HEADER PROTEIN TRANSPORT 03-JUN-03 1PJM
TITLE MOUSE IMPORTIN ALPHA-BIPARTITE NLS FROM HUMAN RETINOBLASTOMA PROTEIN
TITLE 2 COMPLEX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: RETINOBLASTOMA-ASSOCIATED PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: NLS (NUCLEAR LOCALIZATION SIGNAL) BIPARTITE PEPTIDE;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: IMPORTIN ALPHA-2 SUBUNIT;
COMPND 8 CHAIN: B;
COMPND 9 FRAGMENT: NLS BINDING DOMAIN (70-529);
COMPND 10 SYNONYM: KARYOPHERIN ALPHA-2 SUBUNIT;
COMPND 11 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 OTHER_DETAILS: THE PEPTIDE WAS CHEMICALLY SYNTHESIZED. THE SEQUENCE
SOURCE 4 OF THIS PEPTIDE IS NATURALLY FOUND IN HUMAN RETINOBLASTOMA PROTEIN;
SOURCE 5 MOL_ID: 2;
SOURCE 6 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 7 ORGANISM_COMMON: HOUSE MOUSE;
SOURCE 8 ORGANISM_TAXID: 10090;
SOURCE 9 GENE: KPNA2 OR RCH1;
SOURCE 10 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 11 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 12 EXPRESSION_SYSTEM_PLASMID: PET30A
KEYWDS IMPORTIN ALPHA/KARYOPHERIN ALPHA, NUCLEAR LOCALIZATION SEQUENCE (NLS)
KEYWDS 2 RECOGNITION, BIPARTITE NLS, HUMAN RETINOBLASTOMA PROTEIN, PROTEIN
KEYWDS 3 TRANSPORT
EXPDTA X-RAY DIFFRACTION
AUTHOR M.R.M.FONTES,T.TEH,D.JANS,R.I.BRINKWORTH,B.KOBE
REVDAT 4 16-AUG-23 1PJM 1 REMARK
REVDAT 3 27-OCT-21 1PJM 1 SEQADV
REVDAT 2 24-FEB-09 1PJM 1 VERSN
REVDAT 1 19-AUG-03 1PJM 0
JRNL AUTH M.R.M.FONTES,T.TEH,D.JANS,R.I.BRINKWORTH,B.KOBE
JRNL TITL STRUCTURAL BASIS FOR THE SPECIFICITY OF BIPARTITE NUCLEAR
JRNL TITL 2 LOCALIZATION SEQUENCE BINDING BY IMPORTIN-ALPHA
JRNL REF J.BIOL.CHEM. V. 278 27981 2003
JRNL REFN ISSN 0021-9258
JRNL PMID 12695505
JRNL DOI 10.1074/JBC.M303275200
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH M.R.M.FONTES,T.TEH,B.KOBE
REMARK 1 TITL STRUCTURAL BASIS OF RECOGNITION OF MONOPARTITE AND BIPARTITE
REMARK 1 TITL 2 NUCLEAR LOCALIZATION SEQUENCES BY MAMMALIAN IMPORTIN-ALPHA
REMARK 1 REF J.MOL.BIOL. V. 297 1183 2000
REMARK 1 REFN ISSN 0022-2836
REMARK 1 DOI 10.1006/JMBI.2000.3642
REMARK 1 REFERENCE 2
REMARK 1 AUTH B.CATIMEL,T.TEH,M.R.M.FONTES,I.G.JENNINGS,D.JANS,
REMARK 1 AUTH 2 G.J.HOWLETT,E.C.NICE,B.KOBE
REMARK 1 TITL BIOPHYSICAL CHARACTERIZATION OF INTERACTIONS INVOLVING
REMARK 1 TITL 2 IMPOSTIN-ALPHA DURING NUCLEAR IMPORT
REMARK 1 REF J.BIOL.CHEM. V. 276 34189 2001
REMARK 1 REFN ISSN 0021-9258
REMARK 1 DOI 10.1074/JBC.M103531200
REMARK 1 REFERENCE 3
REMARK 1 AUTH B.KOBE
REMARK 1 TITL AUTOINHIBITION BY AN INTERNAL NUCLEAR LOCALIZATION SIGNAL
REMARK 1 TITL 2 REVELED BY THE CRYSTAL STRUCTURE OF MAMMALIAN IMPORTIN ALPHA
REMARK 1 REF NAT.STRUCT.BIOL. V. 6 388 1999
REMARK 1 REFN ISSN 1072-8368
REMARK 1 DOI 10.1038/7625
REMARK 2
REMARK 2 RESOLUTION. 2.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.0
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.57
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 96.0
REMARK 3 NUMBER OF REFLECTIONS : 24323
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 SET) : 0.204
REMARK 3 FREE R VALUE : 0.239
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.800
REMARK 3 FREE R VALUE TEST SET COUNT : 1169
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.007
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.50
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.66
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.20
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 3877
REMARK 3 BIN R VALUE (WORKING SET) : 0.2640
REMARK 3 BIN FREE R VALUE : 0.2990
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.90
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 198
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.021
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3400
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 173
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 53.20
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 46.20
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.60000
REMARK 3 B22 (A**2) : -6.09000
REMARK 3 B33 (A**2) : 6.69000
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) : 0.28
REMARK 3 ESD FROM SIGMAA (A) : 0.25
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.35
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.31
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.006
REMARK 3 BOND ANGLES (DEGREES) : 1.200
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 18.70
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.940
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 1.110 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 1.850 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 1.740 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 2.550 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.36
REMARK 3 BSOL : 38.52
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 3 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : WATER.TOP
REMARK 3 TOPOLOGY FILE 3 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1PJM COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 04-JUN-03.
REMARK 100 THE DEPOSITION ID IS D_1000019367.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-AUG-00
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU RU200
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : MIRRORS
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 25382
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.500
REMARK 200 RESOLUTION RANGE LOW (A) : 99.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.0
REMARK 200 DATA REDUNDANCY : 9.800
REMARK 200 R MERGE (I) : 0.07300
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 19.0000
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 (%) : 98.3
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.40300
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.800
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: PDB ENTRY: 1IAL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 64.01
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.42
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: SODIUM CITRATE, DTT, PH 6.0, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 293K
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 39.50000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 50.49600
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 44.58950
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 50.49600
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 39.50000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 44.58950
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2630 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 18710 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -1.0 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 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 ASN B 70
REMARK 465 VAL B 498
REMARK 465 GLU B 499
REMARK 465 GLU B 500
REMARK 465 GLU B 501
REMARK 465 GLU B 502
REMARK 465 ASP B 503
REMARK 465 GLN B 504
REMARK 465 ASN B 505
REMARK 465 VAL B 506
REMARK 465 VAL B 507
REMARK 465 PRO B 508
REMARK 465 GLU B 509
REMARK 465 THR B 510
REMARK 465 THR B 511
REMARK 465 SER B 512
REMARK 465 GLU B 513
REMARK 465 GLY B 514
REMARK 465 PHE B 515
REMARK 465 ALA B 516
REMARK 465 PHE B 517
REMARK 465 GLN B 518
REMARK 465 VAL B 519
REMARK 465 GLN B 520
REMARK 465 ASP B 521
REMARK 465 GLY B 522
REMARK 465 ALA B 523
REMARK 465 PRO B 524
REMARK 465 GLY B 525
REMARK 465 THR B 526
REMARK 465 PHE B 527
REMARK 465 ASN B 528
REMARK 465 PHE B 529
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 SER B 497 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 SER A 867 -149.57 -54.43
REMARK 500 ASN A 868 -58.48 -157.27
REMARK 500 LYS A 871 159.39 -46.97
REMARK 500 GLU B 107 -54.24 -14.38
REMARK 500 PRO B 111 59.35 -68.00
REMARK 500 ASN B 239 145.04 79.85
REMARK 500 ALA B 389 172.16 169.67
REMARK 500 ASP B 433 102.72 -173.59
REMARK 500 CYS B 467 64.63 -113.86
REMARK 500 HIS B 479 154.48 -43.41
REMARK 500 GLU B 482 -73.69 -39.91
REMARK 500 VAL B 484 -76.66 -64.06
REMARK 500 PHE B 496 -143.32 -122.48
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1EJL RELATED DB: PDB
REMARK 900 IMPORTIN ALPHA - NUCLEOPLASMIN NLS COMPLEX
REMARK 900 RELATED ID: 1EJY RELATED DB: PDB
REMARK 900 IMPORTIN ALPHA - SV40 NLS COMPLEX
REMARK 900 RELATED ID: 1IQ1 RELATED DB: PDB
REMARK 900 IMPORTIN ALPHA - IBB DOMAIN NLS COMPLEX
DBREF 1PJM A 859 878 UNP P06400 RB_HUMAN 857 876
DBREF 1PJM B 70 529 UNP P52293 IMA2_MOUSE 70 529
SEQADV 1PJM CYS A 859 UNP P06400 VAL 858 ENGINEERED MUTATION
SEQADV 1PJM GLY A 860 UNP P06400 LEU 859 ENGINEERED MUTATION
SEQADV 1PJM GLY A 878 UNP P06400 PHE 877 ENGINEERED MUTATION
SEQRES 1 A 20 CYS GLY LYS ARG SER ALA GLU GLY SER ASN PRO PRO LYS
SEQRES 2 A 20 PRO LEU LYS LYS LEU ARG GLY
SEQRES 1 B 460 ASN GLN GLY THR VAL ASN TRP SER VAL GLU ASP ILE VAL
SEQRES 2 B 460 LYS GLY ILE ASN SER ASN ASN LEU GLU SER GLN LEU GLN
SEQRES 3 B 460 ALA THR GLN ALA ALA ARG LYS LEU LEU SER ARG GLU LYS
SEQRES 4 B 460 GLN PRO PRO ILE ASP ASN ILE ILE ARG ALA GLY LEU ILE
SEQRES 5 B 460 PRO LYS PHE VAL SER PHE LEU GLY LYS THR ASP CYS SER
SEQRES 6 B 460 PRO ILE GLN PHE GLU SER ALA TRP ALA LEU THR ASN ILE
SEQRES 7 B 460 ALA SER GLY THR SER GLU GLN THR LYS ALA VAL VAL ASP
SEQRES 8 B 460 GLY GLY ALA ILE PRO ALA PHE ILE SER LEU LEU ALA SER
SEQRES 9 B 460 PRO HIS ALA HIS ILE SER GLU GLN ALA VAL TRP ALA LEU
SEQRES 10 B 460 GLY ASN ILE ALA GLY ASP GLY SER ALA PHE ARG ASP LEU
SEQRES 11 B 460 VAL ILE LYS HIS GLY ALA ILE ASP PRO LEU LEU ALA LEU
SEQRES 12 B 460 LEU ALA VAL PRO ASP LEU SER THR LEU ALA CYS GLY TYR
SEQRES 13 B 460 LEU ARG ASN LEU THR TRP THR LEU SER ASN LEU CYS ARG
SEQRES 14 B 460 ASN LYS ASN PRO ALA PRO PRO LEU ASP ALA VAL GLU GLN
SEQRES 15 B 460 ILE LEU PRO THR LEU VAL ARG LEU LEU HIS HIS ASN ASP
SEQRES 16 B 460 PRO GLU VAL LEU ALA ASP SER CYS TRP ALA ILE SER TYR
SEQRES 17 B 460 LEU THR ASP GLY PRO ASN GLU ARG ILE GLU MET VAL VAL
SEQRES 18 B 460 LYS LYS GLY VAL VAL PRO GLN LEU VAL LYS LEU LEU GLY
SEQRES 19 B 460 ALA THR GLU LEU PRO ILE VAL THR PRO ALA LEU ARG ALA
SEQRES 20 B 460 ILE GLY ASN ILE VAL THR GLY THR ASP GLU GLN THR GLN
SEQRES 21 B 460 LYS VAL ILE ASP ALA GLY ALA LEU ALA VAL PHE PRO SER
SEQRES 22 B 460 LEU LEU THR ASN PRO LYS THR ASN ILE GLN LYS GLU ALA
SEQRES 23 B 460 THR TRP THR MET SER ASN ILE THR ALA GLY ARG GLN ASP
SEQRES 24 B 460 GLN ILE GLN GLN VAL VAL ASN HIS GLY LEU VAL PRO PHE
SEQRES 25 B 460 LEU VAL GLY VAL LEU SER LYS ALA ASP PHE LYS THR GLN
SEQRES 26 B 460 LYS GLU ALA ALA TRP ALA ILE THR ASN TYR THR SER GLY
SEQRES 27 B 460 GLY THR VAL GLU GLN ILE VAL TYR LEU VAL HIS CYS GLY
SEQRES 28 B 460 ILE ILE GLU PRO LEU MET ASN LEU LEU SER ALA LYS ASP
SEQRES 29 B 460 THR LYS ILE ILE GLN VAL ILE LEU ASP ALA ILE SER ASN
SEQRES 30 B 460 ILE PHE GLN ALA ALA GLU LYS LEU GLY GLU THR GLU LYS
SEQRES 31 B 460 LEU SER ILE MET ILE GLU GLU CYS GLY GLY LEU ASP LYS
SEQRES 32 B 460 ILE GLU ALA LEU GLN ARG HIS GLU ASN GLU SER VAL TYR
SEQRES 33 B 460 LYS ALA SER LEU ASN LEU ILE GLU LYS TYR PHE SER VAL
SEQRES 34 B 460 GLU GLU GLU GLU ASP GLN ASN VAL VAL PRO GLU THR THR
SEQRES 35 B 460 SER GLU GLY PHE ALA PHE GLN VAL GLN ASP GLY ALA PRO
SEQRES 36 B 460 GLY THR PHE ASN PHE
FORMUL 3 HOH *173(H2 O)
HELIX 1 1 SER B 77 SER B 87 1 11
HELIX 2 2 ASN B 89 LEU B 104 1 16
HELIX 3 3 PRO B 111 ALA B 118 1 8
HELIX 4 4 LEU B 120 GLY B 129 1 10
HELIX 5 5 LYS B 130 ASP B 132 5 3
HELIX 6 6 CYS B 133 SER B 149 1 17
HELIX 7 7 THR B 151 GLY B 161 1 11
HELIX 8 8 GLY B 162 LEU B 171 1 10
HELIX 9 9 HIS B 175 ASP B 192 1 18
HELIX 10 10 GLY B 193 HIS B 203 1 11
HELIX 11 11 ALA B 205 LEU B 213 1 9
HELIX 12 12 ASP B 217 LEU B 221 5 5
HELIX 13 13 ALA B 222 CYS B 237 1 16
HELIX 14 14 PRO B 245 LEU B 260 1 16
HELIX 15 15 ASP B 264 THR B 279 1 16
HELIX 16 16 PRO B 282 LYS B 291 1 10
HELIX 17 17 VAL B 294 GLY B 303 1 10
HELIX 18 18 GLU B 306 VAL B 321 1 16
HELIX 19 19 THR B 324 ALA B 334 1 11
HELIX 20 20 GLY B 335 ALA B 338 5 4
HELIX 21 21 VAL B 339 LEU B 344 1 6
HELIX 22 22 LYS B 348 THR B 363 1 16
HELIX 23 23 ARG B 366 HIS B 376 1 11
HELIX 24 24 LEU B 378 LYS B 388 1 11
HELIX 25 25 ASP B 390 GLY B 408 1 19
HELIX 26 26 THR B 409 CYS B 419 1 11
HELIX 27 27 ILE B 421 LEU B 429 1 9
HELIX 28 28 ASP B 433 LYS B 453 1 21
HELIX 29 29 GLU B 456 CYS B 467 1 12
HELIX 30 30 GLY B 469 GLU B 474 1 6
HELIX 31 31 ALA B 475 HIS B 479 5 5
HELIX 32 32 ASN B 481 TYR B 495 1 15
CISPEP 1 ASN A 868 PRO A 869 0 -0.17
CISPEP 2 ASN B 241 PRO B 242 0 0.28
CRYST1 79.000 89.179 100.992 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 0.012658 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011213 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009902 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
