HEADER CYTOKINE 22-JUN-07 2QE3
TITLE CRYSTAL STRUCTURE OF HUMAN TL1A EXTRACELLULAR DOMAIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TNF SUPERFAMILY LIGAND TL1A;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: EXTRACELLULAR DOMAIN, RESIDUES 72-251;
COMPND 5 SYNONYM: TUMOR NECROSIS FACTOR LIGAND, SUPERFAMILY, MEMBER 15;
COMPND 6 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: TNFSF15;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21-AI;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET-28A
KEYWDS TL1A, TNFSF, CYTOKINE;, CYTOKINE
EXPDTA X-RAY DIFFRACTION
AUTHOR C.ZHAN,Q.YAN,Y.PATSKOVSKY,W.SHI,R.TORO,J.BONANNO,S.G.NATHENSON,
AUTHOR 2 S.C.ALMO
REVDAT 5 30-AUG-23 2QE3 1 REMARK SEQADV
REVDAT 4 13-JUL-11 2QE3 1 VERSN
REVDAT 3 29-SEP-09 2QE3 1 JRNL
REVDAT 2 24-FEB-09 2QE3 1 VERSN
REVDAT 1 17-JUL-07 2QE3 0
JRNL AUTH C.ZHAN,Q.YAN,Y.PATSKOVSKY,Z.LI,R.TORO,A.MEYER,H.CHENG,
JRNL AUTH 2 M.BRENOWITZ,S.G.NATHENSON,S.C.ALMO
JRNL TITL BIOCHEMICAL AND STRUCTURAL CHARACTERIZATION OF THE HUMAN
JRNL TITL 2 TL1A ECTODOMAIN.
JRNL REF BIOCHEMISTRY V. 48 7636 2009
JRNL REFN ISSN 0006-2960
JRNL PMID 19522538
JRNL DOI 10.1021/BI900031W
REMARK 2
REMARK 2 RESOLUTION. 2.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.3.0034
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) : 2.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.80
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 10462
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) : 0.211
REMARK 3 R VALUE (WORKING SET) : 0.209
REMARK 3 FREE R VALUE : 0.263
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 3.000
REMARK 3 FREE R VALUE TEST SET COUNT : 323
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) : 2.50
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.57
REMARK 3 REFLECTION IN BIN (WORKING SET) : 735
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 BIN R VALUE (WORKING SET) : 0.3950
REMARK 3 BIN FREE R VALUE SET COUNT : 26
REMARK 3 BIN FREE R VALUE : 0.5250
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1121
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 1
REMARK 3 SOLVENT ATOMS : 59
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 54.50
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 51.14
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.244
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.226
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.187
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 9.456
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.937
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.910
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1173 ; 0.027 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 1596 ; 2.355 ; 1.961
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 145 ;11.062 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 53 ;37.538 ;24.151
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 199 ;20.234 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 5 ;17.171 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 178 ; 0.142 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 889 ; 0.009 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 594 ; 0.244 ; 0.300
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 850 ; 0.355 ; 0.500
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 99 ; 0.255 ; 0.500
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): 38 ; 0.178 ; 0.300
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 13 ; 0.289 ; 0.500
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): 727 ; 9.372 ; 3.000
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1157 ;11.473 ; 3.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 509 ;11.975 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 435 ;14.697 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : 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: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS. THE EXTRA DENSITY NEAR RESIDUE ILE 145 AT THE THREE
REMARK 3 FOLD AXIS IS NOT MODELLED.
REMARK 4
REMARK 4 2QE3 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 25-JUN-07.
REMARK 100 THE DEPOSITION ID IS D_1000043482.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 06-APR-07
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 8.50
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X29A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0809
REMARK 200 MONOCHROMATOR : MIRRORS
REMARK 200 OPTICS : MIRRORS
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 : 10856
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.500
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 21.10
REMARK 200 R MERGE (I) : 0.17000
REMARK 200 R SYM (I) : 0.12400
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 3.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.59
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 10.60
REMARK 200 R MERGE FOR SHELL (I) : 0.56000
REMARK 200 R SYM FOR SHELL (I) : 0.96000
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.700
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 2TNF
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 64.70
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.48
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 10 MM CACL2, 100 MM TRIS, PH 8.50, 20%
REMARK 280 METHONAL, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 290K,
REMARK 280 TEMPERATURE 298.0K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 3 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290 5555 Z,X,Y
REMARK 290 6555 Z+1/2,-X+1/2,-Y
REMARK 290 7555 -Z+1/2,-X,Y+1/2
REMARK 290 8555 -Z,X+1/2,-Y+1/2
REMARK 290 9555 Y,Z,X
REMARK 290 10555 -Y,Z+1/2,-X+1/2
REMARK 290 11555 Y+1/2,-Z+1/2,-X
REMARK 290 12555 -Y+1/2,-Z,X+1/2
REMARK 290 13555 Y+3/4,X+1/4,-Z+1/4
REMARK 290 14555 -Y+3/4,-X+3/4,-Z+3/4
REMARK 290 15555 Y+1/4,-X+1/4,Z+3/4
REMARK 290 16555 -Y+1/4,X+3/4,Z+1/4
REMARK 290 17555 X+3/4,Z+1/4,-Y+1/4
REMARK 290 18555 -X+1/4,Z+3/4,Y+1/4
REMARK 290 19555 -X+3/4,-Z+3/4,-Y+3/4
REMARK 290 20555 X+1/4,-Z+1/4,Y+3/4
REMARK 290 21555 Z+3/4,Y+1/4,-X+1/4
REMARK 290 22555 Z+1/4,-Y+1/4,X+3/4
REMARK 290 23555 -Z+1/4,Y+3/4,X+1/4
REMARK 290 24555 -Z+3/4,-Y+3/4,-X+3/4
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 60.20200
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 60.20200
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 60.20200
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 60.20200
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 60.20200
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 60.20200
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY2 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY1 6 0.000000 0.000000 1.000000 60.20200
REMARK 290 SMTRY2 6 -1.000000 0.000000 0.000000 60.20200
REMARK 290 SMTRY3 6 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY1 7 0.000000 0.000000 -1.000000 60.20200
REMARK 290 SMTRY2 7 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 1.000000 0.000000 60.20200
REMARK 290 SMTRY1 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY2 8 1.000000 0.000000 0.000000 60.20200
REMARK 290 SMTRY3 8 0.000000 -1.000000 0.000000 60.20200
REMARK 290 SMTRY1 9 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 9 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY3 9 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 10 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 10 0.000000 0.000000 1.000000 60.20200
REMARK 290 SMTRY3 10 -1.000000 0.000000 0.000000 60.20200
REMARK 290 SMTRY1 11 0.000000 1.000000 0.000000 60.20200
REMARK 290 SMTRY2 11 0.000000 0.000000 -1.000000 60.20200
REMARK 290 SMTRY3 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 12 0.000000 -1.000000 0.000000 60.20200
REMARK 290 SMTRY2 12 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY3 12 1.000000 0.000000 0.000000 60.20200
REMARK 290 SMTRY1 13 0.000000 1.000000 0.000000 90.30300
REMARK 290 SMTRY2 13 1.000000 0.000000 0.000000 30.10100
REMARK 290 SMTRY3 13 0.000000 0.000000 -1.000000 30.10100
REMARK 290 SMTRY1 14 0.000000 -1.000000 0.000000 90.30300
REMARK 290 SMTRY2 14 -1.000000 0.000000 0.000000 90.30300
REMARK 290 SMTRY3 14 0.000000 0.000000 -1.000000 90.30300
REMARK 290 SMTRY1 15 0.000000 1.000000 0.000000 30.10100
REMARK 290 SMTRY2 15 -1.000000 0.000000 0.000000 30.10100
REMARK 290 SMTRY3 15 0.000000 0.000000 1.000000 90.30300
REMARK 290 SMTRY1 16 0.000000 -1.000000 0.000000 30.10100
REMARK 290 SMTRY2 16 1.000000 0.000000 0.000000 90.30300
REMARK 290 SMTRY3 16 0.000000 0.000000 1.000000 30.10100
REMARK 290 SMTRY1 17 1.000000 0.000000 0.000000 90.30300
REMARK 290 SMTRY2 17 0.000000 0.000000 1.000000 30.10100
REMARK 290 SMTRY3 17 0.000000 -1.000000 0.000000 30.10100
REMARK 290 SMTRY1 18 -1.000000 0.000000 0.000000 30.10100
REMARK 290 SMTRY2 18 0.000000 0.000000 1.000000 90.30300
REMARK 290 SMTRY3 18 0.000000 1.000000 0.000000 30.10100
REMARK 290 SMTRY1 19 -1.000000 0.000000 0.000000 90.30300
REMARK 290 SMTRY2 19 0.000000 0.000000 -1.000000 90.30300
REMARK 290 SMTRY3 19 0.000000 -1.000000 0.000000 90.30300
REMARK 290 SMTRY1 20 1.000000 0.000000 0.000000 30.10100
REMARK 290 SMTRY2 20 0.000000 0.000000 -1.000000 30.10100
REMARK 290 SMTRY3 20 0.000000 1.000000 0.000000 90.30300
REMARK 290 SMTRY1 21 0.000000 0.000000 1.000000 90.30300
REMARK 290 SMTRY2 21 0.000000 1.000000 0.000000 30.10100
REMARK 290 SMTRY3 21 -1.000000 0.000000 0.000000 30.10100
REMARK 290 SMTRY1 22 0.000000 0.000000 1.000000 30.10100
REMARK 290 SMTRY2 22 0.000000 -1.000000 0.000000 30.10100
REMARK 290 SMTRY3 22 1.000000 0.000000 0.000000 90.30300
REMARK 290 SMTRY1 23 0.000000 0.000000 -1.000000 30.10100
REMARK 290 SMTRY2 23 0.000000 1.000000 0.000000 90.30300
REMARK 290 SMTRY3 23 1.000000 0.000000 0.000000 30.10100
REMARK 290 SMTRY1 24 0.000000 0.000000 -1.000000 90.30300
REMARK 290 SMTRY2 24 0.000000 -1.000000 0.000000 90.30300
REMARK 290 SMTRY3 24 -1.000000 0.000000 0.000000 90.30300
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 300 REMARK: THE BIOLOGICAL ASSEMBLY IS A TRIMER GENERATED FROM THE
REMARK 300 MONOMER IN THE ASYMMETRIC UNIT.
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: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA,PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 7040 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 16830 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -122.0 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 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT2 2 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT1 3 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT2 3 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT3 3 1.000000 0.000000 0.000000 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 1
REMARK 465 SER A 2
REMARK 465 HIS A 3
REMARK 465 MET A 4
REMARK 465 LEU A 5
REMARK 465 LYS A 6
REMARK 465 GLY A 7
REMARK 465 GLN A 8
REMARK 465 GLU A 9
REMARK 465 PHE A 10
REMARK 465 ALA A 11
REMARK 465 PRO A 12
REMARK 465 SER A 13
REMARK 465 HIS A 14
REMARK 465 GLN A 15
REMARK 465 GLN A 16
REMARK 465 VAL A 17
REMARK 465 TYR A 18
REMARK 465 ALA A 19
REMARK 465 PRO A 20
REMARK 465 LEU A 21
REMARK 465 ARG A 22
REMARK 465 THR A 40
REMARK 465 GLN A 41
REMARK 465 HIS A 42
REMARK 465 PHE A 43
REMARK 465 LYS A 44
REMARK 465 ASN A 45
REMARK 465 GLN A 46
REMARK 465 MET A 91
REMARK 465 THR A 92
REMARK 465 SER A 93
REMARK 465 GLU A 94
REMARK 465 CYS A 95
REMARK 465 SER A 96
REMARK 465 GLU A 97
REMARK 465 ILE A 98
REMARK 465 ARG A 99
REMARK 465 GLN A 100
REMARK 465 ALA A 101
REMARK 465 GLY A 102
REMARK 465 ARG A 103
REMARK 465 PRO A 104
REMARK 465 ASN A 105
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 LEU A 168 CA - CB - CG ANGL. DEV. = -17.4 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 ASP A 26 -12.80 64.74
REMARK 500 HIS A 54 -2.37 -150.69
REMARK 500 GLU A 55 -29.54 -144.03
REMARK 500 ARG A 64 12.58 89.29
REMARK 500 PRO A 122 16.60 -31.93
REMARK 500 GLU A 136 46.66 -80.36
REMARK 500 ASP A 165 100.96 -164.54
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 TYR A 121 PRO A 122 -121.99
REMARK 500 PRO A 122 GLU A 123 148.51
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 A 701
DBREF 2QE3 A 5 184 UNP Q8NFE9 Q8NFE9_HUMAN 72 251
SEQADV 2QE3 GLY A 1 UNP Q8NFE9 CLONING ARTIFACT
SEQADV 2QE3 SER A 2 UNP Q8NFE9 CLONING ARTIFACT
SEQADV 2QE3 HIS A 3 UNP Q8NFE9 CLONING ARTIFACT
SEQADV 2QE3 MET A 4 UNP Q8NFE9 CLONING ARTIFACT
SEQRES 1 A 184 GLY SER HIS MET LEU LYS GLY GLN GLU PHE ALA PRO SER
SEQRES 2 A 184 HIS GLN GLN VAL TYR ALA PRO LEU ARG ALA ASP GLY ASP
SEQRES 3 A 184 LYS PRO ARG ALA HIS LEU THR VAL VAL ARG GLN THR PRO
SEQRES 4 A 184 THR GLN HIS PHE LYS ASN GLN PHE PRO ALA LEU HIS TRP
SEQRES 5 A 184 GLU HIS GLU LEU GLY LEU ALA PHE THR LYS ASN ARG MET
SEQRES 6 A 184 ASN TYR THR ASN LYS PHE LEU LEU ILE PRO GLU SER GLY
SEQRES 7 A 184 ASP TYR PHE ILE TYR SER GLN VAL THR PHE ARG GLY MET
SEQRES 8 A 184 THR SER GLU CYS SER GLU ILE ARG GLN ALA GLY ARG PRO
SEQRES 9 A 184 ASN LYS PRO ASP SER ILE THR VAL VAL ILE THR LYS VAL
SEQRES 10 A 184 THR ASP SER TYR PRO GLU PRO THR GLN LEU LEU MET GLY
SEQRES 11 A 184 THR LYS SER VAL CYS GLU VAL GLY SER ASN TRP PHE GLN
SEQRES 12 A 184 PRO ILE TYR LEU GLY ALA MET PHE SER LEU GLN GLU GLY
SEQRES 13 A 184 ASP LYS LEU MET VAL ASN VAL SER ASP ILE SER LEU VAL
SEQRES 14 A 184 ASP TYR THR LYS GLU ASP LYS THR PHE PHE GLY ALA PHE
SEQRES 15 A 184 LEU LEU
HET CL A 701 1
HETNAM CL CHLORIDE ION
FORMUL 2 CL CL 1-
FORMUL 3 HOH *59(H2 O)
HELIX 1 1 ASP A 165 VAL A 169 5 5
SHEET 1 A 3 TRP A 52 GLU A 53 0
SHEET 2 A 3 ARG A 29 VAL A 34 -1 N THR A 33 O GLU A 53
SHEET 3 A 3 PHE A 60 LYS A 62 -1 O LYS A 62 N ARG A 29
SHEET 1 B 5 TRP A 52 GLU A 53 0
SHEET 2 B 5 ARG A 29 VAL A 34 -1 N THR A 33 O GLU A 53
SHEET 3 B 5 PHE A 178 LEU A 183 -1 O PHE A 179 N LEU A 32
SHEET 4 B 5 GLY A 78 ARG A 89 -1 N TYR A 83 O GLY A 180
SHEET 5 B 5 PHE A 142 LEU A 153 -1 O GLN A 143 N PHE A 88
SHEET 1 C 5 ASN A 66 THR A 68 0
SHEET 2 C 5 PHE A 71 LEU A 73 -1 O LEU A 73 N ASN A 66
SHEET 3 C 5 LYS A 158 VAL A 163 -1 O LEU A 159 N LEU A 72
SHEET 4 C 5 SER A 109 VAL A 117 -1 N VAL A 113 O ASN A 162
SHEET 5 C 5 THR A 125 SER A 133 -1 O GLY A 130 N VAL A 112
CISPEP 1 GLY A 25 ASP A 26 0 6.50
CISPEP 2 GLY A 138 SER A 139 0 -10.05
SITE 1 AC1 2 LYS A 132 GLN A 143
CRYST1 120.404 120.404 120.404 90.00 90.00 90.00 P 41 3 2 24
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 0.008305 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008305 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008305 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
