HEADER IMMUNE SYSTEM 01-JUL-10 3NSJ
TITLE THE X-RAY CRYSTAL STRUCTURE OF LYMPHOCYTE PERFORIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PERFORIN-1;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: P1, LYMPHOCYTE PORE-FORMING PROTEIN, CYTOLYSIN;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: MOUSE;
SOURCE 4 ORGANISM_TAXID: 10090;
SOURCE 5 GENE: PRF1, PFP;
SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: SF21;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PBACPAK9
KEYWDS PORE FORMING PROTEIN, IMMUNE SYSTEM
EXPDTA X-RAY DIFFRACTION
AUTHOR R.H.LAW,J.C.WHISSTOCK,T.T.CARADOC-DAVIES
REVDAT 4 27-DEC-23 3NSJ 1 HETSYN
REVDAT 3 29-JUL-20 3NSJ 1 COMPND REMARK SEQADV HETNAM
REVDAT 3 2 1 LINK SITE
REVDAT 2 15-DEC-10 3NSJ 1 JRNL
REVDAT 1 03-NOV-10 3NSJ 0
JRNL AUTH R.H.LAW,N.LUKOYANOVA,I.VOSKOBOINIK,T.T.CARADOC-DAVIES,
JRNL AUTH 2 K.BARAN,M.A.DUNSTONE,M.E.D'ANGELO,E.V.ORLOVA,F.COULIBALY,
JRNL AUTH 3 S.VERSCHOOR,K.A.BROWNE,A.CICCONE,M.J.KUIPER,P.I.BIRD,
JRNL AUTH 4 J.A.TRAPANI,H.R.SAIBIL,J.C.WHISSTOCK
JRNL TITL THE STRUCTURAL BASIS FOR MEMBRANE BINDING AND PORE FORMATION
JRNL TITL 2 BY LYMPHOCYTE PERFORIN.
JRNL REF NATURE V. 468 447 2010
JRNL REFN ISSN 0028-0836
JRNL PMID 21037563
JRNL DOI 10.1038/NATURE09518
REMARK 2
REMARK 2 RESOLUTION. 2.75 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER-TNT
REMARK 3 AUTHORS : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,
REMARK 3 : PACIOREK,ROVERSI,SMART,VONRHEIN,WOMACK,
REMARK 3 : MATTHEWS,TEN EYCK,TRONRUD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.75
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 47.36
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 32390
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) : 0.197
REMARK 3 R VALUE (WORKING SET) : 0.196
REMARK 3 FREE R VALUE : 0.215
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.200
REMARK 3 FREE R VALUE TEST SET COUNT : 1683
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 16
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 2.75
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 2.84
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 2869
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2333
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2707
REMARK 3 BIN R VALUE (WORKING SET) : 0.2307
REMARK 3 BIN FREE R VALUE : 0.2758
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.65
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 162
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4036
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 40
REMARK 3 SOLVENT ATOMS : 279
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 85.48
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 80.51
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 13.27150
REMARK 3 B22 (A**2) : -12.47740
REMARK 3 B33 (A**2) : -0.79420
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 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.386
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : NULL
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : NULL
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : NULL
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : NULL
REMARK 3
REMARK 3 REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797
REMARK 3 CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.929
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.928
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 4198 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 5716 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 1383 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : 89 ; 2.000 ; HARMONIC
REMARK 3 GENERAL PLANES : 638 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 4198 ; 20.000 ; HARMONIC
REMARK 3 BAD NON-BONDED CONTACTS : 2 ; 5.000 ; SEMIHARMONIC
REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL
REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL
REMARK 3 CHIRAL IMPROPER TORSION : NULL ; NULL ; NULL
REMARK 3 SUM OF OCCUPANCIES : NULL ; NULL ; NULL
REMARK 3 UTILITY DISTANCES : NULL ; NULL ; NULL
REMARK 3 UTILITY ANGLES : NULL ; NULL ; NULL
REMARK 3 UTILITY TORSION : NULL ; NULL ; NULL
REMARK 3 IDEAL-DIST CONTACT TERM : NULL ; NULL ; NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.007
REMARK 3 BOND ANGLES (DEGREES) : 0.98
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 2.28
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 17.36
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 1
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: { A|21 - A|135 A|137 - A|551 A|652 - A|654 A|701 -
REMARK 3 A|702 A|710 - A|713 A|720 - A|721 A|901 - A|901 }
REMARK 3 ORIGIN FOR THE GROUP (A): 10.7897 16.6897 92.7071
REMARK 3 T TENSOR
REMARK 3 T11: -0.0798 T22: 0.0328
REMARK 3 T33: -0.0264 T12: 0.0459
REMARK 3 T13: -0.0011 T23: 0.0267
REMARK 3 L TENSOR
REMARK 3 L11: 0.4139 L22: 0.7434
REMARK 3 L33: 1.2877 L12: -0.5791
REMARK 3 L13: 0.7771 L23: -1.0808
REMARK 3 S TENSOR
REMARK 3 S11: -0.0139 S12: -0.1102 S13: 0.0365
REMARK 3 S21: 0.0306 S22: 0.0694 S23: 0.0351
REMARK 3 S31: -0.0121 S32: 0.0039 S33: -0.0555
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3NSJ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-JUL-10.
REMARK 100 THE DEPOSITION ID IS D_1000060225.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 25-FEB-10
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : AUSTRALIAN SYNCHROTRON
REMARK 200 BEAMLINE : MX2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.953689
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL MONOCHROMATOR
REMARK 200 (SI111)
REMARK 200 OPTICS : SILICON MIRRORS (ADAPTIVE AND U
REMARK 200 -BENT)
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 32550
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.750
REMARK 200 RESOLUTION RANGE LOW (A) : 86.636
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 16.50
REMARK 200 R MERGE (I) : 0.11000
REMARK 200 R SYM (I) : 0.11000
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) : 2.75
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.90
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 16.90
REMARK 200 R MERGE FOR SHELL (I) : 0.10930
REMARK 200 R SYM FOR SHELL (I) : 0.10930
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.100
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MIRAS
REMARK 200 SOFTWARE USED: SHARP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 75.44
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 5.01
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.5 M SODIUM ACETATE, 0.1 M IMIDAZOLE,
REMARK 280 PH 6.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 295K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
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
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 39.32000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 70.51500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 54.90000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 70.51500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 39.32000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 54.90000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 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 PRO A 136
REMARK 465 ALA A 552
REMARK 465 VAL A 553
REMARK 465 TRP A 554
REMARK 465 HIS A 555
REMARK 465 HIS A 556
REMARK 465 HIS A 557
REMARK 465 HIS A 558
REMARK 465 HIS A 559
REMARK 465 HIS A 560
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 31 CD CE NZ
REMARK 470 GLU A 159 CD OE1 OE2
REMARK 470 GLN A 165 OE1 NE2
REMARK 470 LYS A 185 CE NZ
REMARK 470 LYS A 194 CG CD CE NZ
REMARK 470 ARG A 201 CG CD NE CZ NH1 NH2
REMARK 470 ASP A 251 OD1 OD2
REMARK 470 GLN A 268 CG CD OE1 NE2
REMARK 470 SER A 270 OG
REMARK 470 VAL A 271 CG1 CG2
REMARK 470 GLU A 274 OE1 OE2
REMARK 470 LYS A 276 CD CE NZ
REMARK 470 GLU A 280 CD OE1 OE2
REMARK 470 LYS A 282 CG CD CE NZ
REMARK 470 LYS A 283 CG CD CE NZ
REMARK 470 LYS A 286 CG CD CE NZ
REMARK 470 LEU A 307 CG CD1 CD2
REMARK 470 ASP A 308 CG OD1 OD2
REMARK 470 SER A 309 OG
REMARK 470 THR A 310 OG1 CG2
REMARK 470 GLN A 318 CG CD OE1 NE2
REMARK 470 GLU A 350 CD OE1 OE2
REMARK 470 GLN A 352 CG CD OE1 NE2
REMARK 470 ASN A 375 CG OD1 ND2
REMARK 470 ARG A 378 NE CZ NH1 NH2
REMARK 470 SER A 387 OG
REMARK 470 ASP A 390 CG OD1 OD2
REMARK 470 SER A 391 OG
REMARK 470 GLN A 393 CG CD OE1 NE2
REMARK 470 GLU A 395 CG CD OE1 OE2
REMARK 470 GLN A 397 OE1 NE2
REMARK 470 ASP A 398 CG OD1 OD2
REMARK 470 SER A 399 OG
REMARK 470 LYS A 400 CD CE NZ
REMARK 470 ASN A 403 CG OD1 ND2
REMARK 470 GLN A 404 CD OE1 NE2
REMARK 470 ARG A 409 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 463 CE NZ
REMARK 470 GLU A 467 CD OE1 OE2
REMARK 470 TYR A 486 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LYS A 523 CE NZ
REMARK 470 ASP A 544 CG OD1 OD2
REMARK 470 PRO A 545 CG CD
REMARK 470 ASN A 548 CG OD1 ND2
REMARK 470 ARG A 549 CD NE CZ NH1 NH2
REMARK 470 SER A 550 OG
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 ARG A 70 -0.92 62.66
REMARK 500 HIS A 97 -154.16 -105.29
REMARK 500 ALA A 319 97.62 -67.55
REMARK 500 ASP A 435 65.94 -118.45
REMARK 500 PHE A 442 128.33 -171.90
REMARK 500 ASN A 454 74.08 45.16
REMARK 500 GLU A 467 -129.28 57.31
REMARK 500 TYR A 486 -84.35 -40.43
REMARK 500 HIS A 527 -2.92 98.08
REMARK 500 SER A 550 -179.86 173.14
REMARK 500
REMARK 500 REMARK: NULL
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 CA A 702 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 435 OD1
REMARK 620 2 ASP A 483 OD2 110.3
REMARK 620 3 ALA A 484 O 89.2 104.2
REMARK 620 4 HOH A 955 O 113.8 83.9 151.6
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 701 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 485 O
REMARK 620 2 TRP A 488 O 70.4
REMARK 620 3 ASP A 490 OD1 88.0 104.5
REMARK 620 4 HOH A1053 O 158.1 87.7 97.0
REMARK 620 5 HOH A1059 O 100.0 75.9 171.4 74.4
REMARK 620 N 1 2 3 4
DBREF 3NSJ A 21 554 UNP P10820 PERF_MOUSE 21 554
SEQADV 3NSJ GLU A 213 UNP P10820 ARG 213 ENGINEERED MUTATION
SEQADV 3NSJ HIS A 555 UNP P10820 EXPRESSION TAG
SEQADV 3NSJ HIS A 556 UNP P10820 EXPRESSION TAG
SEQADV 3NSJ HIS A 557 UNP P10820 EXPRESSION TAG
SEQADV 3NSJ HIS A 558 UNP P10820 EXPRESSION TAG
SEQADV 3NSJ HIS A 559 UNP P10820 EXPRESSION TAG
SEQADV 3NSJ HIS A 560 UNP P10820 EXPRESSION TAG
SEQRES 1 A 540 PRO CYS TYR THR ALA THR ARG SER GLU CYS LYS GLN LYS
SEQRES 2 A 540 HIS LYS PHE VAL PRO GLY VAL TRP MET ALA GLY GLU GLY
SEQRES 3 A 540 MET ASP VAL THR THR LEU ARG ARG SER GLY SER PHE PRO
SEQRES 4 A 540 VAL ASN THR GLN ARG PHE LEU ARG PRO ASP ARG THR CYS
SEQRES 5 A 540 THR LEU CYS LYS ASN SER LEU MET ARG ASP ALA THR GLN
SEQRES 6 A 540 ARG LEU PRO VAL ALA ILE THR HIS TRP ARG PRO HIS SER
SEQRES 7 A 540 SER HIS CYS GLN ARG ASN VAL ALA ALA ALA LYS VAL HIS
SEQRES 8 A 540 SER THR GLU GLY VAL ALA ARG GLU ALA ALA ALA ASN ILE
SEQRES 9 A 540 ASN ASN ASP TRP ARG VAL GLY LEU ASP VAL ASN PRO ARG
SEQRES 10 A 540 PRO GLU ALA ASN MET ARG ALA SER VAL ALA GLY SER HIS
SEQRES 11 A 540 SER LYS VAL ALA ASN PHE ALA ALA GLU LYS THR TYR GLN
SEQRES 12 A 540 ASP GLN TYR ASN PHE ASN SER ASP THR VAL GLU CYS ARG
SEQRES 13 A 540 MET TYR SER PHE ARG LEU VAL GLN LYS PRO PRO LEU HIS
SEQRES 14 A 540 LEU ASP PHE LYS LYS ALA LEU ARG ALA LEU PRO ARG ASN
SEQRES 15 A 540 PHE ASN SER SER THR GLU HIS ALA TYR HIS GLU LEU ILE
SEQRES 16 A 540 SER SER TYR GLY THR HIS PHE ILE THR ALA VAL ASP LEU
SEQRES 17 A 540 GLY GLY ARG ILE SER VAL LEU THR ALA LEU ARG THR CYS
SEQRES 18 A 540 GLN LEU THR LEU ASN GLY LEU THR ALA ASP GLU VAL GLY
SEQRES 19 A 540 ASP CYS LEU ASN VAL GLU ALA GLN VAL SER ILE GLY ALA
SEQRES 20 A 540 GLN ALA SER VAL SER SER GLU TYR LYS ALA CYS GLU GLU
SEQRES 21 A 540 LYS LYS LYS GLN HIS LYS MET ALA THR SER PHE HIS GLN
SEQRES 22 A 540 THR TYR ARG GLU ARG HIS VAL GLU VAL LEU GLY GLY PRO
SEQRES 23 A 540 LEU ASP SER THR HIS ASP LEU LEU PHE GLY ASN GLN ALA
SEQRES 24 A 540 THR PRO GLU GLN PHE SER THR TRP THR ALA SER LEU PRO
SEQRES 25 A 540 SER ASN PRO GLY LEU VAL ASP TYR SER LEU GLU PRO LEU
SEQRES 26 A 540 HIS THR LEU LEU GLU GLU GLN ASN PRO LYS ARG GLU ALA
SEQRES 27 A 540 LEU ARG GLN ALA ILE SER HIS TYR ILE MET SER ARG ALA
SEQRES 28 A 540 ARG TRP GLN ASN CYS SER ARG PRO CYS ARG SER GLY GLN
SEQRES 29 A 540 HIS LYS SER SER HIS ASP SER CYS GLN CYS GLU CYS GLN
SEQRES 30 A 540 ASP SER LYS VAL THR ASN GLN ASP CYS CYS PRO ARG GLN
SEQRES 31 A 540 ARG GLY LEU ALA HIS LEU VAL VAL SER ASN PHE ARG ALA
SEQRES 32 A 540 GLU HIS LEU TRP GLY ASP TYR THR THR ALA THR ASP ALA
SEQRES 33 A 540 TYR LEU LYS VAL PHE PHE GLY GLY GLN GLU PHE ARG THR
SEQRES 34 A 540 GLY VAL VAL TRP ASN ASN ASN ASN PRO ARG TRP THR ASP
SEQRES 35 A 540 LYS MET ASP PHE GLU ASN VAL LEU LEU SER THR GLY GLY
SEQRES 36 A 540 PRO LEU ARG VAL GLN VAL TRP ASP ALA ASP TYR GLY TRP
SEQRES 37 A 540 ASP ASP ASP LEU LEU GLY SER CYS ASP ARG SER PRO HIS
SEQRES 38 A 540 SER GLY PHE HIS GLU VAL THR CYS GLU LEU ASN HIS GLY
SEQRES 39 A 540 ARG VAL LYS PHE SER TYR HIS ALA LYS CYS LEU PRO HIS
SEQRES 40 A 540 LEU THR GLY GLY THR CYS LEU GLU TYR ALA PRO GLN GLY
SEQRES 41 A 540 LEU LEU GLY ASP PRO PRO GLY ASN ARG SER GLY ALA VAL
SEQRES 42 A 540 TRP HIS HIS HIS HIS HIS HIS
MODRES 3NSJ ASN A 204 ASN GLYCOSYLATION SITE
HET GOL A 652 6
HET GOL A 653 6
HET GOL A 654 6
HET CA A 701 1
HET CA A 702 1
HET IOD A 710 1
HET IOD A 711 1
HET IOD A 712 1
HET IOD A 713 1
HET CL A 720 1
HET CL A 721 1
HET NAG A 722 14
HETNAM GOL GLYCEROL
HETNAM CA CALCIUM ION
HETNAM IOD IODIDE ION
HETNAM CL CHLORIDE ION
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
HETSYN NAG N-ACETYL-BETA-D-GLUCOSAMINE; 2-ACETAMIDO-2-DEOXY-BETA-
HETSYN 2 NAG D-GLUCOSE; 2-ACETAMIDO-2-DEOXY-D-GLUCOSE; 2-ACETAMIDO-
HETSYN 3 NAG 2-DEOXY-GLUCOSE; N-ACETYL-D-GLUCOSAMINE
FORMUL 2 GOL 3(C3 H8 O3)
FORMUL 5 CA 2(CA 2+)
FORMUL 7 IOD 4(I 1-)
FORMUL 11 CL 2(CL 1-)
FORMUL 13 NAG C8 H15 N O6
FORMUL 14 HOH *279(H2 O)
HELIX 1 1 THR A 26 GLN A 32 1 7
HELIX 2 2 GLY A 39 ALA A 43 5 5
HELIX 3 3 SER A 112 ALA A 122 1 11
HELIX 4 4 SER A 151 ASP A 164 1 14
HELIX 5 5 HIS A 189 ALA A 198 1 10
HELIX 6 6 THR A 207 GLY A 219 1 13
HELIX 7 7 THR A 240 ASN A 246 1 7
HELIX 8 8 THR A 249 ILE A 265 1 17
HELIX 9 9 SER A 272 HIS A 285 1 14
HELIX 10 10 SER A 290 TYR A 295 1 6
HELIX 11 11 PRO A 306 THR A 310 5 5
HELIX 12 12 THR A 320 LEU A 331 1 12
HELIX 13 13 HIS A 346 LEU A 349 5 4
HELIX 14 14 PRO A 354 ARG A 370 1 17
HELIX 15 15 ASN A 403 CYS A 407 5 5
SHEET 1 A 3 CYS A 22 ALA A 25 0
SHEET 2 A 3 CYS A 72 LYS A 76 -1 O LEU A 74 N TYR A 23
SHEET 3 A 3 THR A 84 LEU A 87 -1 O GLN A 85 N CYS A 75
SHEET 1 B 4 GLY A 336 PRO A 344 0
SHEET 2 B 4 HIS A 221 ARG A 239 -1 N GLY A 229 O GLY A 336
SHEET 3 B 4 TYR A 166 LEU A 182 -1 N ASN A 169 O THR A 236
SHEET 4 B 4 ALA A 106 VAL A 110 -1 N ALA A 106 O THR A 172
SHEET 1 C 4 GLY A 46 MET A 47 0
SHEET 2 C 4 HIS A 221 ARG A 239 -1 O HIS A 221 N MET A 47
SHEET 3 C 4 TYR A 166 LEU A 182 -1 N ASN A 169 O THR A 236
SHEET 4 C 4 ILE A 91 PRO A 96 -1 N THR A 92 O ARG A 181
SHEET 1 D 4 ARG A 298 LEU A 303 0
SHEET 2 D 4 HIS A 221 ARG A 239 -1 N SER A 233 O GLU A 301
SHEET 3 D 4 TYR A 166 LEU A 182 -1 N ASN A 169 O THR A 236
SHEET 4 D 4 ILE A 91 PRO A 96 -1 N THR A 92 O ARG A 181
SHEET 1 E 2 GLN A 384 LYS A 386 0
SHEET 2 E 2 CYS A 394 CYS A 396 -1 O GLU A 395 N HIS A 385
SHEET 1 F 4 MET A 464 LEU A 470 0
SHEET 2 F 4 LEU A 413 GLU A 424 -1 N VAL A 418 O MET A 464
SHEET 3 F 4 ARG A 515 CYS A 524 -1 O LYS A 517 N ARG A 422
SHEET 4 F 4 GLY A 503 GLU A 510 -1 N VAL A 507 O PHE A 518
SHEET 1 G 4 GLN A 445 ARG A 448 0
SHEET 2 G 4 ALA A 436 PHE A 442 -1 N VAL A 440 O PHE A 447
SHEET 3 G 4 LEU A 477 ASP A 483 -1 O GLN A 480 N LYS A 439
SHEET 4 G 4 ASP A 491 ARG A 498 -1 O ARG A 498 N LEU A 477
SHEET 1 H 2 LEU A 528 THR A 529 0
SHEET 2 H 2 GLU A 535 TYR A 536 -1 O GLU A 535 N THR A 529
SSBOND 1 CYS A 22 CYS A 75 1555 1555 2.05
SSBOND 2 CYS A 30 CYS A 72 1555 1555 2.04
SSBOND 3 CYS A 101 CYS A 175 1555 1555 2.04
SSBOND 4 CYS A 241 CYS A 407 1555 1555 2.04
SSBOND 5 CYS A 376 CYS A 392 1555 1555 2.03
SSBOND 6 CYS A 380 CYS A 394 1555 1555 2.04
SSBOND 7 CYS A 396 CYS A 406 1555 1555 2.04
SSBOND 8 CYS A 496 CYS A 509 1555 1555 2.03
SSBOND 9 CYS A 524 CYS A 533 1555 1555 2.04
LINK ND2 ASN A 204 C1 NAG A 722 1555 1555 1.52
LINK OD1 ASP A 435 CA CA A 702 1555 1555 2.40
LINK OD2 ASP A 483 CA CA A 702 1555 1555 2.45
LINK O ALA A 484 CA CA A 702 1555 1555 2.46
LINK O ASP A 485 CA CA A 701 1555 1555 2.24
LINK O TRP A 488 CA CA A 701 1555 1555 2.73
LINK OD1 ASP A 490 CA CA A 701 1555 1555 2.23
LINK CA CA A 701 O HOH A1053 1555 1555 2.51
LINK CA CA A 701 O HOH A1059 1555 1555 3.05
LINK CA CA A 702 O HOH A 955 1555 1555 2.73
CISPEP 1 GLY A 474 GLY A 475 0 3.22
CRYST1 78.640 109.800 141.030 90.00 90.00 90.00 P 21 21 21 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 0.012716 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009107 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007091 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
