HEADER RNA BINDING PROTEIN 26-SEP-11 3TYT
TITLE CRYSTAL STRUCTURE OF A HETEROGENEOUS NUCLEAR RIBONUCLEOPROTEIN L
TITLE 2 (HNRPL) FROM MUS MUSCULUS AT 1.60 A RESOLUTION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HETEROGENEOUS NUCLEAR RIBONUCLEOPROTEIN L;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: MOUSE;
SOURCE 4 ORGANISM_TAXID: 10090;
SOURCE 5 GENE: BC027206, HNRNPL, HNRPL;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: HK100;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: SPEEDET
KEYWDS FERREDOXIN-LIKE, STRUCTURAL GENOMICS, JOINT CENTER FOR STRUCTURAL
KEYWDS 2 GENOMICS, JCSG, PROTEIN STRUCTURE INITIATIVE, PSI-BIOLOGY, RNA
KEYWDS 3 BINDING PROTEIN, PARTNERSHIP FOR STEM CELL BIOLOGY, PARTNERSHIP FOR
KEYWDS 4 T-CELL BIOLOGY, STEMCELL, TCELL
EXPDTA X-RAY DIFFRACTION
AUTHOR JOINT CENTER FOR STRUCTURAL GENOMICS (JCSG),PARTNERSHIP FOR STEM CELL
AUTHOR 2 BIOLOGY (STEMCELL),PARTNERSHIP FOR T-CELL BIOLOGY (TCELL)
REVDAT 5 01-FEB-23 3TYT 1 REMARK SEQADV
REVDAT 4 25-OCT-17 3TYT 1 REMARK
REVDAT 3 21-OCT-15 3TYT 1 AUTHOR
REVDAT 2 23-NOV-11 3TYT 1 AUTHOR
REVDAT 1 16-NOV-11 3TYT 0
JRNL AUTH JOINT CENTER FOR STRUCTURAL GENOMICS (JCSG),
JRNL AUTH 2 PARTNERSHIP FOR STEM CELL BIOLOGY (STEMCELL),
JRNL AUTH 3 PARTNERSHIP FOR T-CELL BIOLOGY (TCELL)
JRNL TITL CRYSTAL STRUCTURE OF A HETEROGENEOUS NUCLEAR
JRNL TITL 2 RIBONUCLEOPROTEIN L (HNRPL) FROM MUS MUSCULUS AT 1.60 A
JRNL TITL 3 RESOLUTION
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0110
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) : 1.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 41.71
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 51174
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) : 0.178
REMARK 3 R VALUE (WORKING SET) : 0.176
REMARK 3 FREE R VALUE : 0.204
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2597
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) : 1.60
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.64
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3531
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.92
REMARK 3 BIN R VALUE (WORKING SET) : 0.2650
REMARK 3 BIN FREE R VALUE SET COUNT : 184
REMARK 3 BIN FREE R VALUE : 0.2710
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1588
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 48
REMARK 3 SOLVENT ATOMS : 216
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 35.62
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.06000
REMARK 3 B22 (A**2) : -0.06000
REMARK 3 B33 (A**2) : 0.08000
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): 0.063
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.066
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.045
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.453
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.967
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.955
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1768 ; 0.015 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 1264 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2384 ; 1.623 ; 1.968
REMARK 3 BOND ANGLES OTHERS (DEGREES): 3096 ; 0.961 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 236 ; 5.967 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 82 ;38.026 ;24.878
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 313 ;12.681 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 8 ;17.522 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 249 ; 0.101 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1989 ; 0.009 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 354 ; 0.003 ; 0.020
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): 1075 ; 0.917 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 429 ; 0.439 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1748 ; 1.640 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 692 ; 2.681 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 621 ; 4.266 ; 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 : 1
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 376 A 579
REMARK 3 ORIGIN FOR THE GROUP (A): 43.2100 -43.0550 9.3590
REMARK 3 T TENSOR
REMARK 3 T11: 0.1071 T22: 0.1121
REMARK 3 T33: 0.0544 T12: -0.0999
REMARK 3 T13: -0.0283 T23: 0.0114
REMARK 3 L TENSOR
REMARK 3 L11: 1.9503 L22: 1.1535
REMARK 3 L33: 1.6458 L12: 0.8208
REMARK 3 L13: 0.1310 L23: -0.3278
REMARK 3 S TENSOR
REMARK 3 S11: -0.1445 S12: 0.1994 S13: 0.0898
REMARK 3 S21: -0.2223 S22: 0.1794 S23: 0.1931
REMARK 3 S31: 0.2325 S32: -0.2669 S33: -0.0349
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 : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: 1. HYDROGENS HAVE BEEN ADDED IN THE
REMARK 3 RIDING POSITIONS. 2. ATOM RECORD CONTAINS SUM OF TLS AND
REMARK 3 RESIDUAL B FACTORS. 3. ANISOU RECORD CONTAINS SUM OF TLS AND
REMARK 3 RESIDUAL U FACTORS. 4. WATERS WERE EXCLUDED FROM AUTOMATIC TLS
REMARK 3 ASSIGNMENT. 5. CHLORIDE (CL) IONS AND 1,2-ETHANEDIOL (EDO)
REMARK 3 MOLECULES FROM THE CRYSTALLIZATION/CRYOPROTECTION SOLUTION ARE
REMARK 3 MODELED.
REMARK 4
REMARK 4 3TYT COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-OCT-11.
REMARK 100 THE DEPOSITION ID IS D_1000068090.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 03-JUN-11
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 3.6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRL
REMARK 200 BEAMLINE : BL14-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL SI(111)
REMARK 200 OPTICS : VERTICAL FOCUSING MIRROR; DOUBLE
REMARK 200 CRYSTAL SI(111) MONOCHROMATOR
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 325 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA 3.3.15
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 51213
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.600
REMARK 200 RESOLUTION RANGE LOW (A) : 41.709
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 10.90
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.07700
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 15.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.69
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 10.90
REMARK 200 R MERGE FOR SHELL (I) : 1.17000
REMARK 200 R SYM FOR SHELL (I) : 1.17000
REMARK 200 <I/SIGMA(I)> FOR SHELL : 0.600
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: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 69.99
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.10
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 2.0M NACL, 10.0% PEG-6000, NO BUFFER
REMARK 280 PH 3.6, VAPOR DIFFUSION, SITTING DROP, NANODROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 64 2 2
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
REMARK 290 5555 Y,-X+Y,Z+1/3
REMARK 290 6555 X-Y,X,Z+2/3
REMARK 290 7555 Y,X,-Z+1/3
REMARK 290 8555 X-Y,-Y,-Z
REMARK 290 9555 -X,-X+Y,-Z+2/3
REMARK 290 10555 -Y,-X,-Z+1/3
REMARK 290 11555 -X+Y,Y,-Z
REMARK 290 12555 X,X-Y,-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 26.88400
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 53.76800
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 0.00000
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 26.88400
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 53.76800
REMARK 290 SMTRY1 7 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 7 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 26.88400
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 9 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 9 0.000000 0.000000 -1.000000 53.76800
REMARK 290 SMTRY1 10 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 10 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 26.88400
REMARK 290 SMTRY1 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 11 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 12 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 12 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 53.76800
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: ANALYTICAL SIZE EXCLUSION CHROMATOGRAPHY SUPPORTS THE
REMARK 300 ASSIGNMENT OF A MONOMER AS A SIGNIFICANT OLIGOMERIZATION STATE IN
REMARK 300 SOLUTION. HOWEVER, THE PROTEIN APPEARS TO HAVE FORMED STABLE DIMERS
REMARK 300 IN THE CRYSTAL LATTICE.
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: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
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: 6220 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 19160 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -56.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
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 63.71200
REMARK 350 BIOMT2 2 0.866025 -0.500000 0.000000 -110.35242
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 53.76800
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 0
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 ASP A 377 CG OD1 OD2
REMARK 470 TYR A 384 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LYS A 415 CD CE NZ
REMARK 470 LYS A 452 CG CD CE NZ
REMARK 470 LYS A 565 CE NZ
REMARK 470 ASN A 568 CG OD1 ND2
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 631
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 632
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 633
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 634
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 635
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 636
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 637
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 638
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 639
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 640
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 641
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 642
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 643
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 644
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 645
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 423426 RELATED DB: TARGETDB
REMARK 900 RELATED ID: 3S01 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF A HETEROGENEOUS NUCLEAR RIBONUCLEASE PROTEIN L
REMARK 900 (HNRPL) FROM MUS MUSCULUS AT 2.15 A RESOLUTION - (MONOCLINIC FORM)
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THE CONSTRUCT WAS EXPRESSED WITH AN N-TERMINAL PURIFICATION TAG
REMARK 999 MGSDKIHHHHHHENLYFQG. THE TAG WAS REMOVED WITH TEV PROTEASE LEAVING
REMARK 999 ONLY A GLYCINE (0) FOLLOWED BY RESIDUES 376-579 OF THE TARGET
REMARK 999 SEQUENCE. NUMBERING IS BASED ON THE UNIPROTKB Q8R081 VERSION 2
REMARK 999 SEQUENCE.
DBREF 3TYT A 376 579 UNP Q8R081 HNRPL_MOUSE 376 579
SEQADV 3TYT GLY A 0 UNP Q8R081 EXPRESSION TAG
SEQRES 1 A 205 GLY ALA ASP SER PRO VAL LEU MET VAL TYR GLY LEU ASP
SEQRES 2 A 205 GLN SER LYS MET ASN CYS ASP ARG VAL PHE ASN VAL PHE
SEQRES 3 A 205 CYS LEU TYR GLY ASN VAL GLU LYS VAL LYS PHE MET LYS
SEQRES 4 A 205 SER LYS PRO GLY ALA ALA MET VAL GLU MET ALA ASP GLY
SEQRES 5 A 205 TYR ALA VAL ASP ARG ALA ILE THR HIS LEU ASN ASN ASN
SEQRES 6 A 205 PHE MET PHE GLY GLN LYS MET ASN VAL CYS VAL SER LYS
SEQRES 7 A 205 GLN PRO ALA ILE MET PRO GLY GLN SER TYR GLY LEU GLU
SEQRES 8 A 205 ASP GLY SER CYS SER TYR LYS ASP PHE SER GLU SER ARG
SEQRES 9 A 205 ASN ASN ARG PHE SER THR PRO GLU GLN ALA ALA LYS ASN
SEQRES 10 A 205 ARG ILE GLN HIS PRO SER ASN VAL LEU HIS PHE PHE ASN
SEQRES 11 A 205 ALA PRO LEU GLU VAL THR GLU GLU ASN PHE PHE GLU ILE
SEQRES 12 A 205 CYS ASP GLU LEU GLY VAL LYS ARG PRO THR SER VAL LYS
SEQRES 13 A 205 VAL PHE SER GLY LYS SER GLU ARG SER SER SER GLY LEU
SEQRES 14 A 205 LEU GLU TRP ASP SER LYS SER ASP ALA LEU GLU THR LEU
SEQRES 15 A 205 GLY PHE LEU ASN HIS TYR GLN MET LYS ASN PRO ASN GLY
SEQRES 16 A 205 PRO TYR PRO TYR THR LEU LYS LEU CYS PHE
HET CL A 631 1
HET CL A 632 1
HET CL A 633 1
HET CL A 634 1
HET EDO A 635 4
HET EDO A 636 4
HET EDO A 637 4
HET EDO A 638 4
HET EDO A 639 4
HET EDO A 640 4
HET EDO A 641 4
HET EDO A 642 4
HET EDO A 643 4
HET EDO A 644 4
HET EDO A 645 4
HETNAM CL CHLORIDE ION
HETNAM EDO 1,2-ETHANEDIOL
HETSYN EDO ETHYLENE GLYCOL
FORMUL 2 CL 4(CL 1-)
FORMUL 6 EDO 11(C2 H6 O2)
FORMUL 17 HOH *216(H2 O)
HELIX 1 1 ASN A 392 CYS A 401 1 10
HELIX 2 2 ASP A 425 ASN A 437 1 13
HELIX 3 3 THR A 484 ALA A 489 1 6
HELIX 4 4 THR A 510 GLY A 522 1 13
HELIX 5 5 SER A 548 ASN A 560 1 13
SHEET 1 A 5 ASN A 447 VAL A 450 0
SHEET 2 A 5 VAL A 380 TYR A 384 -1 N MET A 382 O CYS A 449
SHEET 3 A 5 ALA A 419 MET A 423 -1 O ALA A 419 N VAL A 383
SHEET 4 A 5 VAL A 406 PHE A 411 -1 N GLU A 407 O GLU A 422
SHEET 5 A 5 TYR A 471 ASP A 473 -1 O LYS A 472 N VAL A 409
SHEET 1 B 2 PHE A 440 MET A 441 0
SHEET 2 B 2 GLN A 444 LYS A 445 -1 O GLN A 444 N MET A 441
SHEET 1 C 4 SER A 528 VAL A 531 0
SHEET 2 C 4 SER A 540 GLU A 545 -1 O GLU A 545 N SER A 528
SHEET 3 C 4 VAL A 499 ALA A 505 -1 N LEU A 500 O LEU A 544
SHEET 4 C 4 LYS A 576 CYS A 578 -1 O CYS A 578 N HIS A 501
SHEET 1 D 2 GLN A 563 MET A 564 0
SHEET 2 D 2 TYR A 573 THR A 574 -1 O TYR A 573 N MET A 564
SSBOND 1 CYS A 469 CYS A 469 1555 4545 2.12
SITE 1 AC1 3 LYS A 490 ASN A 504 THR A 574
SITE 1 AC2 4 ARG A 492 ILE A 493 GLN A 494 ARG A 538
SITE 1 AC3 3 PHE A 440 GLY A 443 SER A 550
SITE 1 AC4 2 MET A 564 LYS A 565
SITE 1 AC5 5 LEU A 386 ASP A 387 GLN A 388 SER A 389
SITE 2 AC5 5 GLN A 444
SITE 1 AC6 6 PHE A 397 ASN A 398 ASN A 479 HOH A 745
SITE 2 AC6 6 HOH A 848 HOH A 853
SITE 1 AC7 6 LYS A 524 ARG A 525 THR A 527 TRP A 546
SITE 2 AC7 6 ASP A 547 ASP A 551
SITE 1 AC8 2 GLN A 563 PRO A 572
SITE 1 AC9 6 ASP A 473 PHE A 474 SER A 475 GLU A 476
SITE 2 AC9 6 SER A 477 HOH A 787
SITE 1 BC1 5 PHE A 532 SER A 533 GLY A 534 ASP A 547
SITE 2 BC1 5 HOH A 859
SITE 1 BC2 2 GLY A 522 HOH A 838
SITE 1 BC3 6 PHE A 440 SER A 548 LYS A 549 SER A 550
SITE 2 BC3 6 HOH A 792 HOH A 854
SITE 1 BC4 8 THR A 434 HIS A 435 ASN A 439 HIS A 495
SITE 2 BC4 8 PRO A 496 LYS A 549 HOH A 684 HOH A 831
SITE 1 BC5 7 ASN A 479 HIS A 561 GLN A 563 THR A 574
SITE 2 BC5 7 HOH A 765 HOH A 771 HOH A 848
SITE 1 BC6 4 PRO A 379 ASP A 425 GLY A 426 HOH A 861
CRYST1 127.424 127.424 80.652 90.00 90.00 120.00 P 64 2 2 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 0.007848 0.004531 0.000000 0.00000
SCALE2 0.000000 0.009062 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012399 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
