HEADER STRUCTURAL PROTEIN 28-FEB-12 4DXS
TITLE HUMAN SUN2-KASH2 COMPLEX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SUN DOMAIN-CONTAINING PROTEIN 2;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: SUN DOMAIN (UNP RESIDUES 522-717);
COMPND 5 SYNONYM: PROTEIN UNC-84 HOMOLOG B, RAB5-INTERACTING PROTEIN, RAB5IP,
COMPND 6 SAD1/UNC-84 PROTEIN-LIKE 2;
COMPND 7 ENGINEERED: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: NESPRIN-2;
COMPND 10 CHAIN: B;
COMPND 11 FRAGMENT: UNP RESIDUES 6857-6885;
COMPND 12 SYNONYM: NUCLEAR ENVELOPE SPECTRIN REPEAT PROTEIN 2, NUCLEUS AND
COMPND 13 ACTIN CONNECTING ELEMENT PROTEIN, PROTEIN NUANCE, SYNAPTIC NUCLEAR
COMPND 14 ENVELOPE PROTEIN 2, SYNE-2;
COMPND 15 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: SUN2, FRIGG, KIAA0668, RAB5IP, UNC84B;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 MOL_ID: 2;
SOURCE 9 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 10 ORGANISM_COMMON: HUMAN;
SOURCE 11 ORGANISM_TAXID: 9606;
SOURCE 12 GENE: SYNE2, KIAA1011, NUA;
SOURCE 13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 14 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS BETA-SANDWICH, LINC COMPLEX, STRUCTURAL PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR B.SOSA,T.U.SCHWARTZ
REVDAT 2 13-SEP-23 4DXS 1 REMARK SEQADV LINK
REVDAT 1 06-JUN-12 4DXS 0
JRNL AUTH B.A.SOSA,A.ROTHBALLER,U.KUTAY,T.U.SCHWARTZ
JRNL TITL LINC COMPLEXES FORM BY BINDING OF THREE KASH PEPTIDES TO
JRNL TITL 2 DOMAIN INTERFACES OF TRIMERIC SUN PROTEINS.
JRNL REF CELL(CAMBRIDGE,MASS.) V. 149 1035 2012
JRNL REFN ISSN 0092-8674
JRNL PMID 22632968
JRNL DOI 10.1016/J.CELL.2012.03.046
REMARK 2
REMARK 2 RESOLUTION. 2.71 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: DEV_975)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.71
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 36.06
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 8909
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.188
REMARK 3 R VALUE (WORKING SET) : 0.182
REMARK 3 FREE R VALUE : 0.241
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.000
REMARK 3 FREE R VALUE TEST SET COUNT : 891
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.10
REMARK 3 SHRINKAGE RADIUS : 0.86
REMARK 3 K_SOL : 0.32
REMARK 3 B_SOL : 48.18
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.420
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.670
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 65.53
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.85000
REMARK 3 B22 (A**2) : -0.85000
REMARK 3 B33 (A**2) : 1.28000
REMARK 3 B12 (A**2) : -0.43000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.013 1825
REMARK 3 ANGLE : 1.732 2492
REMARK 3 CHIRALITY : 0.116 274
REMARK 3 PLANARITY : 0.008 1416
REMARK 3 DIHEDRAL : 14.898 654
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4DXS COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 29-FEB-12.
REMARK 100 THE DEPOSITION ID IS D_1000070916.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-JUL-11
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.4
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 24-ID-E
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9792
REMARK 200 MONOCHROMATOR : SINGLE CRYSTAL SI(220) SIDE
REMARK 200 BOUNCE
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 8912
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.700
REMARK 200 RESOLUTION RANGE LOW (A) : 43.300
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.700
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 5.900
REMARK 200 R MERGE (I) : 0.05500
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 21.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.80
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.8
REMARK 200 DATA REDUNDANCY IN SHELL : 6.10
REMARK 200 R MERGE FOR SHELL (I) : 0.69500
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 4DXT
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 59.07
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.00
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M HEPES, PH 7.4, 7% PEG4000, 10%
REMARK 280 1,6-HEXANEDIOL, 0.25% DM, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: H 3 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z
REMARK 290 3555 -X+Y,-X,Z
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z
REMARK 290 6555 -X,-X+Y,-Z
REMARK 290 7555 X+2/3,Y+1/3,Z+1/3
REMARK 290 8555 -Y+2/3,X-Y+1/3,Z+1/3
REMARK 290 9555 -X+Y+2/3,-X+1/3,Z+1/3
REMARK 290 10555 Y+2/3,X+1/3,-Z+1/3
REMARK 290 11555 X-Y+2/3,-Y+1/3,-Z+1/3
REMARK 290 12555 -X+2/3,-X+Y+1/3,-Z+1/3
REMARK 290 13555 X+1/3,Y+2/3,Z+2/3
REMARK 290 14555 -Y+1/3,X-Y+2/3,Z+2/3
REMARK 290 15555 -X+Y+1/3,-X+2/3,Z+2/3
REMARK 290 16555 Y+1/3,X+2/3,-Z+2/3
REMARK 290 17555 X-Y+1/3,-Y+2/3,-Z+2/3
REMARK 290 18555 -X+1/3,-X+Y+2/3,-Z+2/3
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 0.00000
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 0.00000
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 0.00000
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 0.00000
REMARK 290 SMTRY1 7 1.000000 0.000000 0.000000 39.66000
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 22.89771
REMARK 290 SMTRY3 7 0.000000 0.000000 1.000000 86.67667
REMARK 290 SMTRY1 8 -0.500000 -0.866025 0.000000 39.66000
REMARK 290 SMTRY2 8 0.866025 -0.500000 0.000000 22.89771
REMARK 290 SMTRY3 8 0.000000 0.000000 1.000000 86.67667
REMARK 290 SMTRY1 9 -0.500000 0.866025 0.000000 39.66000
REMARK 290 SMTRY2 9 -0.866025 -0.500000 0.000000 22.89771
REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 86.67667
REMARK 290 SMTRY1 10 -0.500000 0.866025 0.000000 39.66000
REMARK 290 SMTRY2 10 0.866025 0.500000 0.000000 22.89771
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 86.67667
REMARK 290 SMTRY1 11 1.000000 0.000000 0.000000 39.66000
REMARK 290 SMTRY2 11 0.000000 -1.000000 0.000000 22.89771
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 86.67667
REMARK 290 SMTRY1 12 -0.500000 -0.866025 0.000000 39.66000
REMARK 290 SMTRY2 12 -0.866025 0.500000 0.000000 22.89771
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 86.67667
REMARK 290 SMTRY1 13 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 13 0.000000 1.000000 0.000000 45.79542
REMARK 290 SMTRY3 13 0.000000 0.000000 1.000000 173.35333
REMARK 290 SMTRY1 14 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 14 0.866025 -0.500000 0.000000 45.79542
REMARK 290 SMTRY3 14 0.000000 0.000000 1.000000 173.35333
REMARK 290 SMTRY1 15 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 15 -0.866025 -0.500000 0.000000 45.79542
REMARK 290 SMTRY3 15 0.000000 0.000000 1.000000 173.35333
REMARK 290 SMTRY1 16 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 16 0.866025 0.500000 0.000000 45.79542
REMARK 290 SMTRY3 16 0.000000 0.000000 -1.000000 173.35333
REMARK 290 SMTRY1 17 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 17 0.000000 -1.000000 0.000000 45.79542
REMARK 290 SMTRY3 17 0.000000 0.000000 -1.000000 173.35333
REMARK 290 SMTRY1 18 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 18 -0.866025 0.500000 0.000000 45.79542
REMARK 290 SMTRY3 18 0.000000 0.000000 -1.000000 173.35333
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 16480 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 27720 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -83.0 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 BIOMT1 2 -0.500000 -0.866025 0.000000 39.66000
REMARK 350 BIOMT2 2 0.866025 -0.500000 0.000000 68.69314
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 3 -0.500000 0.866025 0.000000 -39.66000
REMARK 350 BIOMT2 3 -0.866025 -0.500000 0.000000 68.69314
REMARK 350 BIOMT3 3 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 516
REMARK 465 PRO A 517
REMARK 465 GLY A 518
REMARK 465 GLY A 519
REMARK 465 SER A 520
REMARK 465 GLY A 521
REMARK 465 GLY B 6851
REMARK 465 PRO B 6852
REMARK 465 GLY B 6853
REMARK 465 GLY B 6854
REMARK 465 SER B 6855
REMARK 465 GLY B 6856
REMARK 465 GLU B 6857
REMARK 465 GLU B 6858
REMARK 465 ASP B 6859
REMARK 465 TYR B 6860
REMARK 465 SER B 6861
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 HIS A 628 CG HIS A 628 CD2 0.056
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 ASP A 542 37.26 39.11
REMARK 500 ARG A 543 -34.22 71.51
REMARK 500 SER A 560 138.02 170.78
REMARK 500 ARG A 562 -122.18 42.79
REMARK 500 PHE A 577 17.92 47.54
REMARK 500 LYS A 644 -98.64 -116.85
REMARK 500 GLU A 653 -71.22 -177.45
REMARK 500 ALA A 681 56.87 25.81
REMARK 500 TYR A 707 -75.95 -77.00
REMARK 500 THR B6863 -149.76 34.82
REMARK 500 ASN B6866 84.94 -169.72
REMARK 500 ARG B6870 56.48 -108.54
REMARK 500 ASN B6880 -151.73 -80.60
REMARK 500
REMARK 500 REMARK: NULL
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 DMU A 801
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K A 802 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 VAL A 590 O
REMARK 620 2 GLN A 593 O 76.6
REMARK 620 3 ASP A 595 O 143.3 95.2
REMARK 620 4 TYR A 707 O 78.2 111.6 136.5
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMU A 801
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K A 802
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4DXR RELATED DB: PDB
REMARK 900 RELATED ID: 4DXT RELATED DB: PDB
DBREF 4DXS A 522 717 UNP Q9UH99 SUN2_HUMAN 522 717
DBREF 4DXS B 6857 6885 UNP Q8WXH0 SYNE2_HUMAN 6857 6885
SEQADV 4DXS GLY A 516 UNP Q9UH99 EXPRESSION TAG
SEQADV 4DXS PRO A 517 UNP Q9UH99 EXPRESSION TAG
SEQADV 4DXS GLY A 518 UNP Q9UH99 EXPRESSION TAG
SEQADV 4DXS GLY A 519 UNP Q9UH99 EXPRESSION TAG
SEQADV 4DXS SER A 520 UNP Q9UH99 EXPRESSION TAG
SEQADV 4DXS GLY A 521 UNP Q9UH99 EXPRESSION TAG
SEQADV 4DXS GLY B 6851 UNP Q8WXH0 EXPRESSION TAG
SEQADV 4DXS PRO B 6852 UNP Q8WXH0 EXPRESSION TAG
SEQADV 4DXS GLY B 6853 UNP Q8WXH0 EXPRESSION TAG
SEQADV 4DXS GLY B 6854 UNP Q8WXH0 EXPRESSION TAG
SEQADV 4DXS SER B 6855 UNP Q8WXH0 EXPRESSION TAG
SEQADV 4DXS GLY B 6856 UNP Q8WXH0 EXPRESSION TAG
SEQRES 1 A 202 GLY PRO GLY GLY SER GLY GLY VAL THR GLU GLU GLN VAL
SEQRES 2 A 202 HIS HIS ILE VAL LYS GLN ALA LEU GLN ARG TYR SER GLU
SEQRES 3 A 202 ASP ARG ILE GLY LEU ALA ASP TYR ALA LEU GLU SER GLY
SEQRES 4 A 202 GLY ALA SER VAL ILE SER THR ARG CYS SER GLU THR TYR
SEQRES 5 A 202 GLU THR LYS THR ALA LEU LEU SER LEU PHE GLY ILE PRO
SEQRES 6 A 202 LEU TRP TYR HIS SER GLN SER PRO ARG VAL ILE LEU GLN
SEQRES 7 A 202 PRO ASP VAL HIS PRO GLY ASN CYS TRP ALA PHE GLN GLY
SEQRES 8 A 202 PRO GLN GLY PHE ALA VAL VAL ARG LEU SER ALA ARG ILE
SEQRES 9 A 202 ARG PRO THR ALA VAL THR LEU GLU HIS VAL PRO LYS ALA
SEQRES 10 A 202 LEU SER PRO ASN SER THR ILE SER SER ALA PRO LYS ASP
SEQRES 11 A 202 PHE ALA ILE PHE GLY PHE ASP GLU ASP LEU GLN GLN GLU
SEQRES 12 A 202 GLY THR LEU LEU GLY LYS PHE THR TYR ASP GLN ASP GLY
SEQRES 13 A 202 GLU PRO ILE GLN THR PHE HIS PHE GLN ALA PRO THR MET
SEQRES 14 A 202 ALA THR TYR GLN VAL VAL GLU LEU ARG ILE LEU THR ASN
SEQRES 15 A 202 TRP GLY HIS PRO GLU TYR THR CYS ILE TYR ARG PHE ARG
SEQRES 16 A 202 VAL HIS GLY GLU PRO ALA HIS
SEQRES 1 B 35 GLY PRO GLY GLY SER GLY GLU GLU ASP TYR SER CYS THR
SEQRES 2 B 35 GLN ALA ASN ASN PHE ALA ARG SER PHE TYR PRO MET LEU
SEQRES 3 B 35 ARG TYR THR ASN GLY PRO PRO PRO THR
HET DMU A 801 25
HET K A 802 1
HETNAM DMU DECYL-BETA-D-MALTOPYRANOSIDE
HETNAM K POTASSIUM ION
HETSYN DMU DECYLMALTOSIDE
FORMUL 3 DMU C22 H42 O11
FORMUL 4 K K 1+
FORMUL 5 HOH *41(H2 O)
HELIX 1 1 THR A 524 GLU A 541 1 18
HELIX 2 2 LEU A 551 GLY A 555 5 5
HELIX 3 3 SER A 587 GLN A 593 5 7
HELIX 4 4 PRO A 630 THR A 638 5 9
HELIX 5 5 ASN B 6867 SER B 6871 5 5
SHEET 1 A 3 SER A 557 SER A 560 0
SHEET 2 A 3 GLY A 609 GLU A 627 -1 O VAL A 612 N SER A 560
SHEET 3 A 3 ILE A 674 HIS A 678 -1 O PHE A 677 N VAL A 624
SHEET 1 B 5 THR A 660 THR A 666 0
SHEET 2 B 5 ASP A 645 PHE A 651 -1 N ILE A 648 O LEU A 662
SHEET 3 B 5 TYR A 687 ILE A 694 -1 O ARG A 693 N ALA A 647
SHEET 4 B 5 GLY A 609 GLU A 627 -1 N VAL A 613 O VAL A 690
SHEET 5 B 5 ARG A 708 PRO A 715 -1 O ARG A 710 N THR A 625
SHEET 1 C 3 ILE A 579 HIS A 584 0
SHEET 2 C 3 ALA A 572 LEU A 576 -1 N LEU A 576 O ILE A 579
SHEET 3 C 3 MET B6875 TYR B6878 -1 O ARG B6877 N LEU A 573
SHEET 1 D 2 TRP A 602 GLN A 605 0
SHEET 2 D 2 TYR A 703 ILE A 706 -1 O ILE A 706 N TRP A 602
SSBOND 1 CYS A 563 CYS B 6862 1555 3565 2.77
SSBOND 2 CYS A 601 CYS A 705 1555 1555 2.10
LINK O VAL A 590 K K A 802 1555 1555 2.74
LINK O GLN A 593 K K A 802 1555 1555 2.95
LINK O ASP A 595 K K A 802 1555 1555 3.29
LINK O TYR A 707 K K A 802 1555 1555 2.71
SITE 1 AC1 9 GLU A 552 SER A 553 LEU A 574 TRP A 582
SITE 2 AC1 9 GLN A 586 ARG A 589 ASN A 600 HOH A 935
SITE 3 AC1 9 TYR B6878
SITE 1 AC2 5 VAL A 590 GLN A 593 ASP A 595 ASN A 600
SITE 2 AC2 5 TYR A 707
CRYST1 79.320 79.320 260.030 90.00 90.00 120.00 H 3 2 18
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 0.012607 0.007279 0.000000 0.00000
SCALE2 0.000000 0.014557 0.000000 0.00000
SCALE3 0.000000 0.000000 0.003846 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
