HEADER HYDROLASE 10-SEP-01 1JY1
TITLE CRYSTAL STRUCTURE OF HUMAN TYROSYL-DNA PHOSPHODIESTERASE (TDP1)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TYROSYL-DNA PHOSPHODIESTERASE;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RESIDUES 149-608;
COMPND 5 SYNONYM: TDP1;
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 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET15B
KEYWDS PLD SUPERFAMILY, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR D.R.DAVIES,H.INTERTHAL,J.J.CHAMPOUX,W.G.J.HOL
REVDAT 4 27-OCT-21 1JY1 1 SEQADV LINK
REVDAT 3 24-FEB-09 1JY1 1 VERSN
REVDAT 2 01-APR-03 1JY1 1 JRNL
REVDAT 1 20-FEB-02 1JY1 0
JRNL AUTH D.R.DAVIES,H.INTERTHAL,J.J.CHAMPOUX,W.G.HOL
JRNL TITL THE CRYSTAL STRUCTURE OF HUMAN TYROSYL-DNA
JRNL TITL 2 PHOSPHODIESTERASE, TDP1.
JRNL REF STRUCTURE V. 10 237 2002
JRNL REFN ISSN 0969-2126
JRNL PMID 11839309
JRNL DOI 10.1016/S0969-2126(02)00707-4
REMARK 2
REMARK 2 RESOLUTION. 1.69 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.69
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 66989
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.198
REMARK 3 R VALUE (WORKING SET) : 0.198
REMARK 3 FREE R VALUE : 0.229
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 3349
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3505
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 345
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 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): NULL
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): NULL
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 DISTANCE RESTRAINTS. RMS SIGMA
REMARK 3 BOND LENGTH (A) : 0.018 ; NULL
REMARK 3 ANGLE DISTANCE (A) : 1.813 ; NULL
REMARK 3 INTRAPLANAR 1-4 DISTANCE (A) : NULL ; NULL
REMARK 3 H-BOND OR METAL COORDINATION (A) : NULL ; NULL
REMARK 3
REMARK 3 PLANE RESTRAINT (A) : NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINT (A**3) : NULL ; NULL
REMARK 3
REMARK 3 NON-BONDED CONTACT RESTRAINTS.
REMARK 3 SINGLE TORSION (A) : NULL ; NULL
REMARK 3 MULTIPLE TORSION (A) : NULL ; NULL
REMARK 3 H-BOND (X...Y) (A) : NULL ; NULL
REMARK 3 H-BOND (X-H...Y) (A) : NULL ; NULL
REMARK 3
REMARK 3 CONFORMATIONAL TORSION ANGLE RESTRAINTS.
REMARK 3 SPECIFIED (DEGREES) : NULL ; NULL
REMARK 3 PLANAR (DEGREES) : NULL ; NULL
REMARK 3 STAGGERED (DEGREES) : NULL ; NULL
REMARK 3 TRANSVERSE (DEGREES) : NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1JY1 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 21-SEP-01.
REMARK 100 THE DEPOSITION ID IS D_1000014317.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 04-MAY-01
REMARK 200 TEMPERATURE (KELVIN) : 113
REMARK 200 PH : 9.6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 5.0.2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9792,0.9794,0.9640
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 59625
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.690
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.0
REMARK 200 DATA REDUNDANCY : 4.480
REMARK 200 R MERGE (I) : 0.06300
REMARK 200 R SYM (I) : 0.06300
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 13.4200
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.69
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.76
REMARK 200 COMPLETENESS FOR SHELL (%) : 76.4
REMARK 200 DATA REDUNDANCY IN SHELL : 1.98
REMARK 200 R MERGE FOR SHELL (I) : 0.19200
REMARK 200 R SYM FOR SHELL (I) : 19.2000
REMARK 200 <I/SIGMA(I)> FOR SHELL : 10.17
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: MAD
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD
REMARK 200 SOFTWARE USED: SOLVE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 52.33
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.58
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 8000, SODIUM CHLORIDE, CHES,
REMARK 280 SPERMINE, PH 9.6, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -X+1/2,Y+1/2,-Z
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 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 93.22250
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 26.01500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 93.22250
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 26.01500
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: THE BIOLOGICAL ASSEMBLY IS A MONOMER.
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 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 SER A 384
REMARK 465 SER A 385
REMARK 465 MSE A 386
REMARK 465 PRO A 387
REMARK 465 ASN A 388
REMARK 465 LYS A 425
REMARK 465 GLU A 426
REMARK 465 SER A 427
REMARK 465 LYS A 428
REMARK 465 THR A 429
REMARK 465 PRO A 430
REMARK 465 GLY A 431
REMARK 465 LYS A 432
REMARK 465 SER A 433
REMARK 465 GLN A 557
REMARK 465 LYS A 558
REMARK 465 PHE A 559
REMARK 465 PHE A 560
REMARK 465 ALA A 561
REMARK 465 GLY A 562
REMARK 465 SER A 563
REMARK 465 GLN A 564
REMARK 465 GLU A 565
REMARK 465 PRO A 566
REMARK 465 MSE A 567
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 LEU A 145 CG CD1 CD2
REMARK 470 GLU A 390 CG CD OE1 OE2
REMARK 470 LYS A 556 CG CD CE NZ
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 728 O HOH A 816 1.98
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 845 O HOH A 845 2655 1.85
REMARK 500 OG SER A 365 NZ LYS A 380 2655 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 ASP A 159 CB - CG - OD2 ANGL. DEV. = 6.9 DEGREES
REMARK 500 ASP A 209 CB - CG - OD2 ANGL. DEV. = 7.5 DEGREES
REMARK 500 ASP A 407 CB - CG - OD2 ANGL. DEV. = 7.1 DEGREES
REMARK 500 ASP A 551 CB - CG - OD2 ANGL. DEV. = 5.9 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 ARG A 232 -125.34 46.51
REMARK 500 HIS A 290 -69.92 -95.64
REMARK 500 GLU A 390 -100.24 -87.05
REMARK 500 SER A 391 35.60 -81.53
REMARK 500 TRP A 411 -44.23 -156.79
REMARK 500 GLN A 470 53.54 -142.91
REMARK 500 ALA A 482 45.67 -140.74
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1JY1 A 149 608 UNP Q9NUW8 TYDP1_HUMAN 149 608
SEQADV 1JY1 LEU A 145 UNP Q9NUW8 EXPRESSION TAG
SEQADV 1JY1 GLU A 146 UNP Q9NUW8 EXPRESSION TAG
SEQADV 1JY1 ASP A 147 UNP Q9NUW8 EXPRESSION TAG
SEQADV 1JY1 PRO A 148 UNP Q9NUW8 EXPRESSION TAG
SEQADV 1JY1 MSE A 157 UNP Q9NUW8 MET 157 MODIFIED RESIDUE
SEQADV 1JY1 MSE A 266 UNP Q9NUW8 MET 266 MODIFIED RESIDUE
SEQADV 1JY1 MSE A 267 UNP Q9NUW8 MET 267 MODIFIED RESIDUE
SEQADV 1JY1 ASN A 322 UNP Q9NUW8 ASP 322 ENGINEERED MUTATION
SEQADV 1JY1 THR A 328 UNP Q9NUW8 MET 328 ENGINEERED MUTATION
SEQADV 1JY1 MSE A 386 UNP Q9NUW8 MET 386 MODIFIED RESIDUE
SEQADV 1JY1 MSE A 420 UNP Q9NUW8 MET 420 MODIFIED RESIDUE
SEQADV 1JY1 MSE A 491 UNP Q9NUW8 MET 491 MODIFIED RESIDUE
SEQADV 1JY1 MSE A 498 UNP Q9NUW8 MET 498 MODIFIED RESIDUE
SEQADV 1JY1 MSE A 533 UNP Q9NUW8 MET 533 MODIFIED RESIDUE
SEQADV 1JY1 LEU A 548 UNP Q9NUW8 PHE 548 ENGINEERED MUTATION
SEQADV 1JY1 MSE A 567 UNP Q9NUW8 MET 567 MODIFIED RESIDUE
SEQADV 1JY1 MSE A 604 UNP Q9NUW8 MET 604 MODIFIED RESIDUE
SEQRES 1 A 464 LEU GLU ASP PRO GLY GLU GLY GLN ASP ILE TRP ASP MSE
SEQRES 2 A 464 LEU ASP LYS GLY ASN PRO PHE GLN PHE TYR LEU THR ARG
SEQRES 3 A 464 VAL SER GLY VAL LYS PRO LYS TYR ASN SER GLY ALA LEU
SEQRES 4 A 464 HIS ILE LYS ASP ILE LEU SER PRO LEU PHE GLY THR LEU
SEQRES 5 A 464 VAL SER SER ALA GLN PHE ASN TYR CYS PHE ASP VAL ASP
SEQRES 6 A 464 TRP LEU VAL LYS GLN TYR PRO PRO GLU PHE ARG LYS LYS
SEQRES 7 A 464 PRO ILE LEU LEU VAL HIS GLY ASP LYS ARG GLU ALA LYS
SEQRES 8 A 464 ALA HIS LEU HIS ALA GLN ALA LYS PRO TYR GLU ASN ILE
SEQRES 9 A 464 SER LEU CYS GLN ALA LYS LEU ASP ILE ALA PHE GLY THR
SEQRES 10 A 464 HIS HIS THR LYS MSE MSE LEU LEU LEU TYR GLU GLU GLY
SEQRES 11 A 464 LEU ARG VAL VAL ILE HIS THR SER ASN LEU ILE HIS ALA
SEQRES 12 A 464 ASP TRP HIS GLN LYS THR GLN GLY ILE TRP LEU SER PRO
SEQRES 13 A 464 LEU TYR PRO ARG ILE ALA ASP GLY THR HIS LYS SER GLY
SEQRES 14 A 464 GLU SER PRO THR HIS PHE LYS ALA ASN LEU ILE SER TYR
SEQRES 15 A 464 LEU THR ALA TYR ASN ALA PRO SER LEU LYS GLU TRP ILE
SEQRES 16 A 464 ASP VAL ILE HIS LYS HIS ASP LEU SER GLU THR ASN VAL
SEQRES 17 A 464 TYR LEU ILE GLY SER THR PRO GLY ARG PHE GLN GLY SER
SEQRES 18 A 464 GLN LYS ASP ASN TRP GLY HIS PHE ARG LEU LYS LYS LEU
SEQRES 19 A 464 LEU LYS ASP HIS ALA SER SER MSE PRO ASN ALA GLU SER
SEQRES 20 A 464 TRP PRO VAL VAL GLY GLN PHE SER SER VAL GLY SER LEU
SEQRES 21 A 464 GLY ALA ASP GLU SER LYS TRP LEU CYS SER GLU PHE LYS
SEQRES 22 A 464 GLU SER MSE LEU THR LEU GLY LYS GLU SER LYS THR PRO
SEQRES 23 A 464 GLY LYS SER SER VAL PRO LEU TYR LEU ILE TYR PRO SER
SEQRES 24 A 464 VAL GLU ASN VAL ARG THR SER LEU GLU GLY TYR PRO ALA
SEQRES 25 A 464 GLY GLY SER LEU PRO TYR SER ILE GLN THR ALA GLU LYS
SEQRES 26 A 464 GLN ASN TRP LEU HIS SER TYR PHE HIS LYS TRP SER ALA
SEQRES 27 A 464 GLU THR SER GLY ARG SER ASN ALA MSE PRO HIS ILE LYS
SEQRES 28 A 464 THR TYR MSE ARG PRO SER PRO ASP PHE SER LYS ILE ALA
SEQRES 29 A 464 TRP PHE LEU VAL THR SER ALA ASN LEU SER LYS ALA ALA
SEQRES 30 A 464 TRP GLY ALA LEU GLU LYS ASN GLY THR GLN LEU MSE ILE
SEQRES 31 A 464 ARG SER TYR GLU LEU GLY VAL LEU PHE LEU PRO SER ALA
SEQRES 32 A 464 LEU GLY LEU ASP SER PHE LYS VAL LYS GLN LYS PHE PHE
SEQRES 33 A 464 ALA GLY SER GLN GLU PRO MSE ALA THR PHE PRO VAL PRO
SEQRES 34 A 464 TYR ASP LEU PRO PRO GLU LEU TYR GLY SER LYS ASP ARG
SEQRES 35 A 464 PRO TRP ILE TRP ASN ILE PRO TYR VAL LYS ALA PRO ASP
SEQRES 36 A 464 THR HIS GLY ASN MSE TRP VAL PRO SER
MODRES 1JY1 MSE A 157 MET SELENOMETHIONINE
MODRES 1JY1 MSE A 266 MET SELENOMETHIONINE
MODRES 1JY1 MSE A 267 MET SELENOMETHIONINE
MODRES 1JY1 MSE A 420 MET SELENOMETHIONINE
MODRES 1JY1 MSE A 491 MET SELENOMETHIONINE
MODRES 1JY1 MSE A 498 MET SELENOMETHIONINE
MODRES 1JY1 MSE A 533 MET SELENOMETHIONINE
MODRES 1JY1 MSE A 604 MET SELENOMETHIONINE
HET MSE A 157 8
HET MSE A 266 8
HET MSE A 267 8
HET MSE A 420 8
HET MSE A 491 8
HET MSE A 498 8
HET MSE A 533 8
HET MSE A 604 8
HETNAM MSE SELENOMETHIONINE
FORMUL 1 MSE 8(C5 H11 N O2 SE)
FORMUL 2 HOH *345(H2 O)
HELIX 1 1 ASP A 153 MSE A 157 5 5
HELIX 2 2 LYS A 175 SER A 180 5 6
HELIX 3 3 HIS A 184 LEU A 189 1 6
HELIX 4 4 SER A 190 GLY A 194 5 5
HELIX 5 5 ASP A 207 TYR A 215 1 9
HELIX 6 6 PRO A 216 ARG A 220 5 5
HELIX 7 7 LYS A 231 LYS A 243 1 13
HELIX 8 8 ILE A 285 HIS A 290 5 6
HELIX 9 9 HIS A 318 ALA A 329 1 12
HELIX 10 10 TYR A 330 ASN A 331 5 2
HELIX 11 11 ALA A 332 SER A 334 5 3
HELIX 12 12 LEU A 335 LYS A 344 1 10
HELIX 13 13 SER A 365 ASN A 369 5 5
HELIX 14 14 TRP A 370 ALA A 383 1 14
HELIX 15 15 GLU A 415 LEU A 421 1 7
HELIX 16 16 SER A 443 THR A 449 1 7
HELIX 17 17 GLY A 453 LEU A 460 5 8
HELIX 18 18 SER A 463 GLU A 468 1 6
HELIX 19 19 LYS A 469 SER A 475 5 7
HELIX 20 20 ALA A 482 GLY A 486 5 5
HELIX 21 21 SER A 518 GLY A 523 1 6
HELIX 22 22 LEU A 544 GLY A 549 5 6
SHEET 1 A 7 PHE A 166 LEU A 168 0
SHEET 2 A 7 GLY A 295 LEU A 298 -1 O ILE A 296 N TYR A 167
SHEET 3 A 7 LEU A 275 HIS A 280 -1 N ILE A 279 O TRP A 297
SHEET 4 A 7 MSE A 266 TYR A 271 -1 N LEU A 269 O ARG A 276
SHEET 5 A 7 LEU A 196 PHE A 202 -1 N PHE A 202 O MSE A 266
SHEET 6 A 7 ILE A 224 HIS A 228 1 O LEU A 225 N GLN A 201
SHEET 7 A 7 ILE A 248 GLN A 252 1 O SER A 249 N ILE A 224
SHEET 1 B 7 TYR A 353 SER A 357 0
SHEET 2 B 7 GLU A 538 PHE A 543 -1 O LEU A 542 N TYR A 353
SHEET 3 B 7 LYS A 506 THR A 513 -1 N PHE A 510 O PHE A 543
SHEET 4 B 7 LYS A 495 PRO A 500 -1 N TYR A 497 O LEU A 511
SHEET 5 B 7 VAL A 394 GLN A 397 -1 N VAL A 395 O MSE A 498
SHEET 6 B 7 LEU A 437 ILE A 440 1 O ILE A 440 N GLY A 396
SHEET 7 B 7 PHE A 477 HIS A 478 1 O HIS A 478 N LEU A 439
SHEET 1 C 5 TYR A 353 SER A 357 0
SHEET 2 C 5 GLU A 538 PHE A 543 -1 O LEU A 542 N TYR A 353
SHEET 3 C 5 LYS A 506 THR A 513 -1 N PHE A 510 O PHE A 543
SHEET 4 C 5 PHE A 553 VAL A 555 -1 O PHE A 553 N ILE A 507
SHEET 5 C 5 THR A 569 PHE A 570 1 O PHE A 570 N LYS A 554
SHEET 1 D 3 GLY A 360 GLN A 363 0
SHEET 2 D 3 GLN A 531 ILE A 534 -1 O LEU A 532 N PHE A 362
SHEET 3 D 3 ALA A 524 GLU A 526 -1 N GLU A 526 O GLN A 531
LINK C ASP A 156 N MSE A 157 1555 1555 1.32
LINK C MSE A 157 N LEU A 158 1555 1555 1.32
LINK C LYS A 265 N MSE A 266 1555 1555 1.33
LINK C MSE A 266 N MSE A 267 1555 1555 1.33
LINK C MSE A 267 N LEU A 268 1555 1555 1.34
LINK C SER A 419 N MSE A 420 1555 1555 1.33
LINK C MSE A 420 N LEU A 421 1555 1555 1.33
LINK C ALA A 490 N MSE A 491 1555 1555 1.32
LINK C MSE A 491 N PRO A 492 1555 1555 1.33
LINK C TYR A 497 N MSE A 498 1555 1555 1.35
LINK C MSE A 498 N ARG A 499 1555 1555 1.33
LINK C LEU A 532 N MSE A 533 1555 1555 1.32
LINK C MSE A 533 N ILE A 534 1555 1555 1.32
LINK C ASN A 603 N MSE A 604 1555 1555 1.33
LINK C MSE A 604 N TRP A 605 1555 1555 1.32
CISPEP 1 LEU A 576 PRO A 577 0 1.12
CRYST1 186.445 52.030 56.313 90.00 90.00 90.00 P 21 21 2 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 0.005364 0.000000 0.000000 0.00000
SCALE2 0.000000 0.019220 0.000000 0.00000
SCALE3 0.000000 0.000000 0.017758 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
