HEADER OXIDOREDUCTASE, TRANSFERASE 24-AUG-09 3IRM
TITLE TRYPANOSOMA CRUZI DIHYDROFOLATE REDUCTASE-THYMIDYLATE SYNTHASE
TITLE 2 COMPLEXED WITH CYCLOGUANIL
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BIFUNCTIONAL DIHYDROFOLATE REDUCTASE-THYMIDYLATE SYNTHASE;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 SYNONYM: DHFR-TS, DIHYDROFOLATE REDUCTASE, THYMIDYLATE SYNTHASE;
COMPND 5 EC: 1.5.1.3, 2.1.1.45;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: TRYPANOSOMA CRUZI;
SOURCE 3 ORGANISM_TAXID: 5693;
SOURCE 4 STRAIN: Y;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3) PLYSS;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET11C
KEYWDS TRYPANOSOMA CRUZI, DHFR-TS ANTIFOLATE COMPLEX, METHYLTRANSFERASE,
KEYWDS 2 MULTIFUNCTIONAL ENZYME, NADP, NUCLEOTIDE BIOSYNTHESIS, ONE-CARBON
KEYWDS 3 METABOLISM, OXIDOREDUCTASE, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR P.CHITNUMSUB,J.YUVANIYAMA,Y.YUTHAVONG
REVDAT 3 06-SEP-23 3IRM 1 REMARK
REVDAT 2 01-NOV-17 3IRM 1 REMARK
REVDAT 1 28-JUL-10 3IRM 0
JRNL AUTH P.CHITNUMSUB,J.YUVANIYAMA,T.VILAIVAN,J.VANICHTANANKUL,
JRNL AUTH 2 S.KAMCHONWONGPAISAN,Y.YUTHAVONG
JRNL TITL STRUCTURAL BASIS OF ANTIFOLATE INHIBITION OF TRYPANOSOMA
JRNL TITL 2 CRUZI DIHYDROFOLATE REDUCTASE-THYMIDYLATE SYNTHASE
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.2
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) : 2.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.97
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 91.5
REMARK 3 NUMBER OF REFLECTIONS : 109675
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) : 0.202
REMARK 3 FREE R VALUE : 0.245
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 5504
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.003
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.10
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.20
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 78.90
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 11224
REMARK 3 BIN R VALUE (WORKING SET) : 0.2430
REMARK 3 BIN FREE R VALUE : 0.2910
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.80
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 570
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.012
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 16462
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 140
REMARK 3 SOLVENT ATOMS : 653
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 31.00
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 34.07
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -2.72000
REMARK 3 B22 (A**2) : 1.25000
REMARK 3 B33 (A**2) : 1.47000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 1.03000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.24
REMARK 3 ESD FROM SIGMAA (A) : 0.19
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) : 0.30
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.24
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.006
REMARK 3 BOND ANGLES (DEGREES) : 1.400
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : OVERALL
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 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : CNS BULK SOLVENT MODEL USED
REMARK 3 KSOL : 0.40
REMARK 3 BSOL : 51.51
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 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3IRM COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 26-AUG-09.
REMARK 100 THE DEPOSITION ID IS D_1000054778.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 21-NOV-05
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SPRING-8
REMARK 200 BEAMLINE : BL38B1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9
REMARK 200 MONOCHROMATOR : MIRROR
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO, HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 109675
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100
REMARK 200 RESOLUTION RANGE LOW (A) : 29.970
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 91.6
REMARK 200 DATA REDUNDANCY : 2.800
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.10300
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.18
REMARK 200 COMPLETENESS FOR SHELL (%) : 79.8
REMARK 200 DATA REDUNDANCY IN SHELL : 2.60
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.40800
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: A PARTIALLY REFINED STRUCTURE OF 3INV
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 44.80
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.23
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG4000, NH4OAC, PH 5.6, MICROBATCH,
REMARK 280 TEMPERATURE 297K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 82.89600
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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: 6100 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 43890 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -47.0 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
REMARK 350 BIOMOLECULE: 2
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: 5550 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 43010 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -44.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D
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 VAL A 521
REMARK 465 MET B 1
REMARK 465 SER B 2
REMARK 465 MET C 1
REMARK 465 LYS C 518
REMARK 465 MET C 519
REMARK 465 ALA C 520
REMARK 465 VAL C 521
REMARK 465 MET D 1
REMARK 465 SER D 2
REMARK 465 SER D 516
REMARK 465 MET D 517
REMARK 465 LYS D 518
REMARK 465 MET D 519
REMARK 465 ALA D 520
REMARK 465 VAL D 521
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 2 -85.12 34.90
REMARK 500 GLU A 14 -67.01 -27.99
REMARK 500 THR A 16 -14.63 -155.20
REMARK 500 ARG A 39 -20.14 -144.70
REMARK 500 PRO A 42 3.98 -57.42
REMARK 500 ASN A 44 73.61 -111.72
REMARK 500 ASN A 63 8.75 86.87
REMARK 500 PRO A 86 -30.47 -39.00
REMARK 500 GLU A 184 15.45 56.89
REMARK 500 CYS A 187 -149.29 -97.70
REMARK 500 SER A 188 -47.64 -136.84
REMARK 500 ASN A 219 -158.32 -55.45
REMARK 500 LYS A 285 118.44 -162.31
REMARK 500 LEU A 331 46.78 -98.99
REMARK 500 PRO A 341 53.21 -69.98
REMARK 500 TYR A 343 -100.04 18.72
REMARK 500 HIS A 349 49.34 -143.66
REMARK 500 THR A 355 -73.40 -122.00
REMARK 500 MET A 517 158.60 86.80
REMARK 500 LYS A 518 -160.38 -128.83
REMARK 500 MET A 519 -42.23 95.41
REMARK 500 GLU B 31 -6.64 -58.35
REMARK 500 ASP B 37 -111.67 -81.11
REMARK 500 ARG B 39 69.11 91.84
REMARK 500 ILE B 41 -1.26 -154.60
REMARK 500 PRO B 42 -10.58 -46.22
REMARK 500 LYS B 62 70.25 -66.24
REMARK 500 ASN B 63 -27.67 175.97
REMARK 500 THR B 102 -44.56 -150.30
REMARK 500 PRO B 113 -93.68 -42.12
REMARK 500 ARG B 118 1.27 -68.57
REMARK 500 ARG B 181 40.96 -82.46
REMARK 500 PRO B 280 53.45 -67.30
REMARK 500 LEU B 331 59.19 -92.54
REMARK 500 MET B 337 -4.46 79.43
REMARK 500 PRO B 341 57.93 -65.51
REMARK 500 TYR B 343 -106.82 28.01
REMARK 500 THR B 355 -65.55 -124.89
REMARK 500 ASN B 468 39.64 -83.28
REMARK 500 SER B 516 82.79 -66.49
REMARK 500 LYS B 518 84.88 -8.23
REMARK 500 ALA B 520 -146.86 170.69
REMARK 500 ARG C 39 -42.41 -139.94
REMARK 500 ILE C 41 70.62 -112.73
REMARK 500 PRO C 42 -24.43 -35.17
REMARK 500 ASN C 44 69.08 -103.33
REMARK 500 LYS C 62 179.38 -38.97
REMARK 500 ALA C 182 -158.69 -166.85
REMARK 500 SER C 183 53.56 -154.31
REMARK 500 VAL C 189 97.71 62.98
REMARK 500
REMARK 500 THIS ENTRY HAS 75 RAMACHANDRAN OUTLIERS.
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 1CY A 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 705
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A 801
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A 802
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A 803
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1CY B 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 B 702
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 B 706
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT B 804
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT B 805
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT B 806
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1CY C 603
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 C 703
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 C 707
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT C 807
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1CY D 604
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 D 704
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 D 708
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT D 808
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3CL9 RELATED DB: PDB
REMARK 900 TCDHFR-TS PROTEIN IN COMPLEX WITH MTX
REMARK 900 RELATED ID: 3HBB RELATED DB: PDB
REMARK 900 TCDHFR-TS PROTEIN IN COMPLEX WITH TMQ
REMARK 900 RELATED ID: 2H2Q RELATED DB: PDB
REMARK 900 TCDHFR-TS PROTEIN IN FOLATE-FREE STATE
REMARK 900 RELATED ID: 3CLB RELATED DB: PDB
REMARK 900 TCDHFR-TS PROTEIN IN COMPLEX WITH TMQ (OLDER REFINEMENT)
REMARK 900 RELATED ID: 3INV RELATED DB: PDB
REMARK 900 TCDHFR-TS PROTEIN IN COMPLEX WITH NADPH, DUMP AND C-448 ANTIFOLATE
REMARK 900 RELATED ID: 3IRN RELATED DB: PDB
REMARK 900 TCDHFR-TS PROTEIN IN COMPLEX WITH NADPH AND CYCLOGUANIL
REMARK 900 RELATED ID: 3IRO RELATED DB: PDB
REMARK 900 TCDHFR-TS PROTEIN IN COMPLEX WITH NADPH NADPH AND Q-8 ANTIFOLATE
DBREF 3IRM A 1 521 UNP Q27793 DRTS_TRYCR 1 521
DBREF 3IRM B 1 521 UNP Q27793 DRTS_TRYCR 1 521
DBREF 3IRM C 1 521 UNP Q27793 DRTS_TRYCR 1 521
DBREF 3IRM D 1 521 UNP Q27793 DRTS_TRYCR 1 521
SEQRES 1 A 521 MET SER LEU PHE LYS ILE ARG MET PRO GLU THR VAL ALA
SEQRES 2 A 521 GLU GLY THR ARG LEU ALA LEU ARG ALA PHE SER LEU VAL
SEQRES 3 A 521 VAL ALA VAL ASP GLU HIS GLY GLY ILE GLY ASP GLY ARG
SEQRES 4 A 521 SER ILE PRO TRP ASN VAL PRO GLU ASP MET LYS PHE PHE
SEQRES 5 A 521 ARG ASP LEU THR THR LYS LEU ARG GLY LYS ASN VAL LYS
SEQRES 6 A 521 PRO SER PRO ALA LYS ARG ASN ALA VAL VAL MET GLY ARG
SEQRES 7 A 521 LYS THR TRP ASP SER ILE PRO PRO LYS PHE ARG PRO LEU
SEQRES 8 A 521 PRO GLY ARG LEU ASN VAL VAL LEU SER SER THR LEU THR
SEQRES 9 A 521 THR GLN HIS LEU LEU ASP GLY LEU PRO ASP GLU GLU LYS
SEQRES 10 A 521 ARG ASN LEU HIS ALA ASP SER ILE VAL ALA VAL ASN GLY
SEQRES 11 A 521 GLY LEU GLU GLN ALA LEU ARG LEU LEU ALA SER PRO ASN
SEQRES 12 A 521 TYR THR PRO SER ILE GLU THR VAL TYR CYS ILE GLY GLY
SEQRES 13 A 521 GLY SER VAL TYR ALA GLU ALA LEU ARG PRO PRO CYS VAL
SEQRES 14 A 521 HIS LEU LEU GLN ALA ILE TYR ARG THR THR ILE ARG ALA
SEQRES 15 A 521 SER GLU SER SER CYS SER VAL PHE PHE ARG VAL PRO GLU
SEQRES 16 A 521 SER GLY THR GLU ALA ALA ALA GLY ILE GLU TRP GLN ARG
SEQRES 17 A 521 GLU THR ILE SER GLU GLU LEU THR SER ALA ASN GLY ASN
SEQRES 18 A 521 GLU THR LYS TYR TYR PHE GLU LYS LEU ILE PRO ARG ASN
SEQRES 19 A 521 ARG GLU GLU GLU GLN TYR LEU SER LEU VAL ASP ARG ILE
SEQRES 20 A 521 ILE ARG GLU GLY ASN VAL LYS HIS ASP ARG THR GLY VAL
SEQRES 21 A 521 GLY THR LEU SER ILE PHE GLY ALA GLN MET ARG PHE SER
SEQRES 22 A 521 LEU ARG ASN ASN ARG LEU PRO LEU LEU THR THR LYS ARG
SEQRES 23 A 521 VAL PHE TRP ARG GLY VAL CYS GLU GLU LEU LEU TRP PHE
SEQRES 24 A 521 LEU ARG GLY GLU THR TYR ALA LYS LYS LEU SER ASP LYS
SEQRES 25 A 521 GLY VAL HIS ILE TRP ASP ASP ASN GLY SER ARG ALA PHE
SEQRES 26 A 521 LEU ASP SER ARG GLY LEU THR GLU TYR GLU GLU MET ASP
SEQRES 27 A 521 LEU GLY PRO VAL TYR GLY PHE GLN TRP ARG HIS PHE GLY
SEQRES 28 A 521 ALA ALA TYR THR HIS HIS ASP ALA ASN TYR ASP GLY GLN
SEQRES 29 A 521 GLY VAL ASP GLN ILE LYS ALA ILE VAL GLU THR LEU LYS
SEQRES 30 A 521 THR ASN PRO ASP ASP ARG ARG MET LEU PHE THR ALA TRP
SEQRES 31 A 521 ASN PRO SER ALA LEU PRO ARG MET ALA LEU PRO PRO CYS
SEQRES 32 A 521 HIS LEU LEU ALA GLN PHE TYR VAL SER ASN GLY GLU LEU
SEQRES 33 A 521 SER CYS MET LEU TYR GLN ARG SER CYS ASP MET GLY LEU
SEQRES 34 A 521 GLY VAL PRO PHE ASN ILE ALA SER TYR ALA LEU LEU THR
SEQRES 35 A 521 ILE LEU ILE ALA LYS ALA THR GLY LEU ARG PRO GLY GLU
SEQRES 36 A 521 LEU VAL HIS THR LEU GLY ASP ALA HIS VAL TYR SER ASN
SEQRES 37 A 521 HIS VAL GLU PRO CYS ASN GLU GLN LEU LYS ARG VAL PRO
SEQRES 38 A 521 ARG ALA PHE PRO TYR LEU VAL PHE ARG ARG GLU ARG GLU
SEQRES 39 A 521 PHE LEU GLU ASP TYR GLU GLU GLY ASP MET GLU VAL ILE
SEQRES 40 A 521 ASP TYR ALA PRO TYR PRO PRO ILE SER MET LYS MET ALA
SEQRES 41 A 521 VAL
SEQRES 1 B 521 MET SER LEU PHE LYS ILE ARG MET PRO GLU THR VAL ALA
SEQRES 2 B 521 GLU GLY THR ARG LEU ALA LEU ARG ALA PHE SER LEU VAL
SEQRES 3 B 521 VAL ALA VAL ASP GLU HIS GLY GLY ILE GLY ASP GLY ARG
SEQRES 4 B 521 SER ILE PRO TRP ASN VAL PRO GLU ASP MET LYS PHE PHE
SEQRES 5 B 521 ARG ASP LEU THR THR LYS LEU ARG GLY LYS ASN VAL LYS
SEQRES 6 B 521 PRO SER PRO ALA LYS ARG ASN ALA VAL VAL MET GLY ARG
SEQRES 7 B 521 LYS THR TRP ASP SER ILE PRO PRO LYS PHE ARG PRO LEU
SEQRES 8 B 521 PRO GLY ARG LEU ASN VAL VAL LEU SER SER THR LEU THR
SEQRES 9 B 521 THR GLN HIS LEU LEU ASP GLY LEU PRO ASP GLU GLU LYS
SEQRES 10 B 521 ARG ASN LEU HIS ALA ASP SER ILE VAL ALA VAL ASN GLY
SEQRES 11 B 521 GLY LEU GLU GLN ALA LEU ARG LEU LEU ALA SER PRO ASN
SEQRES 12 B 521 TYR THR PRO SER ILE GLU THR VAL TYR CYS ILE GLY GLY
SEQRES 13 B 521 GLY SER VAL TYR ALA GLU ALA LEU ARG PRO PRO CYS VAL
SEQRES 14 B 521 HIS LEU LEU GLN ALA ILE TYR ARG THR THR ILE ARG ALA
SEQRES 15 B 521 SER GLU SER SER CYS SER VAL PHE PHE ARG VAL PRO GLU
SEQRES 16 B 521 SER GLY THR GLU ALA ALA ALA GLY ILE GLU TRP GLN ARG
SEQRES 17 B 521 GLU THR ILE SER GLU GLU LEU THR SER ALA ASN GLY ASN
SEQRES 18 B 521 GLU THR LYS TYR TYR PHE GLU LYS LEU ILE PRO ARG ASN
SEQRES 19 B 521 ARG GLU GLU GLU GLN TYR LEU SER LEU VAL ASP ARG ILE
SEQRES 20 B 521 ILE ARG GLU GLY ASN VAL LYS HIS ASP ARG THR GLY VAL
SEQRES 21 B 521 GLY THR LEU SER ILE PHE GLY ALA GLN MET ARG PHE SER
SEQRES 22 B 521 LEU ARG ASN ASN ARG LEU PRO LEU LEU THR THR LYS ARG
SEQRES 23 B 521 VAL PHE TRP ARG GLY VAL CYS GLU GLU LEU LEU TRP PHE
SEQRES 24 B 521 LEU ARG GLY GLU THR TYR ALA LYS LYS LEU SER ASP LYS
SEQRES 25 B 521 GLY VAL HIS ILE TRP ASP ASP ASN GLY SER ARG ALA PHE
SEQRES 26 B 521 LEU ASP SER ARG GLY LEU THR GLU TYR GLU GLU MET ASP
SEQRES 27 B 521 LEU GLY PRO VAL TYR GLY PHE GLN TRP ARG HIS PHE GLY
SEQRES 28 B 521 ALA ALA TYR THR HIS HIS ASP ALA ASN TYR ASP GLY GLN
SEQRES 29 B 521 GLY VAL ASP GLN ILE LYS ALA ILE VAL GLU THR LEU LYS
SEQRES 30 B 521 THR ASN PRO ASP ASP ARG ARG MET LEU PHE THR ALA TRP
SEQRES 31 B 521 ASN PRO SER ALA LEU PRO ARG MET ALA LEU PRO PRO CYS
SEQRES 32 B 521 HIS LEU LEU ALA GLN PHE TYR VAL SER ASN GLY GLU LEU
SEQRES 33 B 521 SER CYS MET LEU TYR GLN ARG SER CYS ASP MET GLY LEU
SEQRES 34 B 521 GLY VAL PRO PHE ASN ILE ALA SER TYR ALA LEU LEU THR
SEQRES 35 B 521 ILE LEU ILE ALA LYS ALA THR GLY LEU ARG PRO GLY GLU
SEQRES 36 B 521 LEU VAL HIS THR LEU GLY ASP ALA HIS VAL TYR SER ASN
SEQRES 37 B 521 HIS VAL GLU PRO CYS ASN GLU GLN LEU LYS ARG VAL PRO
SEQRES 38 B 521 ARG ALA PHE PRO TYR LEU VAL PHE ARG ARG GLU ARG GLU
SEQRES 39 B 521 PHE LEU GLU ASP TYR GLU GLU GLY ASP MET GLU VAL ILE
SEQRES 40 B 521 ASP TYR ALA PRO TYR PRO PRO ILE SER MET LYS MET ALA
SEQRES 41 B 521 VAL
SEQRES 1 C 521 MET SER LEU PHE LYS ILE ARG MET PRO GLU THR VAL ALA
SEQRES 2 C 521 GLU GLY THR ARG LEU ALA LEU ARG ALA PHE SER LEU VAL
SEQRES 3 C 521 VAL ALA VAL ASP GLU HIS GLY GLY ILE GLY ASP GLY ARG
SEQRES 4 C 521 SER ILE PRO TRP ASN VAL PRO GLU ASP MET LYS PHE PHE
SEQRES 5 C 521 ARG ASP LEU THR THR LYS LEU ARG GLY LYS ASN VAL LYS
SEQRES 6 C 521 PRO SER PRO ALA LYS ARG ASN ALA VAL VAL MET GLY ARG
SEQRES 7 C 521 LYS THR TRP ASP SER ILE PRO PRO LYS PHE ARG PRO LEU
SEQRES 8 C 521 PRO GLY ARG LEU ASN VAL VAL LEU SER SER THR LEU THR
SEQRES 9 C 521 THR GLN HIS LEU LEU ASP GLY LEU PRO ASP GLU GLU LYS
SEQRES 10 C 521 ARG ASN LEU HIS ALA ASP SER ILE VAL ALA VAL ASN GLY
SEQRES 11 C 521 GLY LEU GLU GLN ALA LEU ARG LEU LEU ALA SER PRO ASN
SEQRES 12 C 521 TYR THR PRO SER ILE GLU THR VAL TYR CYS ILE GLY GLY
SEQRES 13 C 521 GLY SER VAL TYR ALA GLU ALA LEU ARG PRO PRO CYS VAL
SEQRES 14 C 521 HIS LEU LEU GLN ALA ILE TYR ARG THR THR ILE ARG ALA
SEQRES 15 C 521 SER GLU SER SER CYS SER VAL PHE PHE ARG VAL PRO GLU
SEQRES 16 C 521 SER GLY THR GLU ALA ALA ALA GLY ILE GLU TRP GLN ARG
SEQRES 17 C 521 GLU THR ILE SER GLU GLU LEU THR SER ALA ASN GLY ASN
SEQRES 18 C 521 GLU THR LYS TYR TYR PHE GLU LYS LEU ILE PRO ARG ASN
SEQRES 19 C 521 ARG GLU GLU GLU GLN TYR LEU SER LEU VAL ASP ARG ILE
SEQRES 20 C 521 ILE ARG GLU GLY ASN VAL LYS HIS ASP ARG THR GLY VAL
SEQRES 21 C 521 GLY THR LEU SER ILE PHE GLY ALA GLN MET ARG PHE SER
SEQRES 22 C 521 LEU ARG ASN ASN ARG LEU PRO LEU LEU THR THR LYS ARG
SEQRES 23 C 521 VAL PHE TRP ARG GLY VAL CYS GLU GLU LEU LEU TRP PHE
SEQRES 24 C 521 LEU ARG GLY GLU THR TYR ALA LYS LYS LEU SER ASP LYS
SEQRES 25 C 521 GLY VAL HIS ILE TRP ASP ASP ASN GLY SER ARG ALA PHE
SEQRES 26 C 521 LEU ASP SER ARG GLY LEU THR GLU TYR GLU GLU MET ASP
SEQRES 27 C 521 LEU GLY PRO VAL TYR GLY PHE GLN TRP ARG HIS PHE GLY
SEQRES 28 C 521 ALA ALA TYR THR HIS HIS ASP ALA ASN TYR ASP GLY GLN
SEQRES 29 C 521 GLY VAL ASP GLN ILE LYS ALA ILE VAL GLU THR LEU LYS
SEQRES 30 C 521 THR ASN PRO ASP ASP ARG ARG MET LEU PHE THR ALA TRP
SEQRES 31 C 521 ASN PRO SER ALA LEU PRO ARG MET ALA LEU PRO PRO CYS
SEQRES 32 C 521 HIS LEU LEU ALA GLN PHE TYR VAL SER ASN GLY GLU LEU
SEQRES 33 C 521 SER CYS MET LEU TYR GLN ARG SER CYS ASP MET GLY LEU
SEQRES 34 C 521 GLY VAL PRO PHE ASN ILE ALA SER TYR ALA LEU LEU THR
SEQRES 35 C 521 ILE LEU ILE ALA LYS ALA THR GLY LEU ARG PRO GLY GLU
SEQRES 36 C 521 LEU VAL HIS THR LEU GLY ASP ALA HIS VAL TYR SER ASN
SEQRES 37 C 521 HIS VAL GLU PRO CYS ASN GLU GLN LEU LYS ARG VAL PRO
SEQRES 38 C 521 ARG ALA PHE PRO TYR LEU VAL PHE ARG ARG GLU ARG GLU
SEQRES 39 C 521 PHE LEU GLU ASP TYR GLU GLU GLY ASP MET GLU VAL ILE
SEQRES 40 C 521 ASP TYR ALA PRO TYR PRO PRO ILE SER MET LYS MET ALA
SEQRES 41 C 521 VAL
SEQRES 1 D 521 MET SER LEU PHE LYS ILE ARG MET PRO GLU THR VAL ALA
SEQRES 2 D 521 GLU GLY THR ARG LEU ALA LEU ARG ALA PHE SER LEU VAL
SEQRES 3 D 521 VAL ALA VAL ASP GLU HIS GLY GLY ILE GLY ASP GLY ARG
SEQRES 4 D 521 SER ILE PRO TRP ASN VAL PRO GLU ASP MET LYS PHE PHE
SEQRES 5 D 521 ARG ASP LEU THR THR LYS LEU ARG GLY LYS ASN VAL LYS
SEQRES 6 D 521 PRO SER PRO ALA LYS ARG ASN ALA VAL VAL MET GLY ARG
SEQRES 7 D 521 LYS THR TRP ASP SER ILE PRO PRO LYS PHE ARG PRO LEU
SEQRES 8 D 521 PRO GLY ARG LEU ASN VAL VAL LEU SER SER THR LEU THR
SEQRES 9 D 521 THR GLN HIS LEU LEU ASP GLY LEU PRO ASP GLU GLU LYS
SEQRES 10 D 521 ARG ASN LEU HIS ALA ASP SER ILE VAL ALA VAL ASN GLY
SEQRES 11 D 521 GLY LEU GLU GLN ALA LEU ARG LEU LEU ALA SER PRO ASN
SEQRES 12 D 521 TYR THR PRO SER ILE GLU THR VAL TYR CYS ILE GLY GLY
SEQRES 13 D 521 GLY SER VAL TYR ALA GLU ALA LEU ARG PRO PRO CYS VAL
SEQRES 14 D 521 HIS LEU LEU GLN ALA ILE TYR ARG THR THR ILE ARG ALA
SEQRES 15 D 521 SER GLU SER SER CYS SER VAL PHE PHE ARG VAL PRO GLU
SEQRES 16 D 521 SER GLY THR GLU ALA ALA ALA GLY ILE GLU TRP GLN ARG
SEQRES 17 D 521 GLU THR ILE SER GLU GLU LEU THR SER ALA ASN GLY ASN
SEQRES 18 D 521 GLU THR LYS TYR TYR PHE GLU LYS LEU ILE PRO ARG ASN
SEQRES 19 D 521 ARG GLU GLU GLU GLN TYR LEU SER LEU VAL ASP ARG ILE
SEQRES 20 D 521 ILE ARG GLU GLY ASN VAL LYS HIS ASP ARG THR GLY VAL
SEQRES 21 D 521 GLY THR LEU SER ILE PHE GLY ALA GLN MET ARG PHE SER
SEQRES 22 D 521 LEU ARG ASN ASN ARG LEU PRO LEU LEU THR THR LYS ARG
SEQRES 23 D 521 VAL PHE TRP ARG GLY VAL CYS GLU GLU LEU LEU TRP PHE
SEQRES 24 D 521 LEU ARG GLY GLU THR TYR ALA LYS LYS LEU SER ASP LYS
SEQRES 25 D 521 GLY VAL HIS ILE TRP ASP ASP ASN GLY SER ARG ALA PHE
SEQRES 26 D 521 LEU ASP SER ARG GLY LEU THR GLU TYR GLU GLU MET ASP
SEQRES 27 D 521 LEU GLY PRO VAL TYR GLY PHE GLN TRP ARG HIS PHE GLY
SEQRES 28 D 521 ALA ALA TYR THR HIS HIS ASP ALA ASN TYR ASP GLY GLN
SEQRES 29 D 521 GLY VAL ASP GLN ILE LYS ALA ILE VAL GLU THR LEU LYS
SEQRES 30 D 521 THR ASN PRO ASP ASP ARG ARG MET LEU PHE THR ALA TRP
SEQRES 31 D 521 ASN PRO SER ALA LEU PRO ARG MET ALA LEU PRO PRO CYS
SEQRES 32 D 521 HIS LEU LEU ALA GLN PHE TYR VAL SER ASN GLY GLU LEU
SEQRES 33 D 521 SER CYS MET LEU TYR GLN ARG SER CYS ASP MET GLY LEU
SEQRES 34 D 521 GLY VAL PRO PHE ASN ILE ALA SER TYR ALA LEU LEU THR
SEQRES 35 D 521 ILE LEU ILE ALA LYS ALA THR GLY LEU ARG PRO GLY GLU
SEQRES 36 D 521 LEU VAL HIS THR LEU GLY ASP ALA HIS VAL TYR SER ASN
SEQRES 37 D 521 HIS VAL GLU PRO CYS ASN GLU GLN LEU LYS ARG VAL PRO
SEQRES 38 D 521 ARG ALA PHE PRO TYR LEU VAL PHE ARG ARG GLU ARG GLU
SEQRES 39 D 521 PHE LEU GLU ASP TYR GLU GLU GLY ASP MET GLU VAL ILE
SEQRES 40 D 521 ASP TYR ALA PRO TYR PRO PRO ILE SER MET LYS MET ALA
SEQRES 41 D 521 VAL
HET 1CY A 601 17
HET PO4 A 701 5
HET PO4 A 705 5
HET ACT A 801 4
HET ACT A 802 4
HET ACT A 803 4
HET 1CY B 602 17
HET PO4 B 702 5
HET PO4 B 706 5
HET ACT B 804 4
HET ACT B 805 4
HET ACT B 806 4
HET 1CY C 603 17
HET PO4 C 703 5
HET PO4 C 707 5
HET ACT C 807 4
HET 1CY D 604 17
HET PO4 D 704 5
HET PO4 D 708 5
HET ACT D 808 4
HETNAM 1CY 1-(4-CHLOROPHENYL)-6,6-DIMETHYL-1,6-DIHYDRO-1,3,5-
HETNAM 2 1CY TRIAZINE-2,4-DIAMINE
HETNAM PO4 PHOSPHATE ION
HETNAM ACT ACETATE ION
HETSYN 1CY CYCLOGUANIL
FORMUL 5 1CY 4(C11 H14 CL N5)
FORMUL 6 PO4 8(O4 P 3-)
FORMUL 8 ACT 8(C2 H3 O2 1-)
FORMUL 25 HOH *653(H2 O)
HELIX 1 1 MET A 1 LYS A 5 5 5
HELIX 2 2 ALA A 13 ARG A 17 5 5
HELIX 3 3 VAL A 45 LYS A 58 1 14
HELIX 4 4 ARG A 78 SER A 83 1 6
HELIX 5 5 PRO A 85 ARG A 89 5 5
HELIX 6 6 THR A 104 GLY A 111 1 8
HELIX 7 7 ASP A 114 ALA A 122 1 9
HELIX 8 8 GLY A 131 ALA A 140 1 10
HELIX 9 9 GLY A 156 LEU A 164 1 9
HELIX 10 10 PRO A 167 HIS A 170 5 4
HELIX 11 11 THR A 198 ALA A 202 5 5
HELIX 12 12 ASN A 234 GLY A 251 1 18
HELIX 13 13 ARG A 275 ARG A 278 5 4
HELIX 14 14 PHE A 288 ARG A 301 1 14
HELIX 15 15 ALA A 306 ASP A 311 1 6
HELIX 16 16 SER A 322 ARG A 329 1 8
HELIX 17 17 VAL A 342 PHE A 350 1 9
HELIX 18 18 ASP A 367 ASN A 379 1 13
HELIX 19 19 ALA A 394 MET A 398 5 5
HELIX 20 20 LEU A 429 THR A 449 1 21
HELIX 21 21 HIS A 469 LEU A 477 1 9
HELIX 22 22 PHE A 495 TYR A 499 5 5
HELIX 23 23 GLU A 500 GLY A 502 5 3
HELIX 24 24 ALA B 13 ARG B 17 5 5
HELIX 25 25 VAL B 45 LYS B 58 1 14
HELIX 26 26 ARG B 78 SER B 83 1 6
HELIX 27 27 PRO B 85 ARG B 89 5 5
HELIX 28 28 THR B 104 GLY B 111 1 8
HELIX 29 29 GLY B 131 LEU B 139 1 9
HELIX 30 30 GLY B 156 LEU B 164 1 9
HELIX 31 31 PRO B 167 HIS B 170 5 4
HELIX 32 32 THR B 198 ALA B 202 5 5
HELIX 33 33 ASN B 234 GLY B 251 1 18
HELIX 34 34 ARG B 275 ARG B 278 5 4
HELIX 35 35 PHE B 288 ARG B 301 1 14
HELIX 36 36 ALA B 306 ASP B 311 1 6
HELIX 37 37 ASP B 318 GLY B 321 5 4
HELIX 38 38 SER B 322 ARG B 329 1 8
HELIX 39 39 TYR B 343 PHE B 350 1 8
HELIX 40 40 ASP B 367 ASN B 379 1 13
HELIX 41 41 ALA B 394 MET B 398 5 5
HELIX 42 42 LEU B 429 THR B 449 1 21
HELIX 43 43 HIS B 469 LEU B 477 1 9
HELIX 44 44 PHE B 495 TYR B 499 5 5
HELIX 45 45 GLU B 500 GLY B 502 5 3
HELIX 46 46 ALA C 13 ARG C 17 5 5
HELIX 47 47 VAL C 45 LYS C 58 1 14
HELIX 48 48 ARG C 78 SER C 83 1 6
HELIX 49 49 PRO C 85 ARG C 89 5 5
HELIX 50 50 THR C 104 GLY C 111 1 8
HELIX 51 51 ASP C 114 HIS C 121 1 8
HELIX 52 52 GLY C 131 ALA C 140 1 10
HELIX 53 53 GLY C 156 LEU C 164 1 9
HELIX 54 54 PRO C 167 HIS C 170 5 4
HELIX 55 55 ASN C 234 GLY C 251 1 18
HELIX 56 56 ARG C 275 ARG C 278 5 4
HELIX 57 57 PHE C 288 ARG C 301 1 14
HELIX 58 58 ALA C 306 ASP C 311 1 6
HELIX 59 59 ASP C 318 GLY C 321 5 4
HELIX 60 60 SER C 322 ARG C 329 1 8
HELIX 61 61 VAL C 342 PHE C 350 1 9
HELIX 62 62 ASP C 367 ASN C 379 1 13
HELIX 63 63 ALA C 394 MET C 398 5 5
HELIX 64 64 LEU C 429 THR C 449 1 21
HELIX 65 65 HIS C 469 LEU C 477 1 9
HELIX 66 66 PHE C 495 TYR C 499 5 5
HELIX 67 67 GLU C 500 GLY C 502 5 3
HELIX 68 68 ALA D 13 ARG D 17 5 5
HELIX 69 69 VAL D 45 LYS D 58 1 14
HELIX 70 70 ARG D 78 SER D 83 1 6
HELIX 71 71 PRO D 85 ARG D 89 5 5
HELIX 72 72 THR D 104 GLY D 111 1 8
HELIX 73 73 GLU D 116 HIS D 121 1 6
HELIX 74 74 GLY D 131 SER D 141 1 11
HELIX 75 75 GLY D 156 LEU D 164 1 9
HELIX 76 76 PRO D 167 HIS D 170 5 4
HELIX 77 77 THR D 198 ALA D 202 5 5
HELIX 78 78 ASN D 234 GLY D 251 1 18
HELIX 79 79 ARG D 275 ARG D 278 5 4
HELIX 80 80 PHE D 288 ARG D 301 1 14
HELIX 81 81 ALA D 306 ASP D 311 1 6
HELIX 82 82 TRP D 317 SER D 322 1 6
HELIX 83 83 SER D 322 SER D 328 1 7
HELIX 84 84 VAL D 342 PHE D 350 1 9
HELIX 85 85 ASP D 367 ASN D 379 1 13
HELIX 86 86 ALA D 394 MET D 398 5 5
HELIX 87 87 LEU D 429 THR D 449 1 21
HELIX 88 88 HIS D 469 LEU D 477 1 9
HELIX 89 89 PHE D 495 TYR D 499 5 5
HELIX 90 90 GLU D 500 GLY D 502 5 3
SHEET 1 A 8 ILE A 125 VAL A 128 0
SHEET 2 A 8 ARG A 94 LEU A 99 1 N VAL A 98 O VAL A 126
SHEET 3 A 8 ARG A 71 GLY A 77 1 N VAL A 74 O VAL A 97
SHEET 4 A 8 ILE A 148 CYS A 153 1 O TYR A 152 N VAL A 75
SHEET 5 A 8 PHE A 23 ASP A 30 1 N SER A 24 O CYS A 153
SHEET 6 A 8 LEU A 172 ILE A 180 1 O TYR A 176 N LEU A 25
SHEET 7 A 8 LYS A 224 PRO A 232 -1 O LEU A 230 N ILE A 175
SHEET 8 A 8 TRP A 206 ILE A 211 -1 N GLU A 209 O LYS A 229
SHEET 1 B 8 ILE A 125 VAL A 128 0
SHEET 2 B 8 ARG A 94 LEU A 99 1 N VAL A 98 O VAL A 126
SHEET 3 B 8 ARG A 71 GLY A 77 1 N VAL A 74 O VAL A 97
SHEET 4 B 8 ILE A 148 CYS A 153 1 O TYR A 152 N VAL A 75
SHEET 5 B 8 PHE A 23 ASP A 30 1 N SER A 24 O CYS A 153
SHEET 6 B 8 LEU A 172 ILE A 180 1 O TYR A 176 N LEU A 25
SHEET 7 B 8 LYS A 224 PRO A 232 -1 O LEU A 230 N ILE A 175
SHEET 8 B 8 LEU A 215 THR A 216 -1 N LEU A 215 O TYR A 225
SHEET 1 C 2 GLY A 34 GLY A 36 0
SHEET 2 C 2 VAL A 189 PHE A 190 -1 O VAL A 189 N ILE A 35
SHEET 1 D 6 ASN A 252 HIS A 255 0
SHEET 2 D 6 GLY A 261 SER A 273 -1 O SER A 264 N ASN A 252
SHEET 3 D 6 ARG A 452 TYR A 466 -1 O HIS A 458 N MET A 270
SHEET 4 D 6 GLU A 415 ASP A 426 1 N CYS A 418 O VAL A 457
SHEET 5 D 6 HIS A 404 SER A 412 -1 N TYR A 410 O SER A 417
SHEET 6 D 6 LEU A 386 THR A 388 -1 N PHE A 387 O ALA A 407
SHEET 1 E 2 TYR A 486 PHE A 489 0
SHEET 2 E 2 MET A 504 ILE A 507 -1 O GLU A 505 N VAL A 488
SHEET 1 F 8 ILE B 125 VAL B 128 0
SHEET 2 F 8 ARG B 94 LEU B 99 1 N VAL B 98 O VAL B 128
SHEET 3 F 8 ARG B 71 GLY B 77 1 N MET B 76 O LEU B 99
SHEET 4 F 8 ILE B 148 CYS B 153 1 O THR B 150 N ALA B 73
SHEET 5 F 8 PHE B 23 ASP B 30 1 N SER B 24 O CYS B 153
SHEET 6 F 8 LEU B 172 ILE B 180 1 O THR B 178 N VAL B 29
SHEET 7 F 8 LYS B 224 PRO B 232 -1 O LEU B 230 N ILE B 175
SHEET 8 F 8 TRP B 206 ILE B 211 -1 N GLU B 209 O LYS B 229
SHEET 1 G 8 ILE B 125 VAL B 128 0
SHEET 2 G 8 ARG B 94 LEU B 99 1 N VAL B 98 O VAL B 128
SHEET 3 G 8 ARG B 71 GLY B 77 1 N MET B 76 O LEU B 99
SHEET 4 G 8 ILE B 148 CYS B 153 1 O THR B 150 N ALA B 73
SHEET 5 G 8 PHE B 23 ASP B 30 1 N SER B 24 O CYS B 153
SHEET 6 G 8 LEU B 172 ILE B 180 1 O THR B 178 N VAL B 29
SHEET 7 G 8 LYS B 224 PRO B 232 -1 O LEU B 230 N ILE B 175
SHEET 8 G 8 LEU B 215 THR B 216 -1 N LEU B 215 O TYR B 225
SHEET 1 H 2 GLY B 34 GLY B 36 0
SHEET 2 H 2 VAL B 189 PHE B 190 -1 O VAL B 189 N ILE B 35
SHEET 1 I 6 ASN B 252 HIS B 255 0
SHEET 2 I 6 GLY B 261 SER B 273 -1 O SER B 264 N ASN B 252
SHEET 3 I 6 ARG B 452 TYR B 466 -1 O HIS B 458 N MET B 270
SHEET 4 I 6 GLU B 415 ASP B 426 1 N CYS B 418 O VAL B 457
SHEET 5 I 6 HIS B 404 SER B 412 -1 N TYR B 410 O SER B 417
SHEET 6 I 6 LEU B 386 THR B 388 -1 N PHE B 387 O ALA B 407
SHEET 1 J 2 TYR B 486 PHE B 489 0
SHEET 2 J 2 MET B 504 ILE B 507 -1 O GLU B 505 N VAL B 488
SHEET 1 K 8 ILE C 125 VAL C 128 0
SHEET 2 K 8 ARG C 94 LEU C 99 1 N VAL C 98 O VAL C 128
SHEET 3 K 8 ARG C 71 GLY C 77 1 N VAL C 74 O VAL C 97
SHEET 4 K 8 ILE C 148 CYS C 153 1 O TYR C 152 N VAL C 75
SHEET 5 K 8 PHE C 23 ASP C 30 1 N SER C 24 O CYS C 153
SHEET 6 K 8 LEU C 172 ILE C 180 1 O TYR C 176 N LEU C 25
SHEET 7 K 8 LYS C 224 PRO C 232 -1 O LEU C 230 N ILE C 175
SHEET 8 K 8 TRP C 206 ILE C 211 -1 N GLU C 209 O LYS C 229
SHEET 1 L 8 ILE C 125 VAL C 128 0
SHEET 2 L 8 ARG C 94 LEU C 99 1 N VAL C 98 O VAL C 128
SHEET 3 L 8 ARG C 71 GLY C 77 1 N VAL C 74 O VAL C 97
SHEET 4 L 8 ILE C 148 CYS C 153 1 O TYR C 152 N VAL C 75
SHEET 5 L 8 PHE C 23 ASP C 30 1 N SER C 24 O CYS C 153
SHEET 6 L 8 LEU C 172 ILE C 180 1 O TYR C 176 N LEU C 25
SHEET 7 L 8 LYS C 224 PRO C 232 -1 O LEU C 230 N ILE C 175
SHEET 8 L 8 LEU C 215 THR C 216 -1 N LEU C 215 O TYR C 225
SHEET 1 M 6 ASN C 252 HIS C 255 0
SHEET 2 M 6 GLY C 261 SER C 273 -1 O SER C 264 N ASN C 252
SHEET 3 M 6 ARG C 452 TYR C 466 -1 O HIS C 458 N MET C 270
SHEET 4 M 6 GLU C 415 ASP C 426 1 N LEU C 416 O ARG C 452
SHEET 5 M 6 HIS C 404 SER C 412 -1 N TYR C 410 O SER C 417
SHEET 6 M 6 LEU C 386 THR C 388 -1 N PHE C 387 O ALA C 407
SHEET 1 N 2 TYR C 486 PHE C 489 0
SHEET 2 N 2 MET C 504 ILE C 507 -1 O GLU C 505 N VAL C 488
SHEET 1 O 8 ILE D 125 VAL D 128 0
SHEET 2 O 8 ARG D 94 LEU D 99 1 N VAL D 98 O VAL D 128
SHEET 3 O 8 ARG D 71 GLY D 77 1 N VAL D 74 O VAL D 97
SHEET 4 O 8 ILE D 148 GLY D 155 1 O TYR D 152 N VAL D 75
SHEET 5 O 8 PHE D 23 ASP D 30 1 N SER D 24 O CYS D 153
SHEET 6 O 8 LEU D 172 ILE D 180 1 O TYR D 176 N LEU D 25
SHEET 7 O 8 LYS D 224 PRO D 232 -1 O LEU D 230 N ILE D 175
SHEET 8 O 8 TRP D 206 ILE D 211 -1 N GLU D 209 O LYS D 229
SHEET 1 P 8 ILE D 125 VAL D 128 0
SHEET 2 P 8 ARG D 94 LEU D 99 1 N VAL D 98 O VAL D 128
SHEET 3 P 8 ARG D 71 GLY D 77 1 N VAL D 74 O VAL D 97
SHEET 4 P 8 ILE D 148 GLY D 155 1 O TYR D 152 N VAL D 75
SHEET 5 P 8 PHE D 23 ASP D 30 1 N SER D 24 O CYS D 153
SHEET 6 P 8 LEU D 172 ILE D 180 1 O TYR D 176 N LEU D 25
SHEET 7 P 8 LYS D 224 PRO D 232 -1 O LEU D 230 N ILE D 175
SHEET 8 P 8 LEU D 215 THR D 216 -1 N LEU D 215 O TYR D 225
SHEET 1 Q 6 ASN D 252 HIS D 255 0
SHEET 2 Q 6 GLY D 261 SER D 273 -1 O SER D 264 N ASN D 252
SHEET 3 Q 6 ARG D 452 TYR D 466 -1 O LEU D 456 N PHE D 272
SHEET 4 Q 6 GLU D 415 ASP D 426 1 N CYS D 418 O VAL D 457
SHEET 5 Q 6 HIS D 404 SER D 412 -1 N GLN D 408 O MET D 419
SHEET 6 Q 6 LEU D 386 THR D 388 -1 N PHE D 387 O ALA D 407
SHEET 1 R 2 TYR D 486 PHE D 489 0
SHEET 2 R 2 MET D 504 ILE D 507 -1 O GLU D 505 N VAL D 488
CISPEP 1 ARG A 89 PRO A 90 0 -0.16
CISPEP 2 THR A 145 PRO A 146 0 0.34
CISPEP 3 PRO A 166 PRO A 167 0 0.20
CISPEP 4 ARG B 89 PRO B 90 0 -0.28
CISPEP 5 THR B 145 PRO B 146 0 -0.21
CISPEP 6 PRO B 166 PRO B 167 0 0.35
CISPEP 7 ARG C 89 PRO C 90 0 -0.10
CISPEP 8 THR C 145 PRO C 146 0 0.57
CISPEP 9 PRO C 166 PRO C 167 0 0.07
CISPEP 10 ARG D 89 PRO D 90 0 -0.31
CISPEP 11 THR D 145 PRO D 146 0 0.31
CISPEP 12 PRO D 166 PRO D 167 0 0.22
SITE 1 AC1 10 VAL A 26 VAL A 27 ALA A 28 ASP A 48
SITE 2 AC1 10 MET A 49 PHE A 52 THR A 80 ILE A 84
SITE 3 AC1 10 ILE A 154 TYR A 160
SITE 1 AC2 5 ARG A 423 SER A 424 HOH A1626 ARG B 383
SITE 2 AC2 5 ARG B 384
SITE 1 AC3 6 ARG A 78 LEU A 99 SER A 100 SER A 101
SITE 2 AC3 6 THR A 102 HOH A1091
SITE 1 AC4 8 GLY A 77 ARG A 78 LYS A 79 THR A 80
SITE 2 AC4 8 GLY A 156 SER A 158 ACT A 802 HOH A1091
SITE 1 AC5 6 ARG A 39 LYS A 79 GLY A 156 GLY A 157
SITE 2 AC5 6 SER A 158 ACT A 801
SITE 1 AC6 3 VAL A 193 TRP A 206 ARG A 208
SITE 1 AC7 12 VAL B 26 VAL B 27 ALA B 28 ARG B 39
SITE 2 AC7 12 ASP B 48 MET B 49 PHE B 52 THR B 80
SITE 3 AC7 12 ILE B 84 ILE B 154 TYR B 160 THR B 178
SITE 1 AC8 4 ARG A 383 ARG A 384 ARG B 423 SER B 424
SITE 1 AC9 5 ARG B 78 SER B 100 SER B 101 THR B 102
SITE 2 AC9 5 HOH B1545
SITE 1 BC1 6 GLY B 77 ARG B 78 LYS B 79 THR B 80
SITE 2 BC1 6 GLY B 156 SER B 158
SITE 1 BC2 7 SER B 24 GLN B 173 ALA B 174 TYR B 176
SITE 2 BC2 7 LYS B 229 HOH B1248 HOH B1580
SITE 1 BC3 7 ILE B 248 ASN B 474 HOH B1216 HOH B1578
SITE 2 BC3 7 ARG D 208 THR D 210 ILE D 211
SITE 1 BC4 10 VAL C 26 VAL C 27 ALA C 28 ASP C 48
SITE 2 BC4 10 PHE C 52 THR C 80 ILE C 84 ILE C 154
SITE 3 BC4 10 TYR C 160 THR C 178
SITE 1 BC5 4 ARG C 423 SER C 424 ARG D 383 ARG D 384
SITE 1 BC6 7 ARG C 78 LEU C 99 SER C 100 SER C 101
SITE 2 BC6 7 THR C 102 HOH C1005 HOH C1475
SITE 1 BC7 5 LYS C 79 THR C 80 GLY C 156 SER C 158
SITE 2 BC7 5 HOH C1325
SITE 1 BC8 10 VAL D 26 VAL D 27 ALA D 28 ASP D 48
SITE 2 BC8 10 MET D 49 PHE D 52 THR D 80 ILE D 84
SITE 3 BC8 10 ILE D 154 THR D 178
SITE 1 BC9 5 ARG C 383 ARG C 384 ARG D 423 SER D 424
SITE 2 BC9 5 HOH D1566
SITE 1 CC1 5 ARG D 78 SER D 100 SER D 101 THR D 102
SITE 2 CC1 5 HOH D1008
SITE 1 CC2 8 GLY D 77 LYS D 79 THR D 80 GLY D 156
SITE 2 CC2 8 SER D 158 VAL D 159 HOH D1338 HOH D1497
CRYST1 81.436 165.792 84.767 90.00 113.40 90.00 P 1 21 1 8
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 0.012280 0.000000 0.005313 0.00000
SCALE2 0.000000 0.006032 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012854 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
