14 HOH B 703 HOH B 704
CRYST1 46.507 56.729 60.180 90.00 106.67 90.00 P 1 21 1 2
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 0.021502 0.000000 0.006438 0.00000
SCALE2 0.000000 0.017628 0.000000 0.00000
SCALE3 0.000000 0.000000 0.017346 0.00000
(ATOM LINES ARE NOT SHOWN.)
END