HEADER TRANSPORT PROTEIN 25-JUL-14 4U5U
TITLE IMPORTIN-ALPHA MINOR NLS SITE INHIBITOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: IMPORTIN SUBUNIT ALPHA-1;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 72-497;
COMPND 5 SYNONYM: IMPORTIN ALPHA P1,KARYOPHERIN SUBUNIT ALPHA-2,PENDULIN,PORE
COMPND 6 TARGETING COMPLEX 58 KDA SUBUNIT,PTAC58,RAG COHORT PROTEIN 1,SRP1-
COMPND 7 ALPHA;
COMPND 8 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: KPNA2, RCH1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS TPX2, TRANSPORT PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR M.STEWART,E.VALKOV,R.S.HOLVEY
REVDAT 2 08-JUL-15 4U5U 1 JRNL
REVDAT 1 13-MAY-15 4U5U 0
JRNL AUTH R.S.HOLVEY,E.VALKOV,D.NEAL,M.STEWART,C.ABELL
JRNL TITL SELECTIVE TARGETING OF THE TPX2 SITE OF IMPORTIN-ALPHA USING
JRNL TITL 2 FRAGMENT-BASED LIGAND DESIGN.
JRNL REF CHEMMEDCHEM V. 10 1232 2015
JRNL REFN ESSN 1860-7187
JRNL PMID 25899172
JRNL DOI 10.1002/CMDC.201500014
REMARK 2
REMARK 2 RESOLUTION. 1.96 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: DEV_1702)
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 : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.96
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 36.61
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 3 NUMBER OF REFLECTIONS : 51651
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.197
REMARK 3 R VALUE (WORKING SET) : 0.195
REMARK 3 FREE R VALUE : 0.216
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2634
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 36.6140 - 5.2253 0.94 2592 156 0.1897 0.2038
REMARK 3 2 5.2253 - 4.1493 1.00 2641 153 0.1627 0.1782
REMARK 3 3 4.1493 - 3.6253 1.00 2626 144 0.1583 0.1768
REMARK 3 4 3.6253 - 3.2941 1.00 2638 111 0.1856 0.2381
REMARK 3 5 3.2941 - 3.0581 1.00 2611 142 0.2019 0.2164
REMARK 3 6 3.0581 - 2.8779 1.00 2565 167 0.2039 0.2069
REMARK 3 7 2.8779 - 2.7338 1.00 2588 138 0.1984 0.2285
REMARK 3 8 2.7338 - 2.6149 1.00 2607 112 0.2030 0.2390
REMARK 3 9 2.6149 - 2.5142 1.00 2584 129 0.2064 0.1920
REMARK 3 10 2.5142 - 2.4275 1.00 2602 125 0.1962 0.2295
REMARK 3 11 2.4275 - 2.3516 1.00 2561 139 0.2054 0.2217
REMARK 3 12 2.3516 - 2.2844 1.00 2557 155 0.2069 0.2411
REMARK 3 13 2.2844 - 2.2242 1.00 2579 120 0.2267 0.2769
REMARK 3 14 2.2242 - 2.1700 1.00 2565 129 0.2359 0.2545
REMARK 3 15 2.1700 - 2.1207 1.00 2570 129 0.2362 0.2512
REMARK 3 16 2.1207 - 2.0755 1.00 2533 153 0.2572 0.3205
REMARK 3 17 2.0755 - 2.0340 1.00 2562 135 0.2704 0.2895
REMARK 3 18 2.0340 - 1.9956 1.00 2514 160 0.2982 0.2981
REMARK 3 19 1.9956 - 1.9600 0.99 2522 137 0.3352 0.3419
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.230
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 21.910
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) : 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 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 : 0.008 3327
REMARK 3 ANGLE : 1.248 4541
REMARK 3 CHIRALITY : 0.047 548
REMARK 3 PLANARITY : 0.006 584
REMARK 3 DIHEDRAL : 14.271 1203
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
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 4U5U COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 28-JUL-14.
REMARK 100 THE DEPOSITION ID IS D_1000202861.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 28-SEP-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID14-4
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9763
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 51660
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.960
REMARK 200 RESOLUTION RANGE LOW (A) : 67.100
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 200 DATA REDUNDANCY : 4.800
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 14.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 68.13
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.86
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: SEE MANUSCRIPT, VAPOR DIFFUSION,
REMARK 280 HANGING DROP, TEMPERATURE 291K
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 39.33350
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 50.04100
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 45.23450
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 50.04100
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 39.33350
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 45.23450
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 300 REMARK: BIOLOGICAL UNIT IS THE SAME AS ASYM.
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 TOTAL BURIED SURFACE AREA: 0 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 18670 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 0.0 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 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 108 CG CD CE NZ
REMARK 470 LYS A 348 CG CD CE NZ
REMARK 470 LYS A 432 CG CD CE NZ
REMARK 470 LYS A 459 CG CD CE NZ
REMARK 470 ARG A 478 CG CD NE CZ NH1 NH2
REMARK 470 TYR A 485 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LYS A 486 CG CD CE NZ
REMARK 470 SER A 497 OG
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 O HOH A 753 O HOH A 784 1.81
REMARK 500 O HOH A 814 O HOH A 877 1.87
REMARK 500 O HOH A 772 O HOH A 862 1.91
REMARK 500 OD2 ASP A 192 O HOH A 844 1.93
REMARK 500 O HOH A 680 O HOH A 875 1.94
REMARK 500 O HOH A 751 O HOH A 856 1.96
REMARK 500 OD2 ASP A 217 O HOH A 601 1.97
REMARK 500 O HOH A 648 O HOH A 819 2.02
REMARK 500 O HOH A 691 O HOH A 767 2.04
REMARK 500 O HOH A 630 O HOH A 662 2.05
REMARK 500 OD1 ASP A 247 O HOH A 843 2.05
REMARK 500 O HOH A 809 O HOH A 814 2.07
REMARK 500 O HOH A 686 O HOH A 802 2.09
REMARK 500 O HOH A 643 O HOH A 658 2.10
REMARK 500 O HOH A 751 O HOH A 825 2.12
REMARK 500 O HOH A 797 O HOH A 868 2.14
REMARK 500 NE1 TRP A 357 O HOH A 788 2.15
REMARK 500 O HOH A 864 O HOH A 866 2.16
REMARK 500 OE1 GLN A 372 O HOH A 807 2.16
REMARK 500 O HOH A 627 O HOH A 692 2.18
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH A 659 O HOH A 666 4555 2.05
REMARK 500 O HOH A 663 O HOH A 858 4455 2.14
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 ASN A 88 56.70 -95.31
REMARK 500 ASP A 433 105.71 -160.24
REMARK 500 GLU A 456 32.32 -140.01
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A 877 DISTANCE = 5.84 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 3D2 A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 3D2 A 502
DBREF 4U5U A 72 497 UNP P52293 IMA1_MOUSE 72 497
SEQRES 1 A 426 GLY THR VAL ASN TRP SER VAL GLU ASP ILE VAL LYS GLY
SEQRES 2 A 426 ILE ASN SER ASN ASN LEU GLU SER GLN LEU GLN ALA THR
SEQRES 3 A 426 GLN ALA ALA ARG LYS LEU LEU SER ARG GLU LYS GLN PRO
SEQRES 4 A 426 PRO ILE ASP ASN ILE ILE ARG ALA GLY LEU ILE PRO LYS
SEQRES 5 A 426 PHE VAL SER PHE LEU GLY LYS THR ASP CYS SER PRO ILE
SEQRES 6 A 426 GLN PHE GLU SER ALA TRP ALA LEU THR ASN ILE ALA SER
SEQRES 7 A 426 GLY THR SER GLU GLN THR LYS ALA VAL VAL ASP GLY GLY
SEQRES 8 A 426 ALA ILE PRO ALA PHE ILE SER LEU LEU ALA SER PRO HIS
SEQRES 9 A 426 ALA HIS ILE SER GLU GLN ALA VAL TRP ALA LEU GLY ASN
SEQRES 10 A 426 ILE ALA GLY ASP GLY SER ALA PHE ARG ASP LEU VAL ILE
SEQRES 11 A 426 LYS HIS GLY ALA ILE ASP PRO LEU LEU ALA LEU LEU ALA
SEQRES 12 A 426 VAL PRO ASP LEU SER THR LEU ALA CYS GLY TYR LEU ARG
SEQRES 13 A 426 ASN LEU THR TRP THR LEU SER ASN LEU CYS ARG ASN LYS
SEQRES 14 A 426 ASN PRO ALA PRO PRO LEU ASP ALA VAL GLU GLN ILE LEU
SEQRES 15 A 426 PRO THR LEU VAL ARG LEU LEU HIS HIS ASN ASP PRO GLU
SEQRES 16 A 426 VAL LEU ALA ASP SER CYS TRP ALA ILE SER TYR LEU THR
SEQRES 17 A 426 ASP GLY PRO ASN GLU ARG ILE GLU MET VAL VAL LYS LYS
SEQRES 18 A 426 GLY VAL VAL PRO GLN LEU VAL LYS LEU LEU GLY ALA THR
SEQRES 19 A 426 GLU LEU PRO ILE VAL THR PRO ALA LEU ARG ALA ILE GLY
SEQRES 20 A 426 ASN ILE VAL THR GLY THR ASP GLU GLN THR GLN LYS VAL
SEQRES 21 A 426 ILE ASP ALA GLY ALA LEU ALA VAL PHE PRO SER LEU LEU
SEQRES 22 A 426 THR ASN PRO LYS THR ASN ILE GLN LYS GLU ALA THR TRP
SEQRES 23 A 426 THR MET SER ASN ILE THR ALA GLY ARG GLN ASP GLN ILE
SEQRES 24 A 426 GLN GLN VAL VAL ASN HIS GLY LEU VAL PRO PHE LEU VAL
SEQRES 25 A 426 GLY VAL LEU SER LYS ALA ASP PHE LYS THR GLN LYS GLU
SEQRES 26 A 426 ALA ALA TRP ALA ILE THR ASN TYR THR SER GLY GLY THR
SEQRES 27 A 426 VAL GLU GLN ILE VAL TYR LEU VAL HIS CYS GLY ILE ILE
SEQRES 28 A 426 GLU PRO LEU MET ASN LEU LEU SER ALA LYS ASP THR LYS
SEQRES 29 A 426 ILE ILE GLN VAL ILE LEU ASP ALA ILE SER ASN ILE PHE
SEQRES 30 A 426 GLN ALA ALA GLU LYS LEU GLY GLU THR GLU LYS LEU SER
SEQRES 31 A 426 ILE MET ILE GLU GLU CYS GLY GLY LEU ASP LYS ILE GLU
SEQRES 32 A 426 ALA LEU GLN ARG HIS GLU ASN GLU SER VAL TYR LYS ALA
SEQRES 33 A 426 SER LEU ASN LEU ILE GLU LYS TYR PHE SER
HET 3D2 A 501 23
HET 3D2 A 502 23
HETNAM 3D2 N~2~-[3-(PYRIDIN-3-YL)BENZYL]-L-LYSINAMIDE
FORMUL 2 3D2 2(C18 H24 N4 O)
FORMUL 4 HOH *282(H2 O)
HELIX 1 AA1 SER A 77 ASN A 86 1 10
HELIX 2 AA2 ASN A 89 ARG A 106 1 18
HELIX 3 AA3 PRO A 111 ALA A 118 1 8
HELIX 4 AA4 LEU A 120 GLY A 129 1 10
HELIX 5 AA5 CYS A 133 SER A 149 1 17
HELIX 6 AA6 THR A 151 GLY A 161 1 11
HELIX 7 AA7 GLY A 162 LEU A 171 1 10
HELIX 8 AA8 HIS A 175 ASP A 192 1 18
HELIX 9 AA9 GLY A 193 HIS A 203 1 11
HELIX 10 AB1 ALA A 205 LEU A 212 1 8
HELIX 11 AB2 ASP A 217 LEU A 221 5 5
HELIX 12 AB3 ALA A 222 CYS A 237 1 16
HELIX 13 AB4 PRO A 245 LEU A 260 1 16
HELIX 14 AB5 ASP A 264 THR A 279 1 16
HELIX 15 AB6 PRO A 282 LYS A 291 1 10
HELIX 16 AB7 VAL A 294 GLY A 303 1 10
HELIX 17 AB8 GLU A 306 VAL A 321 1 16
HELIX 18 AB9 THR A 324 ALA A 334 1 11
HELIX 19 AC1 GLY A 335 ALA A 338 5 4
HELIX 20 AC2 VAL A 339 LEU A 344 1 6
HELIX 21 AC3 LYS A 348 THR A 363 1 16
HELIX 22 AC4 ARG A 366 HIS A 376 1 11
HELIX 23 AC5 GLY A 377 LYS A 388 1 12
HELIX 24 AC6 ASP A 390 GLY A 408 1 19
HELIX 25 AC7 THR A 409 CYS A 419 1 11
HELIX 26 AC8 ILE A 421 LEU A 428 1 8
HELIX 27 AC9 LEU A 429 ALA A 431 5 3
HELIX 28 AD1 ASP A 433 LYS A 453 1 21
HELIX 29 AD2 GLU A 456 CYS A 467 1 12
HELIX 30 AD3 GLY A 468 LEU A 476 1 9
HELIX 31 AD4 ASN A 481 PHE A 496 1 16
CISPEP 1 ASN A 241 PRO A 242 0 -0.80
SITE 1 AC1 7 SER A 360 ASN A 361 ALA A 364 GLU A 396
SITE 2 AC1 7 TRP A 399 ASN A 403 HOH A 762
SITE 1 AC2 7 LYS A 353 GLU A 354 TRP A 357 GLU A 396
SITE 2 AC2 7 HOH A 727 HOH A 745 HOH A 757
CRYST1 78.667 90.469 100.082 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 0.012712 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011054 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009992 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
