HEADER TRANSCRIPTION REGULATOR 26-AUG-10 3OMC
TITLE STRUCTURE OF HUMAN SND1 EXTENDED TUDOR DOMAIN IN COMPLEX WITH THE
TITLE 2 SYMMETRICALLY DIMETHYLATED ARGININE PIWIL1 PEPTIDE R4ME2S
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: STAPHYLOCOCCAL NUCLEASE DOMAIN-CONTAINING PROTEIN 1;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: TUDOR DOMAIN (UNP RESIDUES 650-910);
COMPND 5 SYNONYM: 100 KDA COACTIVATOR,EBNA2 COACTIVATOR P100,TUDOR DOMAIN-
COMPND 6 CONTAINING PROTEIN 11,P100 CO-ACTIVATOR;
COMPND 7 ENGINEERED: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: SYNTHETIC PEPTIDE;
COMPND 10 CHAIN: C, D;
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: SND1, TDRD11;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21-(DE3)-V2R-PRARE2;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET28-MHL;
SOURCE 11 MOL_ID: 2;
SOURCE 12 SYNTHETIC: YES;
SOURCE 13 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;
SOURCE 14 ORGANISM_TAXID: 32630;
SOURCE 15 OTHER_DETAILS: SYMMETRICALLY DIMETHYLATED ARGININE PEPTIDE R4ME2S
SOURCE 16 DERIVED FROM PIWIL1
KEYWDS STAPHYLOCOCCAL NUCLEASE DOMAIN-CONTAINING PROTEIN 1, TDRD11, SND1,
KEYWDS 2 PIWIL1/MIWI, STRUCTURAL GENOMICS CONSORTIUM, SGC, P100 EXTENDED
KEYWDS 3 TUDOR DOMAIN, TRANSCRIPTION REGULATION, SYMMETRICALLY DIMETHYLATED
KEYWDS 4 ARGININE PEPTIDES DERIVED FROM PIWIL1, TRANSCRIPTION REGULATOR
EXPDTA X-RAY DIFFRACTION
AUTHOR R.LAM,K.LIU,Y.H.GUO,C.B.BIAN,C.XU,F.MACKENZIE,C.BOUNTRA,J.WEIGELT,
AUTHOR 2 C.H.ARROWSMITH,A.M.EDWARDS,A.BOCHKAREV,J.MIN,STRUCTURAL GENOMICS
AUTHOR 3 CONSORTIUM (SGC)
REVDAT 6 06-SEP-23 3OMC 1 REMARK LINK
REVDAT 5 15-NOV-17 3OMC 1 COMPND SOURCE DBREF
REVDAT 4 08-NOV-17 3OMC 1 REMARK
REVDAT 3 19-JAN-11 3OMC 1 JRNL
REVDAT 2 20-OCT-10 3OMC 1 JRNL
REVDAT 1 15-SEP-10 3OMC 0
JRNL AUTH K.LIU,C.CHEN,Y.GUO,R.LAM,C.BIAN,C.XU,D.Y.ZHAO,J.JIN,
JRNL AUTH 2 F.MACKENZIE,T.PAWSON,J.MIN
JRNL TITL STRUCTURAL BASIS FOR RECOGNITION OF ARGININE METHYLATED PIWI
JRNL TITL 2 PROTEINS BY THE EXTENDED TUDOR DOMAIN.
JRNL REF PROC.NATL.ACAD.SCI.USA V. 107 18398 2010
JRNL REFN ISSN 0027-8424
JRNL PMID 20937909
JRNL DOI 10.1073/PNAS.1013106107
REMARK 2
REMARK 2 RESOLUTION. 1.77 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC REFMAC_5.6.0081
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) : 1.77
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 25.05
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 41488
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) : 0.180
REMARK 3 R VALUE (WORKING SET) : 0.179
REMARK 3 FREE R VALUE : 0.213
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2088
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) : 1.77
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.82
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2854
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.82
REMARK 3 BIN R VALUE (WORKING SET) : 0.2160
REMARK 3 BIN FREE R VALUE SET COUNT : 148
REMARK 3 BIN FREE R VALUE : 0.2690
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3501
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 1
REMARK 3 SOLVENT ATOMS : 280
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 29.34
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.22000
REMARK 3 B22 (A**2) : -0.43000
REMARK 3 B33 (A**2) : -0.80000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.85000
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): 0.119
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.079
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.822
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.959
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.939
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3583 ; 0.010 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4861 ; 1.175 ; 1.958
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 441 ; 5.452 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 178 ;34.118 ;24.045
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 589 ;12.657 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 27 ;11.324 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 538 ; 0.083 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2769 ; 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): 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 : 4
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 681 A 897
REMARK 3 ORIGIN FOR THE GROUP (A): 3.8630 0.7430 8.8930
REMARK 3 T TENSOR
REMARK 3 T11: 0.0092 T22: 0.0222
REMARK 3 T33: 0.0234 T12: 0.0050
REMARK 3 T13: 0.0076 T23: -0.0047
REMARK 3 L TENSOR
REMARK 3 L11: 0.1683 L22: 0.6176
REMARK 3 L33: 0.7607 L12: -0.2350
REMARK 3 L13: 0.3238 L23: -0.4657
REMARK 3 S TENSOR
REMARK 3 S11: -0.0234 S12: 0.0099 S13: -0.0068
REMARK 3 S21: 0.0541 S22: 0.0178 S23: -0.0102
REMARK 3 S31: -0.0411 S32: 0.0179 S33: 0.0056
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 682 B 897
REMARK 3 ORIGIN FOR THE GROUP (A): 3.8790 1.9010 47.7710
REMARK 3 T TENSOR
REMARK 3 T11: 0.0234 T22: 0.0129
REMARK 3 T33: 0.0179 T12: -0.0057
REMARK 3 T13: -0.0040 T23: 0.0014
REMARK 3 L TENSOR
REMARK 3 L11: 0.0925 L22: 0.6135
REMARK 3 L33: 1.3908 L12: -0.1852
REMARK 3 L13: 0.3203 L23: -0.5221
REMARK 3 S TENSOR
REMARK 3 S11: -0.0121 S12: 0.0146 S13: -0.0039
REMARK 3 S21: -0.0427 S22: -0.0356 S23: 0.0121
REMARK 3 S31: -0.0946 S32: 0.0712 S33: 0.0477
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 2 C 8
REMARK 3 ORIGIN FOR THE GROUP (A): 17.3900 -4.8870 8.3050
REMARK 3 T TENSOR
REMARK 3 T11: 0.0535 T22: 0.1376
REMARK 3 T33: 0.0681 T12: 0.0771
REMARK 3 T13: 0.0108 T23: 0.0234
REMARK 3 L TENSOR
REMARK 3 L11: 1.7225 L22: 5.4071
REMARK 3 L33: 6.4581 L12: -2.1884
REMARK 3 L13: -1.9150 L23: -0.9389
REMARK 3 S TENSOR
REMARK 3 S11: -0.1813 S12: -0.1040 S13: 0.0759
REMARK 3 S21: 0.0179 S22: -0.2015 S23: -0.4627
REMARK 3 S31: 0.4652 S32: 0.5380 S33: 0.3828
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 3 D 3
REMARK 3 ORIGIN FOR THE GROUP (A): 11.0940 -6.4480 49.0400
REMARK 3 T TENSOR
REMARK 3 T11: 0.0929 T22: 0.1927
REMARK 3 T33: 0.1837 T12: -0.0435
REMARK 3 T13: 0.0702 T23: -0.0522
REMARK 3 L TENSOR
REMARK 3 L11: 72.0067 L22: 22.0773
REMARK 3 L33: 35.2271 L12: -4.6180
REMARK 3 L13: 0.2032 L23: -27.7127
REMARK 3 S TENSOR
REMARK 3 S11: 0.8241 S12: 2.8634 S13: 0.4592
REMARK 3 S21: 0.7336 S22: -1.1058 S23: -0.2584
REMARK 3 S31: -0.9965 S32: 1.1600 S33: 0.2817
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH 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 USED IF PRESENT IN
REMARK 3 THE INPUT. U VALUES: WITH TLS ADDED
REMARK 4
REMARK 4 3OMC COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 31-AUG-10.
REMARK 100 THE DEPOSITION ID IS D_1000061296.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 11-JUN-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) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU FR-E SUPERBRIGHT
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : GRAPHITE
REMARK 200 OPTICS : VARIMAX HR
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS HTC
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO, HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK, HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 41508
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.770
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 200 DATA REDUNDANCY : 3.600
REMARK 200 R MERGE (I) : 0.04000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 18.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.77
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.83
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.0
REMARK 200 DATA REDUNDANCY IN SHELL : 3.50
REMARK 200 R MERGE FOR SHELL (I) : 0.28200
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: MOLREP
REMARK 200 STARTING MODEL: PDB ENTRY 2O4X
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 30.29
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.76
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% PEG1500, 1:500 V8 PROTEASE, PH
REMARK 280 7.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 291K
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 37.91700
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
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 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1010 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 12270 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -7.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C
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: 580 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 11750 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -13.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, 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 650
REMARK 465 LYS A 651
REMARK 465 GLN A 652
REMARK 465 LYS A 653
REMARK 465 LYS A 654
REMARK 465 GLU A 655
REMARK 465 LYS A 656
REMARK 465 VAL A 657
REMARK 465 TRP A 658
REMARK 465 ALA A 659
REMARK 465 HIS A 660
REMARK 465 TYR A 661
REMARK 465 GLU A 662
REMARK 465 GLU A 663
REMARK 465 GLN A 664
REMARK 465 PRO A 665
REMARK 465 VAL A 666
REMARK 465 GLU A 667
REMARK 465 GLU A 668
REMARK 465 VAL A 669
REMARK 465 MET A 670
REMARK 465 PRO A 671
REMARK 465 VAL A 672
REMARK 465 LEU A 673
REMARK 465 GLU A 674
REMARK 465 GLU A 675
REMARK 465 LYS A 676
REMARK 465 GLU A 677
REMARK 465 ARG A 678
REMARK 465 SER A 679
REMARK 465 ALA A 680
REMARK 465 PHE A 898
REMARK 465 ARG A 899
REMARK 465 ALA A 900
REMARK 465 ASP A 901
REMARK 465 ASP A 902
REMARK 465 ALA A 903
REMARK 465 ASP A 904
REMARK 465 GLU A 905
REMARK 465 PHE A 906
REMARK 465 GLY A 907
REMARK 465 TYR A 908
REMARK 465 SER A 909
REMARK 465 ARG A 910
REMARK 465 ALA B 650
REMARK 465 LYS B 651
REMARK 465 GLN B 652
REMARK 465 LYS B 653
REMARK 465 LYS B 654
REMARK 465 GLU B 655
REMARK 465 LYS B 656
REMARK 465 VAL B 657
REMARK 465 TRP B 658
REMARK 465 ALA B 659
REMARK 465 HIS B 660
REMARK 465 TYR B 661
REMARK 465 GLU B 662
REMARK 465 GLU B 663
REMARK 465 GLN B 664
REMARK 465 PRO B 665
REMARK 465 VAL B 666
REMARK 465 GLU B 667
REMARK 465 GLU B 668
REMARK 465 VAL B 669
REMARK 465 MET B 670
REMARK 465 PRO B 671
REMARK 465 VAL B 672
REMARK 465 LEU B 673
REMARK 465 GLU B 674
REMARK 465 GLU B 675
REMARK 465 LYS B 676
REMARK 465 GLU B 677
REMARK 465 ARG B 678
REMARK 465 SER B 679
REMARK 465 ALA B 680
REMARK 465 SER B 681
REMARK 465 PHE B 898
REMARK 465 ARG B 899
REMARK 465 ALA B 900
REMARK 465 ASP B 901
REMARK 465 ASP B 902
REMARK 465 ALA B 903
REMARK 465 ASP B 904
REMARK 465 GLU B 905
REMARK 465 PHE B 906
REMARK 465 GLY B 907
REMARK 465 TYR B 908
REMARK 465 SER B 909
REMARK 465 ARG B 910
REMARK 465 THR C 1
REMARK 465 THR D 1
REMARK 465 GLY D 2
REMARK 465 ALA D 4
REMARK 465 ARG D 5
REMARK 465 ALA D 6
REMARK 465 ARG D 7
REMARK 465 ALA D 8
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 LYS A 683 CG CD CE NZ
REMARK 470 ARG B 819 CG CD NE CZ NH1 NH2
REMARK 470 ASP B 846 CG OD1 OD2
REMARK 470 GLN B 872 CG CD OE1 NE2
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 ASP A 846 -71.26 -74.32
REMARK 500 ASN A 891 -106.38 53.36
REMARK 500 ASP B 846 -83.07 -68.23
REMARK 500 ASN B 891 -106.07 55.08
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 RESIDUE CL B 1000
DBREF 3OMC A 650 910 UNP Q7KZF4 SND1_HUMAN 650 910
DBREF 3OMC B 650 910 UNP Q7KZF4 SND1_HUMAN 650 910
DBREF 3OMC C 1 8 PDB 3OMC 3OMC 1 8
DBREF 3OMC D 1 8 PDB 3OMC 3OMC 1 8
SEQRES 1 A 261 ALA LYS GLN LYS LYS GLU LYS VAL TRP ALA HIS TYR GLU
SEQRES 2 A 261 GLU GLN PRO VAL GLU GLU VAL MET PRO VAL LEU GLU GLU
SEQRES 3 A 261 LYS GLU ARG SER ALA SER TYR LYS PRO VAL PHE VAL THR
SEQRES 4 A 261 GLU ILE THR ASP ASP LEU HIS PHE TYR VAL GLN ASP VAL
SEQRES 5 A 261 GLU THR GLY THR GLN LEU GLU LYS LEU MET GLU ASN MET
SEQRES 6 A 261 ARG ASN ASP ILE ALA SER HIS PRO PRO VAL GLU GLY SER
SEQRES 7 A 261 TYR ALA PRO ARG ARG GLY GLU PHE CYS ILE ALA LYS PHE
SEQRES 8 A 261 VAL ASP GLY GLU TRP TYR ARG ALA ARG VAL GLU LYS VAL
SEQRES 9 A 261 GLU SER PRO ALA LYS ILE HIS VAL PHE TYR ILE ASP TYR
SEQRES 10 A 261 GLY ASN ARG GLU VAL LEU PRO SER THR ARG LEU GLY THR
SEQRES 11 A 261 LEU SER PRO ALA PHE SER THR ARG VAL LEU PRO ALA GLN
SEQRES 12 A 261 ALA THR GLU TYR ALA PHE ALA PHE ILE GLN VAL PRO GLN
SEQRES 13 A 261 ASP ASP ASP ALA ARG THR ASP ALA VAL ASP SER VAL VAL
SEQRES 14 A 261 ARG ASP ILE GLN ASN THR GLN CYS LEU LEU ASN VAL GLU
SEQRES 15 A 261 HIS LEU SER ALA GLY CYS PRO HIS VAL THR LEU GLN PHE
SEQRES 16 A 261 ALA ASP SER LYS GLY ASP VAL GLY LEU GLY LEU VAL LYS
SEQRES 17 A 261 GLU GLY LEU VAL MET VAL GLU VAL ARG LYS GLU LYS GLN
SEQRES 18 A 261 PHE GLN LYS VAL ILE THR GLU TYR LEU ASN ALA GLN GLU
SEQRES 19 A 261 SER ALA LYS SER ALA ARG LEU ASN LEU TRP ARG TYR GLY
SEQRES 20 A 261 ASP PHE ARG ALA ASP ASP ALA ASP GLU PHE GLY TYR SER
SEQRES 21 A 261 ARG
SEQRES 1 B 261 ALA LYS GLN LYS LYS GLU LYS VAL TRP ALA HIS TYR GLU
SEQRES 2 B 261 GLU GLN PRO VAL GLU GLU VAL MET PRO VAL LEU GLU GLU
SEQRES 3 B 261 LYS GLU ARG SER ALA SER TYR LYS PRO VAL PHE VAL THR
SEQRES 4 B 261 GLU ILE THR ASP ASP LEU HIS PHE TYR VAL GLN ASP VAL
SEQRES 5 B 261 GLU THR GLY THR GLN LEU GLU LYS LEU MET GLU ASN MET
SEQRES 6 B 261 ARG ASN ASP ILE ALA SER HIS PRO PRO VAL GLU GLY SER
SEQRES 7 B 261 TYR ALA PRO ARG ARG GLY GLU PHE CYS ILE ALA LYS PHE
SEQRES 8 B 261 VAL ASP GLY GLU TRP TYR ARG ALA ARG VAL GLU LYS VAL
SEQRES 9 B 261 GLU SER PRO ALA LYS ILE HIS VAL PHE TYR ILE ASP TYR
SEQRES 10 B 261 GLY ASN ARG GLU VAL LEU PRO SER THR ARG LEU GLY THR
SEQRES 11 B 261 LEU SER PRO ALA PHE SER THR ARG VAL LEU PRO ALA GLN
SEQRES 12 B 261 ALA THR GLU TYR ALA PHE ALA PHE ILE GLN VAL PRO GLN
SEQRES 13 B 261 ASP ASP ASP ALA ARG THR ASP ALA VAL ASP SER VAL VAL
SEQRES 14 B 261 ARG ASP ILE GLN ASN THR GLN CYS LEU LEU ASN VAL GLU
SEQRES 15 B 261 HIS LEU SER ALA GLY CYS PRO HIS VAL THR LEU GLN PHE
SEQRES 16 B 261 ALA ASP SER LYS GLY ASP VAL GLY LEU GLY LEU VAL LYS
SEQRES 17 B 261 GLU GLY LEU VAL MET VAL GLU VAL ARG LYS GLU LYS GLN
SEQRES 18 B 261 PHE GLN LYS VAL ILE THR GLU TYR LEU ASN ALA GLN GLU
SEQRES 19 B 261 SER ALA LYS SER ALA ARG LEU ASN LEU TRP ARG TYR GLY
SEQRES 20 B 261 ASP PHE ARG ALA ASP ASP ALA ASP GLU PHE GLY TYR SER
SEQRES 21 B 261 ARG
SEQRES 1 C 8 THR GLY 2MR ALA ARG ALA ARG ALA
SEQRES 1 D 8 THR GLY 2MR ALA ARG ALA ARG ALA
MODRES 3OMC 2MR C 3 ARG N3, N4-DIMETHYLARGININE
MODRES 3OMC 2MR D 3 ARG N3, N4-DIMETHYLARGININE
HET 2MR C 3 13
HET 2MR D 3 13
HET CL B1000 1
HETNAM 2MR N3, N4-DIMETHYLARGININE
HETNAM CL CHLORIDE ION
FORMUL 3 2MR 2(C8 H18 N4 O2)
FORMUL 5 CL CL 1-
FORMUL 6 HOH *280(H2 O)
HELIX 1 1 THR A 703 HIS A 721 1 19
HELIX 2 2 PRO A 722 GLY A 726 5 5
HELIX 3 3 PRO A 773 THR A 775 5 3
HELIX 4 4 SER A 781 SER A 785 5 5
HELIX 5 5 ASP A 806 GLN A 822 1 17
HELIX 6 6 ASP A 850 GLU A 858 1 9
HELIX 7 7 GLU A 868 GLN A 870 5 3
HELIX 8 8 PHE A 871 ALA A 888 1 18
HELIX 9 9 LEU A 890 ARG A 894 5 5
HELIX 10 10 THR B 703 HIS B 721 1 19
HELIX 11 11 PRO B 723 SER B 727 5 5
HELIX 12 12 PRO B 773 THR B 775 5 3
HELIX 13 13 SER B 781 SER B 785 5 5
HELIX 14 14 ASP B 806 GLN B 822 1 17
HELIX 15 15 ASP B 850 GLU B 858 1 9
HELIX 16 16 GLU B 868 GLN B 870 5 3
HELIX 17 17 PHE B 871 ALA B 888 1 18
HELIX 18 18 LEU B 890 ARG B 894 5 5
SHEET 1 A 6 LYS A 683 ILE A 690 0
SHEET 2 A 6 HIS A 695 ASP A 700 -1 O GLN A 699 N PHE A 686
SHEET 3 A 6 ALA A 793 PHE A 798 -1 O TYR A 796 N PHE A 696
SHEET 4 A 6 HIS A 839 PHE A 844 1 O VAL A 840 N ALA A 797
SHEET 5 A 6 THR A 824 HIS A 832 -1 N HIS A 832 O HIS A 839
SHEET 6 A 6 LYS A 683 ILE A 690 -1 N VAL A 685 O CYS A 826
SHEET 1 B 5 ARG A 769 LEU A 772 0
SHEET 2 B 5 LYS A 758 TYR A 763 -1 N ILE A 759 O LEU A 772
SHEET 3 B 5 TRP A 745 SER A 755 -1 N GLU A 751 O HIS A 760
SHEET 4 B 5 PHE A 735 LYS A 739 -1 N ALA A 738 O TYR A 746
SHEET 5 B 5 LEU A 777 GLY A 778 -1 O GLY A 778 N ILE A 737
SHEET 1 C 2 ILE A 801 GLN A 802 0
SHEET 2 C 2 MET A 862 VAL A 863 -1 O MET A 862 N GLN A 802
SHEET 1 D 6 LYS B 683 ILE B 690 0
SHEET 2 D 6 PHE B 696 ASP B 700 -1 O GLN B 699 N PHE B 686
SHEET 3 D 6 ALA B 793 PHE B 798 -1 O TYR B 796 N PHE B 696
SHEET 4 D 6 HIS B 839 PHE B 844 1 O VAL B 840 N ALA B 797
SHEET 5 D 6 THR B 824 HIS B 832 -1 N HIS B 832 O HIS B 839
SHEET 6 D 6 LYS B 683 ILE B 690 -1 N VAL B 685 O CYS B 826
SHEET 1 E 5 ARG B 769 LEU B 772 0
SHEET 2 E 5 LYS B 758 PHE B 762 -1 N ILE B 759 O LEU B 772
SHEET 3 E 5 TRP B 745 SER B 755 -1 N GLU B 751 O HIS B 760
SHEET 4 E 5 PHE B 735 LYS B 739 -1 N CYS B 736 O ALA B 748
SHEET 5 E 5 LEU B 777 THR B 779 -1 O GLY B 778 N ILE B 737
SHEET 1 F 2 ILE B 801 GLN B 802 0
SHEET 2 F 2 MET B 862 VAL B 863 -1 O MET B 862 N GLN B 802
LINK C GLY C 2 N 2MR C 3 1555 1555 1.33
LINK C 2MR C 3 N ALA C 4 1555 1555 1.34
SITE 1 AC1 2 PRO B 723 THR B 779
CRYST1 35.622 75.834 80.177 90.00 90.37 90.00 P 1 21 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 0.028073 0.000000 0.000183 0.00000
SCALE2 0.000000 0.013187 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012473 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
