HEADER MEMBRANE PROTEIN/SIGNALING PROTEIN 19-APR-11 3RL8
TITLE CRYSTAL STRUCTURE OF HDLG1-PDZ2 COMPLEXED WITH APC
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DISKS LARGE HOMOLOG 1;
COMPND 3 CHAIN: A, B, C, D, E;
COMPND 4 FRAGMENT: UNP RESIDUES 315-410;
COMPND 5 SYNONYM: SYNAPSE-ASSOCIATED PROTEIN 97, SAP-97, SAP97, HDLG;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: 11-MER PEPTIDE FROM ADENOMATOUS POLYPOSIS COLI PROTEIN;
COMPND 9 CHAIN: F;
COMPND 10 SYNONYM: APC-C11;
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: DLG1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET28A;
SOURCE 11 MOL_ID: 2;
SOURCE 12 SYNTHETIC: YES;
SOURCE 13 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 14 ORGANISM_COMMON: HUMAN;
SOURCE 15 ORGANISM_TAXID: 9606;
SOURCE 16 OTHER_DETAILS: THIS SEQUENCE OCCURS NATURALLY IN HUMANS
KEYWDS PDZ-LIGAND COMPLEX, MEMBRANE PROTEIN-SIGNALING PROTEIN COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR Z.ZHANG,H.LI,G.WU
REVDAT 3 01-NOV-23 3RL8 1 SEQADV
REVDAT 2 21-DEC-16 3RL8 1 TITLE
REVDAT 1 14-DEC-11 3RL8 0
JRNL AUTH Z.ZHANG,H.LI,L.CHEN,X.LU,J.ZHANG,P.XU,K.LIN,G.WU
JRNL TITL MOLECULAR BASIS FOR THE RECOGNITION OF ADENOMATOUS POLYPOSIS
JRNL TITL 2 COLI BY THE DISCS LARGE 1 PROTEIN.
JRNL REF PLOS ONE V. 6 23507 2011
JRNL REFN ESSN 1932-6203
JRNL PMID 21858148
JRNL DOI 10.1371/JOURNAL.PONE.0023507
REMARK 2
REMARK 2 RESOLUTION. 2.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0102
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) : 2.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 30711
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) : 0.206
REMARK 3 R VALUE (WORKING SET) : 0.204
REMARK 3 FREE R VALUE : 0.245
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1545
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) : 2.20
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.26
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2108
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.29
REMARK 3 BIN R VALUE (WORKING SET) : 0.2240
REMARK 3 BIN FREE R VALUE SET COUNT : 126
REMARK 3 BIN FREE R VALUE : 0.2800
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3507
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 286
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 38.82
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -2.51000
REMARK 3 B22 (A**2) : 0.37000
REMARK 3 B33 (A**2) : 2.05000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.23000
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): 0.198
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.139
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 11.851
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.939
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.916
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3576 ; 0.012 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4819 ; 1.306 ; 1.981
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 469 ; 5.954 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 126 ;40.406 ;26.905
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 675 ;15.885 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 569 ; 0.093 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2552 ; 0.005 ; 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): 2312 ; 0.449 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3714 ; 0.842 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1264 ; 1.508 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1103 ; 2.529 ; 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 : A B C D E
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 317 A 405 4
REMARK 3 1 B 317 B 405 4
REMARK 3 1 C 317 C 405 4
REMARK 3 1 D 317 D 405 4
REMARK 3 1 E 317 E 405 4
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 1 A (A): 653 ; 0.570 ; 0.500
REMARK 3 MEDIUM POSITIONAL 1 B (A): 653 ; 0.550 ; 0.500
REMARK 3 MEDIUM POSITIONAL 1 C (A): 653 ; 0.750 ; 0.500
REMARK 3 MEDIUM POSITIONAL 1 D (A): 653 ; 0.450 ; 0.500
REMARK 3 MEDIUM POSITIONAL 1 E (A): 653 ; 0.370 ; 0.500
REMARK 3 MEDIUM THERMAL 1 A (A**2): 653 ; 1.000 ; 2.000
REMARK 3 MEDIUM THERMAL 1 B (A**2): 653 ; 0.960 ; 2.000
REMARK 3 MEDIUM THERMAL 1 C (A**2): 653 ; 0.790 ; 2.000
REMARK 3 MEDIUM THERMAL 1 D (A**2): 653 ; 0.620 ; 2.000
REMARK 3 MEDIUM THERMAL 1 E (A**2): 653 ; 0.520 ; 2.000
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 7
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 316 A 409
REMARK 3 ORIGIN FOR THE GROUP (A): 20.4883 5.4581 42.0125
REMARK 3 T TENSOR
REMARK 3 T11: 0.1693 T22: 0.0260
REMARK 3 T33: 0.1462 T12: -0.0048
REMARK 3 T13: -0.0487 T23: -0.0154
REMARK 3 L TENSOR
REMARK 3 L11: 8.0496 L22: 3.2562
REMARK 3 L33: 1.6170 L12: -0.6752
REMARK 3 L13: -1.1211 L23: -0.0178
REMARK 3 S TENSOR
REMARK 3 S11: -0.0203 S12: 0.2372 S13: -0.1639
REMARK 3 S21: -0.2210 S22: 0.0673 S23: 0.2234
REMARK 3 S31: 0.2861 S32: 0.0381 S33: -0.0470
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 316 B 405
REMARK 3 ORIGIN FOR THE GROUP (A): 52.0523 6.0989 41.1407
REMARK 3 T TENSOR
REMARK 3 T11: 0.1177 T22: 0.0206
REMARK 3 T33: 0.1418 T12: 0.0181
REMARK 3 T13: -0.0063 T23: 0.0230
REMARK 3 L TENSOR
REMARK 3 L11: 11.3171 L22: 4.4867
REMARK 3 L33: 1.2439 L12: 1.4452
REMARK 3 L13: 1.6766 L23: 0.3877
REMARK 3 S TENSOR
REMARK 3 S11: -0.0882 S12: 0.3217 S13: 0.3777
REMARK 3 S21: 0.0684 S22: 0.0426 S23: -0.2013
REMARK 3 S31: -0.2369 S32: -0.0518 S33: 0.0457
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 316 C 410
REMARK 3 ORIGIN FOR THE GROUP (A): 29.2410 8.7956 63.8628
REMARK 3 T TENSOR
REMARK 3 T11: 0.1804 T22: 0.2566
REMARK 3 T33: 0.1221 T12: -0.0156
REMARK 3 T13: 0.0185 T23: 0.0065
REMARK 3 L TENSOR
REMARK 3 L11: 3.2474 L22: 2.6480
REMARK 3 L33: 5.6620 L12: -0.0316
REMARK 3 L13: 1.5558 L23: -0.0373
REMARK 3 S TENSOR
REMARK 3 S11: 0.0438 S12: -0.6426 S13: -0.1395
REMARK 3 S21: 0.1881 S22: 0.0046 S23: 0.1983
REMARK 3 S31: 0.1636 S32: -0.4782 S33: -0.0484
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 316 D 409
REMARK 3 ORIGIN FOR THE GROUP (A): 44.0424 20.1692 79.7109
REMARK 3 T TENSOR
REMARK 3 T11: 0.1507 T22: 0.3888
REMARK 3 T33: 0.1554 T12: 0.0221
REMARK 3 T13: -0.0051 T23: -0.0482
REMARK 3 L TENSOR
REMARK 3 L11: 12.0597 L22: 4.0904
REMARK 3 L33: 3.9069 L12: 0.9363
REMARK 3 L13: 2.2009 L23: 1.5415
REMARK 3 S TENSOR
REMARK 3 S11: 0.0115 S12: -0.9700 S13: 0.3414
REMARK 3 S21: 0.1897 S22: -0.1347 S23: -0.1176
REMARK 3 S31: -0.0119 S32: -0.0352 S33: 0.1232
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : E 316 E 405
REMARK 3 ORIGIN FOR THE GROUP (A): 8.1057 20.7229 79.1349
REMARK 3 T TENSOR
REMARK 3 T11: 0.2144 T22: 0.4815
REMARK 3 T33: 0.3167 T12: 0.0145
REMARK 3 T13: 0.0204 T23: -0.0461
REMARK 3 L TENSOR
REMARK 3 L11: 19.4618 L22: 1.5905
REMARK 3 L33: 4.6954 L12: 1.2878
REMARK 3 L13: -2.6299 L23: 0.1915
REMARK 3 S TENSOR
REMARK 3 S11: -0.0960 S12: -0.0081 S13: 0.7736
REMARK 3 S21: -0.1065 S22: 0.2362 S23: 0.3158
REMARK 3 S31: 0.1088 S32: 0.0045 S33: -0.1402
REMARK 3
REMARK 3 TLS GROUP : 6
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : F 2838 F 2843
REMARK 3 ORIGIN FOR THE GROUP (A): 57.1838 -4.0696 48.9956
REMARK 3 T TENSOR
REMARK 3 T11: 0.3883 T22: 0.2755
REMARK 3 T33: 0.3986 T12: 0.0947
REMARK 3 T13: -0.1830 T23: 0.0141
REMARK 3 L TENSOR
REMARK 3 L11: 46.3981 L22: 50.4297
REMARK 3 L33: 32.8998 L12: -33.7563
REMARK 3 L13: 17.2550 L23: -0.2484
REMARK 3 S TENSOR
REMARK 3 S11: -0.6677 S12: -0.6898 S13: -1.1980
REMARK 3 S21: 2.8535 S22: 1.5932 S23: -1.6130
REMARK 3 S31: 1.4764 S32: 1.8893 S33: -0.9255
REMARK 3
REMARK 3 TLS GROUP : 7
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 3 A 286
REMARK 3 ORIGIN FOR THE GROUP (A): 32.5764 10.3953 55.8690
REMARK 3 T TENSOR
REMARK 3 T11: 0.3355 T22: 0.2545
REMARK 3 T33: 0.3235 T12: 0.0127
REMARK 3 T13: -0.0131 T23: 0.0030
REMARK 3 L TENSOR
REMARK 3 L11: 1.3384 L22: 0.2511
REMARK 3 L33: 0.3011 L12: 0.0411
REMARK 3 L13: -0.1060 L23: 0.0232
REMARK 3 S TENSOR
REMARK 3 S11: -0.0026 S12: -0.3100 S13: 0.0105
REMARK 3 S21: 0.0264 S22: -0.0271 S23: 0.0087
REMARK 3 S31: -0.0142 S32: -0.0245 S33: 0.0297
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: WITH TLS ADDED
REMARK 4
REMARK 4 3RL8 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 28-APR-11.
REMARK 100 THE DEPOSITION ID IS D_1000065070.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 30-NOV-10
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRF
REMARK 200 BEAMLINE : BL17U
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97916
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 30730
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.200
REMARK 200 RESOLUTION RANGE LOW (A) : 85.380
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 6.000
REMARK 200 R MERGE (I) : 0.08800
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 17.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.28
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : 6.00
REMARK 200 R MERGE FOR SHELL (I) : 0.21600
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: 1ZOK
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 52.65
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.60
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.8M NA2HPO4, 0.9M KH2PO4, PH 7.5,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 287K
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 26.25100
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: HEXAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, 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 MET A 306
REMARK 465 GLY A 307
REMARK 465 HIS A 308
REMARK 465 HIS A 309
REMARK 465 HIS A 310
REMARK 465 HIS A 311
REMARK 465 HIS A 312
REMARK 465 HIS A 313
REMARK 465 MET A 314
REMARK 465 GLU A 315
REMARK 465 MET A 410
REMARK 465 MET B 306
REMARK 465 GLY B 307
REMARK 465 HIS B 308
REMARK 465 HIS B 309
REMARK 465 HIS B 310
REMARK 465 HIS B 311
REMARK 465 HIS B 312
REMARK 465 HIS B 313
REMARK 465 MET B 314
REMARK 465 GLU B 315
REMARK 465 THR B 406
REMARK 465 SER B 407
REMARK 465 MET B 408
REMARK 465 TYR B 409
REMARK 465 MET B 410
REMARK 465 MET C 306
REMARK 465 GLY C 307
REMARK 465 HIS C 308
REMARK 465 HIS C 309
REMARK 465 HIS C 310
REMARK 465 HIS C 311
REMARK 465 HIS C 312
REMARK 465 HIS C 313
REMARK 465 MET C 314
REMARK 465 GLU C 315
REMARK 465 MET D 306
REMARK 465 GLY D 307
REMARK 465 HIS D 308
REMARK 465 HIS D 309
REMARK 465 HIS D 310
REMARK 465 HIS D 311
REMARK 465 HIS D 312
REMARK 465 HIS D 313
REMARK 465 MET D 314
REMARK 465 GLU D 315
REMARK 465 MET D 410
REMARK 465 MET E 306
REMARK 465 GLY E 307
REMARK 465 HIS E 308
REMARK 465 HIS E 309
REMARK 465 HIS E 310
REMARK 465 HIS E 311
REMARK 465 HIS E 312
REMARK 465 HIS E 313
REMARK 465 MET E 314
REMARK 465 GLU E 315
REMARK 465 THR E 406
REMARK 465 SER E 407
REMARK 465 MET E 408
REMARK 465 TYR E 409
REMARK 465 MET E 410
REMARK 465 ARG F 2833
REMARK 465 HIS F 2834
REMARK 465 SER F 2835
REMARK 465 GLY F 2836
REMARK 465 SER F 2837
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 C 410 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 ASN A 339 56.83 -143.85
REMARK 500 ASN A 375 -127.02 49.84
REMARK 500 ASN A 393 41.99 -79.16
REMARK 500 SER A 395 -149.27 -103.59
REMARK 500 ASN B 339 49.43 -151.57
REMARK 500 ASN C 339 47.23 -144.26
REMARK 500 TYR C 409 -8.52 82.09
REMARK 500 ASN D 339 51.14 -140.83
REMARK 500 ASN D 376 -6.14 74.59
REMARK 500 SER D 407 -154.70 -106.63
REMARK 500 ASN E 339 56.52 -141.28
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3RL7 RELATED DB: PDB
DBREF 3RL8 A 315 410 UNP Q12959 DLG1_HUMAN 315 410
DBREF 3RL8 B 315 410 UNP Q12959 DLG1_HUMAN 315 410
DBREF 3RL8 C 315 410 UNP Q12959 DLG1_HUMAN 315 410
DBREF 3RL8 D 315 410 UNP Q12959 DLG1_HUMAN 315 410
DBREF 3RL8 E 315 410 UNP Q12959 DLG1_HUMAN 315 410
DBREF 3RL8 F 2833 2843 UNP P25054 APC_HUMAN 2833 2843
SEQADV 3RL8 MET A 306 UNP Q12959 EXPRESSION TAG
SEQADV 3RL8 GLY A 307 UNP Q12959 EXPRESSION TAG
SEQADV 3RL8 HIS A 308 UNP Q12959 EXPRESSION TAG
SEQADV 3RL8 HIS A 309 UNP Q12959 EXPRESSION TAG
SEQADV 3RL8 HIS A 310 UNP Q12959 EXPRESSION TAG
SEQADV 3RL8 HIS A 311 UNP Q12959 EXPRESSION TAG
SEQADV 3RL8 HIS A 312 UNP Q12959 EXPRESSION TAG
SEQADV 3RL8 HIS A 313 UNP Q12959 EXPRESSION TAG
SEQADV 3RL8 MET A 314 UNP Q12959 EXPRESSION TAG
SEQADV 3RL8 MET B 306 UNP Q12959 EXPRESSION TAG
SEQADV 3RL8 GLY B 307 UNP Q12959 EXPRESSION TAG
SEQADV 3RL8 HIS B 308 UNP Q12959 EXPRESSION TAG
SEQADV 3RL8 HIS B 309 UNP Q12959 EXPRESSION TAG
SEQADV 3RL8 HIS B 310 UNP Q12959 EXPRESSION TAG
SEQADV 3RL8 HIS B 311 UNP Q12959 EXPRESSION TAG
SEQADV 3RL8 HIS B 312 UNP Q12959 EXPRESSION TAG
SEQADV 3RL8 HIS B 313 UNP Q12959 EXPRESSION TAG
SEQADV 3RL8 MET B 314 UNP Q12959 EXPRESSION TAG
SEQADV 3RL8 MET C 306 UNP Q12959 EXPRESSION TAG
SEQADV 3RL8 GLY C 307 UNP Q12959 EXPRESSION TAG
SEQADV 3RL8 HIS C 308 UNP Q12959 EXPRESSION TAG
SEQADV 3RL8 HIS C 309 UNP Q12959 EXPRESSION TAG
SEQADV 3RL8 HIS C 310 UNP Q12959 EXPRESSION TAG
SEQADV 3RL8 HIS C 311 UNP Q12959 EXPRESSION TAG
SEQADV 3RL8 HIS C 312 UNP Q12959 EXPRESSION TAG
SEQADV 3RL8 HIS C 313 UNP Q12959 EXPRESSION TAG
SEQADV 3RL8 MET C 314 UNP Q12959 EXPRESSION TAG
SEQADV 3RL8 MET D 306 UNP Q12959 EXPRESSION TAG
SEQADV 3RL8 GLY D 307 UNP Q12959 EXPRESSION TAG
SEQADV 3RL8 HIS D 308 UNP Q12959 EXPRESSION TAG
SEQADV 3RL8 HIS D 309 UNP Q12959 EXPRESSION TAG
SEQADV 3RL8 HIS D 310 UNP Q12959 EXPRESSION TAG
SEQADV 3RL8 HIS D 311 UNP Q12959 EXPRESSION TAG
SEQADV 3RL8 HIS D 312 UNP Q12959 EXPRESSION TAG
SEQADV 3RL8 HIS D 313 UNP Q12959 EXPRESSION TAG
SEQADV 3RL8 MET D 314 UNP Q12959 EXPRESSION TAG
SEQADV 3RL8 MET E 306 UNP Q12959 EXPRESSION TAG
SEQADV 3RL8 GLY E 307 UNP Q12959 EXPRESSION TAG
SEQADV 3RL8 HIS E 308 UNP Q12959 EXPRESSION TAG
SEQADV 3RL8 HIS E 309 UNP Q12959 EXPRESSION TAG
SEQADV 3RL8 HIS E 310 UNP Q12959 EXPRESSION TAG
SEQADV 3RL8 HIS E 311 UNP Q12959 EXPRESSION TAG
SEQADV 3RL8 HIS E 312 UNP Q12959 EXPRESSION TAG
SEQADV 3RL8 HIS E 313 UNP Q12959 EXPRESSION TAG
SEQADV 3RL8 MET E 314 UNP Q12959 EXPRESSION TAG
SEQRES 1 A 105 MET GLY HIS HIS HIS HIS HIS HIS MET GLU LYS ILE MET
SEQRES 2 A 105 GLU ILE LYS LEU ILE LYS GLY PRO LYS GLY LEU GLY PHE
SEQRES 3 A 105 SER ILE ALA GLY GLY VAL GLY ASN GLN HIS ILE PRO GLY
SEQRES 4 A 105 ASP ASN SER ILE TYR VAL THR LYS ILE ILE GLU GLY GLY
SEQRES 5 A 105 ALA ALA HIS LYS ASP GLY LYS LEU GLN ILE GLY ASP LYS
SEQRES 6 A 105 LEU LEU ALA VAL ASN ASN VAL CYS LEU GLU GLU VAL THR
SEQRES 7 A 105 HIS GLU GLU ALA VAL THR ALA LEU LYS ASN THR SER ASP
SEQRES 8 A 105 PHE VAL TYR LEU LYS VAL ALA LYS PRO THR SER MET TYR
SEQRES 9 A 105 MET
SEQRES 1 B 105 MET GLY HIS HIS HIS HIS HIS HIS MET GLU LYS ILE MET
SEQRES 2 B 105 GLU ILE LYS LEU ILE LYS GLY PRO LYS GLY LEU GLY PHE
SEQRES 3 B 105 SER ILE ALA GLY GLY VAL GLY ASN GLN HIS ILE PRO GLY
SEQRES 4 B 105 ASP ASN SER ILE TYR VAL THR LYS ILE ILE GLU GLY GLY
SEQRES 5 B 105 ALA ALA HIS LYS ASP GLY LYS LEU GLN ILE GLY ASP LYS
SEQRES 6 B 105 LEU LEU ALA VAL ASN ASN VAL CYS LEU GLU GLU VAL THR
SEQRES 7 B 105 HIS GLU GLU ALA VAL THR ALA LEU LYS ASN THR SER ASP
SEQRES 8 B 105 PHE VAL TYR LEU LYS VAL ALA LYS PRO THR SER MET TYR
SEQRES 9 B 105 MET
SEQRES 1 C 105 MET GLY HIS HIS HIS HIS HIS HIS MET GLU LYS ILE MET
SEQRES 2 C 105 GLU ILE LYS LEU ILE LYS GLY PRO LYS GLY LEU GLY PHE
SEQRES 3 C 105 SER ILE ALA GLY GLY VAL GLY ASN GLN HIS ILE PRO GLY
SEQRES 4 C 105 ASP ASN SER ILE TYR VAL THR LYS ILE ILE GLU GLY GLY
SEQRES 5 C 105 ALA ALA HIS LYS ASP GLY LYS LEU GLN ILE GLY ASP LYS
SEQRES 6 C 105 LEU LEU ALA VAL ASN ASN VAL CYS LEU GLU GLU VAL THR
SEQRES 7 C 105 HIS GLU GLU ALA VAL THR ALA LEU LYS ASN THR SER ASP
SEQRES 8 C 105 PHE VAL TYR LEU LYS VAL ALA LYS PRO THR SER MET TYR
SEQRES 9 C 105 MET
SEQRES 1 D 105 MET GLY HIS HIS HIS HIS HIS HIS MET GLU LYS ILE MET
SEQRES 2 D 105 GLU ILE LYS LEU ILE LYS GLY PRO LYS GLY LEU GLY PHE
SEQRES 3 D 105 SER ILE ALA GLY GLY VAL GLY ASN GLN HIS ILE PRO GLY
SEQRES 4 D 105 ASP ASN SER ILE TYR VAL THR LYS ILE ILE GLU GLY GLY
SEQRES 5 D 105 ALA ALA HIS LYS ASP GLY LYS LEU GLN ILE GLY ASP LYS
SEQRES 6 D 105 LEU LEU ALA VAL ASN ASN VAL CYS LEU GLU GLU VAL THR
SEQRES 7 D 105 HIS GLU GLU ALA VAL THR ALA LEU LYS ASN THR SER ASP
SEQRES 8 D 105 PHE VAL TYR LEU LYS VAL ALA LYS PRO THR SER MET TYR
SEQRES 9 D 105 MET
SEQRES 1 E 105 MET GLY HIS HIS HIS HIS HIS HIS MET GLU LYS ILE MET
SEQRES 2 E 105 GLU ILE LYS LEU ILE LYS GLY PRO LYS GLY LEU GLY PHE
SEQRES 3 E 105 SER ILE ALA GLY GLY VAL GLY ASN GLN HIS ILE PRO GLY
SEQRES 4 E 105 ASP ASN SER ILE TYR VAL THR LYS ILE ILE GLU GLY GLY
SEQRES 5 E 105 ALA ALA HIS LYS ASP GLY LYS LEU GLN ILE GLY ASP LYS
SEQRES 6 E 105 LEU LEU ALA VAL ASN ASN VAL CYS LEU GLU GLU VAL THR
SEQRES 7 E 105 HIS GLU GLU ALA VAL THR ALA LEU LYS ASN THR SER ASP
SEQRES 8 E 105 PHE VAL TYR LEU LYS VAL ALA LYS PRO THR SER MET TYR
SEQRES 9 E 105 MET
SEQRES 1 F 11 ARG HIS SER GLY SER TYR LEU VAL THR SER VAL
FORMUL 7 HOH *286(H2 O)
HELIX 1 1 GLY A 357 GLY A 363 1 7
HELIX 2 2 THR A 383 ASN A 393 1 11
HELIX 3 3 GLY B 357 GLY B 363 1 7
HELIX 4 4 THR B 383 ASN B 393 1 11
HELIX 5 5 GLY C 357 GLY C 363 1 7
HELIX 6 6 THR C 383 ASN C 393 1 11
HELIX 7 7 GLY D 357 GLY D 363 1 7
HELIX 8 8 THR D 383 ASN D 393 1 11
HELIX 9 9 GLY E 357 GLY E 363 1 7
HELIX 10 10 THR E 383 ASN E 393 1 11
SHEET 1 A 5 ILE A 317 ILE A 323 0
SHEET 2 A 5 PHE A 397 ALA A 403 -1 O LEU A 400 N ILE A 320
SHEET 3 A 5 LYS A 370 VAL A 374 -1 N LYS A 370 O ALA A 403
SHEET 4 A 5 ILE A 348 ILE A 353 -1 N ILE A 348 O LEU A 371
SHEET 5 A 5 PHE A 331 GLY A 335 -1 N ALA A 334 O TYR A 349
SHEET 1 B 4 ILE A 317 ILE A 323 0
SHEET 2 B 4 PHE A 397 ALA A 403 -1 O LEU A 400 N ILE A 320
SHEET 3 B 4 LYS A 370 VAL A 374 -1 N LYS A 370 O ALA A 403
SHEET 4 B 4 VAL A 377 CYS A 378 -1 O VAL A 377 N VAL A 374
SHEET 1 C 5 ILE B 317 ILE B 323 0
SHEET 2 C 5 PHE B 397 ALA B 403 -1 O LEU B 400 N ILE B 320
SHEET 3 C 5 LYS B 370 VAL B 374 -1 N LEU B 372 O LYS B 401
SHEET 4 C 5 ILE B 348 ILE B 353 -1 N ILE B 348 O LEU B 371
SHEET 5 C 5 PHE B 331 GLY B 335 -1 N ALA B 334 O TYR B 349
SHEET 1 D 4 ILE B 317 ILE B 323 0
SHEET 2 D 4 PHE B 397 ALA B 403 -1 O LEU B 400 N ILE B 320
SHEET 3 D 4 LYS B 370 VAL B 374 -1 N LEU B 372 O LYS B 401
SHEET 4 D 4 VAL B 377 CYS B 378 -1 O VAL B 377 N VAL B 374
SHEET 1 E 5 ILE C 317 ILE C 323 0
SHEET 2 E 5 PHE C 397 ALA C 403 -1 O VAL C 402 N MET C 318
SHEET 3 E 5 LYS C 370 VAL C 374 -1 N LEU C 372 O LYS C 401
SHEET 4 E 5 ILE C 348 ILE C 353 -1 N ILE C 348 O LEU C 371
SHEET 5 E 5 PHE C 331 GLY C 335 -1 N ALA C 334 O TYR C 349
SHEET 1 F 4 ILE C 317 ILE C 323 0
SHEET 2 F 4 PHE C 397 ALA C 403 -1 O VAL C 402 N MET C 318
SHEET 3 F 4 LYS C 370 VAL C 374 -1 N LEU C 372 O LYS C 401
SHEET 4 F 4 VAL C 377 CYS C 378 -1 O VAL C 377 N VAL C 374
SHEET 1 G 5 ILE D 317 ILE D 323 0
SHEET 2 G 5 PHE D 397 ALA D 403 -1 O LEU D 400 N ILE D 320
SHEET 3 G 5 LYS D 370 VAL D 374 -1 N LEU D 372 O LYS D 401
SHEET 4 G 5 ILE D 348 ILE D 353 -1 N ILE D 348 O LEU D 371
SHEET 5 G 5 PHE D 331 GLY D 335 -1 N ALA D 334 O TYR D 349
SHEET 1 H 4 ILE D 317 ILE D 323 0
SHEET 2 H 4 PHE D 397 ALA D 403 -1 O LEU D 400 N ILE D 320
SHEET 3 H 4 LYS D 370 VAL D 374 -1 N LEU D 372 O LYS D 401
SHEET 4 H 4 VAL D 377 CYS D 378 -1 O VAL D 377 N VAL D 374
SHEET 1 I 5 ILE E 317 ILE E 323 0
SHEET 2 I 5 PHE E 397 ALA E 403 -1 O LEU E 400 N ILE E 320
SHEET 3 I 5 LYS E 370 VAL E 374 -1 N LEU E 372 O LYS E 401
SHEET 4 I 5 ILE E 348 ILE E 353 -1 N ILE E 348 O LEU E 371
SHEET 5 I 5 PHE E 331 GLY E 335 -1 N ALA E 334 O TYR E 349
SHEET 1 J 4 ILE E 317 ILE E 323 0
SHEET 2 J 4 PHE E 397 ALA E 403 -1 O LEU E 400 N ILE E 320
SHEET 3 J 4 LYS E 370 VAL E 374 -1 N LEU E 372 O LYS E 401
SHEET 4 J 4 VAL E 377 CYS E 378 -1 O VAL E 377 N VAL E 374
CRYST1 67.806 52.502 87.426 90.00 102.42 90.00 P 1 21 1 10
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 0.014748 0.000000 0.003247 0.00000
SCALE2 0.000000 0.019047 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011712 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
