HEADER SIGNALING PROTEIN, PROTEIN BINDING 27-APR-12 4EWI
TITLE CRYSTAL STRUCTURE OF THE NLRP4 PYRIN DOMAIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: NACHT, LRR AND PYD DOMAINS-CONTAINING PROTEIN 4;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: CANCER/TESTIS ANTIGEN 58, CT58, PAAD AND NACHT-CONTAINING
COMPND 5 PROTEIN 2, PYRIN AND NACHT-CONTAINING PROTEIN 2, PYRIN-CONTAINING
COMPND 6 APAF1-LIKE PROTEIN 4, RIBONUCLEASE INHIBITOR 2;
COMPND 7 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: NLRP4, NALP4, PAN2, PYPAF4, RNH2;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21 STAR DE3;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET28
KEYWDS NLR PROTEINS, DEATH DOMAIN, PYRIN DOMAIN, NLRP4, ASC, INNATE IMMUNE
KEYWDS 2 SYSTEM, INFLAMMASOME, APOPTOSIS, PROTEIN-PROTEIN INTERACTION,
KEYWDS 3 SIGNALING PROTEIN, PROTEIN BINDING
EXPDTA X-RAY DIFFRACTION
AUTHOR C.EIBL,M.HESSENBERGER,S.PUEHRINGER,R.PAGE,K.DIEDERICHS,W.PETI
REVDAT 4 28-FEB-24 4EWI 1 REMARK SEQADV
REVDAT 3 15-NOV-17 4EWI 1 REMARK
REVDAT 2 31-OCT-12 4EWI 1 JRNL
REVDAT 1 05-SEP-12 4EWI 0
JRNL AUTH C.EIBL,S.GRIGORIU,M.HESSENBERGER,J.WENGER,S.PUEHRINGER,
JRNL AUTH 2 A.S.PINHEIRO,R.N.WAGNER,M.PROELL,J.C.REED,R.PAGE,
JRNL AUTH 3 K.DIEDERICHS,W.PETI
JRNL TITL STRUCTURAL AND FUNCTIONAL ANALYSIS OF THE NLRP4 PYRIN
JRNL TITL 2 DOMAIN.
JRNL REF BIOCHEMISTRY V. 51 7330 2012
JRNL REFN ISSN 0006-2960
JRNL PMID 22928810
JRNL DOI 10.1021/BI3007059
REMARK 2
REMARK 2 RESOLUTION. 2.28 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: DEV_1009)
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 : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.28
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 40.76
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 3 NUMBER OF REFLECTIONS : 13245
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.209
REMARK 3 R VALUE (WORKING SET) : 0.207
REMARK 3 FREE R VALUE : 0.246
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.700
REMARK 3 FREE R VALUE TEST SET COUNT : 623
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 40.7653 - 3.6187 1.00 3293 160 0.1801 0.2027
REMARK 3 2 3.6187 - 2.8725 1.00 3148 156 0.2262 0.2803
REMARK 3 3 2.8725 - 2.5095 1.00 3117 146 0.2576 0.3337
REMARK 3 4 2.5095 - 2.2800 0.99 3064 161 0.2794 0.3302
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.20
REMARK 3 SHRINKAGE RADIUS : 0.98
REMARK 3 K_SOL : 0.33
REMARK 3 B_SOL : 49.48
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.250
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.440
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 11.31370
REMARK 3 B22 (A**2) : 11.31370
REMARK 3 B33 (A**2) : -22.62740
REMARK 3 B12 (A**2) : 0.00000
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 : 0.015 1642
REMARK 3 ANGLE : 1.626 2189
REMARK 3 CHIRALITY : 0.090 223
REMARK 3 PLANARITY : 0.009 270
REMARK 3 DIHEDRAL : 16.398 650
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 6
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: ( CHAIN A AND RESID 8:22 )
REMARK 3 ORIGIN FOR THE GROUP (A): 20.4145 36.4216 13.5441
REMARK 3 T TENSOR
REMARK 3 T11: 0.6424 T22: 0.4538
REMARK 3 T33: 0.4459 T12: -0.0063
REMARK 3 T13: 0.0881 T23: 0.0453
REMARK 3 L TENSOR
REMARK 3 L11: 6.4989 L22: 7.6471
REMARK 3 L33: 7.2219 L12: 0.0637
REMARK 3 L13: 2.0421 L23: -3.2234
REMARK 3 S TENSOR
REMARK 3 S11: -0.1395 S12: -0.1502 S13: -0.4062
REMARK 3 S21: -0.2051 S22: 0.0744 S23: -0.0398
REMARK 3 S31: 0.7371 S32: 0.6829 S33: 0.0650
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: ( CHAIN A AND RESID 23:54 )
REMARK 3 ORIGIN FOR THE GROUP (A): 8.2680 33.2832 21.2854
REMARK 3 T TENSOR
REMARK 3 T11: 0.8099 T22: 0.5333
REMARK 3 T33: 0.5912 T12: -0.0904
REMARK 3 T13: 0.1460 T23: 0.0341
REMARK 3 L TENSOR
REMARK 3 L11: 7.6905 L22: 3.5417
REMARK 3 L33: 6.9517 L12: 0.4837
REMARK 3 L13: -1.7232 L23: -0.7690
REMARK 3 S TENSOR
REMARK 3 S11: -0.3378 S12: -0.5653 S13: -0.5379
REMARK 3 S21: 0.3779 S22: 0.0281 S23: 0.4596
REMARK 3 S31: 0.4874 S32: -0.7894 S33: 0.3097
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: ( CHAIN A AND RESID 55:95 )
REMARK 3 ORIGIN FOR THE GROUP (A): 15.1960 44.8650 17.7915
REMARK 3 T TENSOR
REMARK 3 T11: 0.5090 T22: 0.3044
REMARK 3 T33: 0.3760 T12: -0.0176
REMARK 3 T13: 0.0870 T23: -0.0199
REMARK 3 L TENSOR
REMARK 3 L11: 9.9248 L22: 4.6236
REMARK 3 L33: 7.7241 L12: -0.7408
REMARK 3 L13: 1.7486 L23: -0.4932
REMARK 3 S TENSOR
REMARK 3 S11: -0.1492 S12: -0.6642 S13: 0.1411
REMARK 3 S21: 0.2278 S22: 0.2386 S23: 0.1209
REMARK 3 S31: 0.2011 S32: -0.0916 S33: -0.0894
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: ( CHAIN B AND RESID 8:22 )
REMARK 3 ORIGIN FOR THE GROUP (A): 11.9476 56.4083 4.5460
REMARK 3 T TENSOR
REMARK 3 T11: 0.6040 T22: 0.3258
REMARK 3 T33: 0.5012 T12: -0.0476
REMARK 3 T13: -0.0786 T23: -0.0289
REMARK 3 L TENSOR
REMARK 3 L11: 6.3778 L22: 8.6053
REMARK 3 L33: 2.0000 L12: -2.7348
REMARK 3 L13: 1.4434 L23: -4.2029
REMARK 3 S TENSOR
REMARK 3 S11: -0.0718 S12: 0.1876 S13: 0.8153
REMARK 3 S21: 0.8116 S22: -0.1796 S23: 0.2460
REMARK 3 S31: -1.3855 S32: 0.1490 S33: 0.2514
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: ( CHAIN B AND RESID 23:54 )
REMARK 3 ORIGIN FOR THE GROUP (A): 3.1992 49.9851 -5.4976
REMARK 3 T TENSOR
REMARK 3 T11: 0.5375 T22: 0.7885
REMARK 3 T33: 0.5856 T12: 0.0054
REMARK 3 T13: -0.1714 T23: 0.0558
REMARK 3 L TENSOR
REMARK 3 L11: 5.6096 L22: 3.6874
REMARK 3 L33: 8.7822 L12: 0.2832
REMARK 3 L13: 0.5817 L23: 3.2662
REMARK 3 S TENSOR
REMARK 3 S11: 0.0613 S12: 0.8523 S13: -0.3450
REMARK 3 S21: -0.6122 S22: -0.2559 S23: 0.7518
REMARK 3 S31: -0.3241 S32: -1.1082 S33: 0.1946
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: ( CHAIN B AND RESID 55:94 )
REMARK 3 ORIGIN FOR THE GROUP (A): 15.3331 47.2764 0.0801
REMARK 3 T TENSOR
REMARK 3 T11: 0.5768 T22: 0.4603
REMARK 3 T33: 0.3644 T12: -0.0494
REMARK 3 T13: -0.0313 T23: 0.0203
REMARK 3 L TENSOR
REMARK 3 L11: 6.6024 L22: 7.0644
REMARK 3 L33: 4.3052 L12: 1.1306
REMARK 3 L13: -1.0346 L23: -0.2157
REMARK 3 S TENSOR
REMARK 3 S11: -0.1874 S12: 0.5195 S13: -0.1069
REMARK 3 S21: -0.6863 S22: 0.0355 S23: -0.2068
REMARK 3 S31: 0.1878 S32: -0.3420 S33: 0.1519
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 4EWI COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-MAY-12.
REMARK 100 THE DEPOSITION ID IS D_1000072156.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 05-AUG-10
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.2
REMARK 200 NUMBER OF CRYSTALS USED : 2
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : BESSY
REMARK 200 BEAMLINE : 14.1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.91841, 0.97958, 0.97973,
REMARK 200 0.9719
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL MONOCHROMATOR
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RAYONIX MX-225
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 13300
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.280
REMARK 200 RESOLUTION RANGE LOW (A) : 40.760
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 7.700
REMARK 200 R MERGE (I) : 0.05900
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 20.8200
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.28
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.42
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : 7.90
REMARK 200 R MERGE FOR SHELL (I) : 0.82200
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.950
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: MAD
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD
REMARK 200 SOFTWARE USED: SHELXD
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 51.16
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.52
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M DISODIUM TARTRATE, 2.2 M
REMARK 280 AMMONIUM SULFATE, PH 7.2, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+1/3
REMARK 290 6555 -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 83.28800
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 41.64400
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 41.64400
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 83.28800
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3
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: 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 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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
REMARK 350 BIOMOLECULE: 3
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 6990 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 18840 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -76.0 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 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 107.57248
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 41.64400
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH B 310 LIES ON A SPECIAL POSITION.
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 0
REMARK 465 MET A 1
REMARK 465 ALA A 2
REMARK 465 ALA A 3
REMARK 465 SER A 4
REMARK 465 THR A 96
REMARK 465 LYS A 97
REMARK 465 THR A 98
REMARK 465 TYR A 99
REMARK 465 GLN A 100
REMARK 465 ALA A 101
REMARK 465 HIS A 102
REMARK 465 ALA A 103
REMARK 465 LYS A 104
REMARK 465 GLN A 105
REMARK 465 LYS A 106
REMARK 465 PHE A 107
REMARK 465 SER A 108
REMARK 465 ARG A 109
REMARK 465 LEU A 110
REMARK 465 GLU A 111
REMARK 465 GLY B -1
REMARK 465 SER B 0
REMARK 465 MET B 1
REMARK 465 ALA B 2
REMARK 465 ALA B 3
REMARK 465 SER B 4
REMARK 465 TYR B 95
REMARK 465 THR B 96
REMARK 465 LYS B 97
REMARK 465 THR B 98
REMARK 465 TYR B 99
REMARK 465 GLN B 100
REMARK 465 ALA B 101
REMARK 465 HIS B 102
REMARK 465 ALA B 103
REMARK 465 LYS B 104
REMARK 465 GLN B 105
REMARK 465 LYS B 106
REMARK 465 PHE B 107
REMARK 465 SER B 108
REMARK 465 ARG B 109
REMARK 465 LEU B 110
REMARK 465 GLU B 111
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 OE2 GLU B 21 NH2 ARG B 24 2.16
REMARK 500 OE1 GLU A 91 O HOH A 319 2.19
REMARK 500
REMARK 500 REMARK: NULL
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 37 CA - CB - CG ANGL. DEV. = 14.8 DEGREES
REMARK 500 LEU A 37 CB - CG - CD2 ANGL. DEV. = 13.2 DEGREES
REMARK 500 LEU A 39 CB - CG - CD1 ANGL. DEV. = -10.9 DEGREES
REMARK 500 LEU B 39 CA - CB - CG ANGL. DEV. = 15.7 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 GLU A 64 169.98 60.72
REMARK 500 ARG A 81 47.80 -105.23
REMARK 500 ARG A 81 44.91 -103.28
REMARK 500 GLU B 64 169.08 59.30
REMARK 500 ARG B 81 47.80 -102.09
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 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 202
DBREF 4EWI A 1 110 UNP Q96MN2 NALP4_HUMAN 1 110
DBREF 4EWI B 1 110 UNP Q96MN2 NALP4_HUMAN 1 110
SEQADV 4EWI GLY A -1 UNP Q96MN2 EXPRESSION TAG
SEQADV 4EWI SER A 0 UNP Q96MN2 EXPRESSION TAG
SEQADV 4EWI GLU A 111 UNP Q96MN2 CLONING ARTIFACT
SEQADV 4EWI GLY B -1 UNP Q96MN2 EXPRESSION TAG
SEQADV 4EWI SER B 0 UNP Q96MN2 EXPRESSION TAG
SEQADV 4EWI GLU B 111 UNP Q96MN2 CLONING ARTIFACT
SEQRES 1 A 113 GLY SER MET ALA ALA SER PHE PHE SER ASP PHE GLY LEU
SEQRES 2 A 113 MET TRP TYR LEU GLU GLU LEU LYS LYS GLU GLU PHE ARG
SEQRES 3 A 113 LYS PHE LYS GLU HIS LEU LYS GLN MET THR LEU GLN LEU
SEQRES 4 A 113 GLU LEU LYS GLN ILE PRO TRP THR GLU VAL LYS LYS ALA
SEQRES 5 A 113 SER ARG GLU GLU LEU ALA ASN LEU LEU ILE LYS HIS TYR
SEQRES 6 A 113 GLU GLU GLN GLN ALA TRP ASN ILE THR LEU ARG ILE PHE
SEQRES 7 A 113 GLN LYS MET ASP ARG LYS ASP LEU CYS MET LYS VAL MET
SEQRES 8 A 113 ARG GLU ARG THR GLY TYR THR LYS THR TYR GLN ALA HIS
SEQRES 9 A 113 ALA LYS GLN LYS PHE SER ARG LEU GLU
SEQRES 1 B 113 GLY SER MET ALA ALA SER PHE PHE SER ASP PHE GLY LEU
SEQRES 2 B 113 MET TRP TYR LEU GLU GLU LEU LYS LYS GLU GLU PHE ARG
SEQRES 3 B 113 LYS PHE LYS GLU HIS LEU LYS GLN MET THR LEU GLN LEU
SEQRES 4 B 113 GLU LEU LYS GLN ILE PRO TRP THR GLU VAL LYS LYS ALA
SEQRES 5 B 113 SER ARG GLU GLU LEU ALA ASN LEU LEU ILE LYS HIS TYR
SEQRES 6 B 113 GLU GLU GLN GLN ALA TRP ASN ILE THR LEU ARG ILE PHE
SEQRES 7 B 113 GLN LYS MET ASP ARG LYS ASP LEU CYS MET LYS VAL MET
SEQRES 8 B 113 ARG GLU ARG THR GLY TYR THR LYS THR TYR GLN ALA HIS
SEQRES 9 B 113 ALA LYS GLN LYS PHE SER ARG LEU GLU
HET CL A 201 1
HET CL B 201 1
HET SO4 B 202 5
HETNAM CL CHLORIDE ION
HETNAM SO4 SULFATE ION
FORMUL 3 CL 2(CL 1-)
FORMUL 5 SO4 O4 S 2-
FORMUL 6 HOH *40(H2 O)
HELIX 1 1 PHE A 9 GLU A 16 1 8
HELIX 2 2 LYS A 19 LEU A 37 1 19
HELIX 3 3 PRO A 43 ALA A 50 1 8
HELIX 4 4 SER A 51 MET A 79 1 29
HELIX 5 5 ARG A 81 GLY A 94 1 14
HELIX 6 6 PHE B 9 GLU B 16 1 8
HELIX 7 7 LYS B 19 LEU B 37 1 19
HELIX 8 8 PRO B 43 ALA B 50 1 8
HELIX 9 9 SER B 51 MET B 79 1 29
HELIX 10 10 ARG B 81 GLY B 94 1 14
SITE 1 AC1 1 ARG A 52
SITE 1 AC2 1 ARG B 52
SITE 1 AC3 5 ARG A 24 LYS A 25 LYS B 31 TRP B 44
SITE 2 AC3 5 LYS B 48
CRYST1 62.107 62.107 124.932 90.00 90.00 120.00 P 32 2 1 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 0.016101 0.009296 0.000000 0.00000
SCALE2 0.000000 0.018592 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008004 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
