HEADER TRANSFERASE 04-NOV-98 1TC2
TITLE TERNARY SUBSTRATE COMPLEX OF THE HYPOXANTHINE
TITLE 2 PHOSPHORIBOSYLTRANSFERASE FROM TRYPANOSOMA CRUZI
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN (HYPOXANTHINE PHOSPHORIBOSYLTRANSFERASE);
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 2.4.2.8;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: TRYPANOSOMA CRUZI;
SOURCE 3 ORGANISM_TAXID: 5693;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS TRANSFERASE, GLYCOSYLTRANSFERASE, PHOSPHORIBOSYLTRANSFERASE,
KEYWDS 2 NUCLEOTIDE METABOLISM, PURINE SALVAGE, TERNARY COMPLEX, NEAR
KEYWDS 3 TRANSITION STATE
EXPDTA X-RAY DIFFRACTION
AUTHOR P.J.FOCIA,S.P.CRAIG III,A.E.EAKIN
REVDAT 7 23-AUG-23 1TC2 1 HETSYN
REVDAT 6 29-JUL-20 1TC2 1 COMPND REMARK SEQADV HETNAM
REVDAT 6 2 1 LINK SITE
REVDAT 5 31-JAN-18 1TC2 1 JRNL
REVDAT 4 24-JAN-18 1TC2 1 JRNL
REVDAT 3 24-FEB-09 1TC2 1 VERSN
REVDAT 2 01-APR-03 1TC2 1 JRNL
REVDAT 1 08-MAR-00 1TC2 0
JRNL AUTH P.J.FOCIA,S.P.CRAIG III,A.E.EAKIN
JRNL TITL APPROACHING THE TRANSITION STATE IN THE CRYSTAL STRUCTURE OF
JRNL TITL 2 A PHOSPHORIBOSYLTRANSFERASE.
JRNL REF BIOCHEMISTRY V. 37 17120 1998
JRNL REFN ISSN 0006-2960
JRNL PMID 9860824
JRNL DOI 10.1021/BI9821465
REMARK 2
REMARK 2 RESOLUTION. 1.81 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.851
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.81
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 6.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 1.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 29719
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) : 0.183
REMARK 3 FREE R VALUE : 0.232
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.900
REMARK 3 FREE R VALUE TEST SET COUNT : 1756
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 15
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.81
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.85
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 1403
REMARK 3 BIN R VALUE (WORKING SET) : 0.2590
REMARK 3 BIN FREE R VALUE : 0.3020
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.16
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 82
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3039
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 68
REMARK 3 SOLVENT ATOMS : 193
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 COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 1.560
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 24.48
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.360
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : 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 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 : PARHCSDX.PRO
REMARK 3 PARAMETER FILE 2 : PARAM11X.DNA (MODIFIED FOR 7HP)
REMARK 3 PARAMETER FILE 3 : PRPP.PAR
REMARK 3 PARAMETER FILE 4 : PARAM19.ION (MODIFIED)
REMARK 3 PARAMETER FILE 5 : PARAM11.WAT
REMARK 3 PARAMETER FILE 6 : NULL
REMARK 3 TOPOLOGY FILE 1 : TOPHCSDX.PRO
REMARK 3 TOPOLOGY FILE 2 : TOPH11.DNA (MODIFIED FOR 7HP)
REMARK 3 TOPOLOGY FILE 3 : PRPP.TOP
REMARK 3 TOPOLOGY FILE 4 : TOPH19.ION (MODIFIED)
REMARK 3 TOPOLOGY FILE 5 : TOPH11.WAT
REMARK 3 TOPOLOGY FILE 6 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 PATCH STATEMENTS WERE USED FOR CIS PEPTIDES AND METAL-OXYGEN BONDS
REMARK 3
REMARK 3 SER 88 IS POORLY ORDERED IN SUBUNIT A
REMARK 3
REMARK 3 THE ENERGIES FOR METAL-OXYGEN BOND LENGTHS AND ANGLES
REMARK 3 WERE SET ARTIFICIALLY LOW DURING REFINEMENT IN ORDER TO
REMARK 3 ALLOW THESE ATOMS MORE FREEDOM TO ADJUST
REMARK 4
REMARK 4 1TC2 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-JUL-99.
REMARK 100 THE DEPOSITION ID IS D_1000007329.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 04-JUL-97
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 4.6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRL
REMARK 200 BEAMLINE : BL7-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.08
REMARK 200 MONOCHROMATOR : NULL
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 : 33026
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.810
REMARK 200 RESOLUTION RANGE LOW (A) : 20.600
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 88.8
REMARK 200 DATA REDUNDANCY : 3.600
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.05100
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 20.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.81
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.85
REMARK 200 COMPLETENESS FOR SHELL (%) : 80.1
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.32000
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.800
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: PDB ENTRY 1TC1
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 39.35
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.03
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 4.6
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 50.88000
REMARK 290 SMTRY3 2 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: 5710 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 15650 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -66.0 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 MET A 1
REMARK 465 PRO A 2
REMARK 465 ARG A 3
REMARK 465 GLU A 4
REMARK 465 ALA A 191
REMARK 465 GLU A 192
REMARK 465 ARG A 193
REMARK 465 GLU A 194
REMARK 465 ALA A 195
REMARK 465 ALA A 196
REMARK 465 ARG A 197
REMARK 465 GLN A 198
REMARK 465 LYS A 199
REMARK 465 LYS A 200
REMARK 465 GLN A 201
REMARK 465 ARG A 202
REMARK 465 ALA A 203
REMARK 465 ILE A 204
REMARK 465 GLY A 205
REMARK 465 SER A 206
REMARK 465 ALA A 207
REMARK 465 ASP A 208
REMARK 465 THR A 209
REMARK 465 ASP A 210
REMARK 465 ARG A 211
REMARK 465 ASP A 212
REMARK 465 ALA A 213
REMARK 465 LYS A 214
REMARK 465 ARG A 215
REMARK 465 GLU A 216
REMARK 465 PHE A 217
REMARK 465 HIS A 218
REMARK 465 SER A 219
REMARK 465 LYS A 220
REMARK 465 TYR A 221
REMARK 465 MET B 501
REMARK 465 PRO B 502
REMARK 465 LYS B 699
REMARK 465 LYS B 700
REMARK 465 GLN B 701
REMARK 465 ARG B 702
REMARK 465 ALA B 703
REMARK 465 ILE B 704
REMARK 465 GLY B 705
REMARK 465 SER B 706
REMARK 465 ALA B 707
REMARK 465 ASP B 708
REMARK 465 THR B 709
REMARK 465 ASP B 710
REMARK 465 ARG B 711
REMARK 465 ASP B 712
REMARK 465 ALA B 713
REMARK 465 LYS B 714
REMARK 465 ARG B 715
REMARK 465 GLU B 716
REMARK 465 PHE B 717
REMARK 465 HIS B 718
REMARK 465 SER B 719
REMARK 465 LYS B 720
REMARK 465 TYR B 721
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 GLU A 6 CG CD OE1 OE2
REMARK 470 LYS A 34 CG CD CE NZ
REMARK 470 ARG A 39 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 84 CG CD OE1 OE2
REMARK 470 ARG A 99 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 131 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 145 CG CD OE1 OE2
REMARK 470 GLU A 188 CG CD OE1 OE2
REMARK 470 TYR A 190 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 GLU B 504 CG CD OE1 OE2
REMARK 470 LYS B 534 CG CD CE NZ
REMARK 470 GLN B 591 CG CD OE1 NE2
REMARK 470 GLU B 645 CG CD OE1 OE2
REMARK 470 GLN B 698 CG CD OE1 NE2
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 LYS A 34 -5.87 -50.58
REMARK 500 TYR A 41 -56.87 66.81
REMARK 500 ASP A 115 -86.05 -125.95
REMARK 500 LYS B 510 162.57 179.87
REMARK 500 TYR B 541 -57.97 71.24
REMARK 500 ASN B 543 55.27 -146.11
REMARK 500 SER B 581 -44.69 -148.06
REMARK 500 ASP B 615 -89.78 -124.82
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 TYR B 672 0.07 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 902 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 171 OD1
REMARK 620 2 PRP A 801 O1B 82.5
REMARK 620 3 PRP A 801 O2A 164.8 82.6
REMARK 620 4 HOH A1284 O 90.5 86.0 91.1
REMARK 620 5 HOH A1285 O 94.3 176.7 100.6 94.5
REMARK 620 6 HOH A1286 O 86.0 88.9 91.1 174.2 90.5
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 900 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 PRP A 801 O2
REMARK 620 2 PRP A 801 O1 67.3
REMARK 620 3 PRP A 801 O3 82.3 74.1
REMARK 620 4 PRP A 801 O3B 83.4 83.5 156.7
REMARK 620 5 HOH A1282 O 100.4 167.0 101.0 99.7
REMARK 620 6 HOH A1283 O 151.4 84.4 94.2 89.6 108.1
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B 912 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 671 OD1
REMARK 620 2 PRP B 811 O2A 171.4
REMARK 620 3 PRP B 811 O1B 83.9 87.6
REMARK 620 4 HOH B1287 O 91.5 90.7 94.5
REMARK 620 5 HOH B1288 O 82.4 106.2 166.3 85.4
REMARK 620 6 HOH B1289 O 81.8 97.4 94.6 168.1 84.0
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN B 910 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 PRP B 811 O2
REMARK 620 2 PRP B 811 O3 71.6
REMARK 620 3 PRP B 811 O3B 97.7 158.6
REMARK 620 4 PRP B 811 O1 68.5 71.7 87.2
REMARK 620 5 HOH B1290 O 97.7 102.4 97.2 166.0
REMARK 620 6 HOH B1291 O 152.7 87.4 96.1 88.8 103.8
REMARK 620 N 1 2 3 4 5
DBREF 1TC2 A 1 221 UNP Q27796 Q27796_TRYCR 1 221
DBREF 1TC2 B 501 721 UNP Q27796 Q27796_TRYCR 1 221
SEQADV 1TC2 LYS A 23 UNP Q27796 MET 23 VARIANT
SEQADV 1TC2 CYS A 66 UNP Q27796 SER 66 VARIANT
SEQADV 1TC2 LEU A 86 UNP Q27796 VAL 86 VARIANT
SEQADV 1TC2 LYS B 523 UNP Q27796 MET 23 VARIANT
SEQADV 1TC2 CYS B 566 UNP Q27796 SER 66 VARIANT
SEQADV 1TC2 LEU B 586 UNP Q27796 VAL 86 VARIANT
SEQRES 1 A 221 MET PRO ARG GLU TYR GLU PHE ALA GLU LYS ILE LEU PHE
SEQRES 2 A 221 THR GLU GLU GLU ILE ARG THR ARG ILE LYS GLU VAL ALA
SEQRES 3 A 221 LYS ARG ILE ALA ASP ASP TYR LYS GLY LYS GLY LEU ARG
SEQRES 4 A 221 PRO TYR VAL ASN PRO LEU VAL LEU ILE SER VAL LEU LYS
SEQRES 5 A 221 GLY SER PHE MET PHE THR ALA ASP LEU CYS ARG ALA LEU
SEQRES 6 A 221 CYS ASP PHE ASN VAL PRO VAL ARG MET GLU PHE ILE CYS
SEQRES 7 A 221 VAL SER SER TYR GLY GLU GLY LEU THR SER SER GLY GLN
SEQRES 8 A 221 VAL ARG MET LEU LEU ASP THR ARG HIS SER ILE GLU GLY
SEQRES 9 A 221 HIS HIS VAL LEU ILE VAL GLU ASP ILE VAL ASP THR ALA
SEQRES 10 A 221 LEU THR LEU ASN TYR LEU TYR HIS MET TYR PHE THR ARG
SEQRES 11 A 221 ARG PRO ALA SER LEU LYS THR VAL VAL LEU LEU ASP LYS
SEQRES 12 A 221 ARG GLU GLY ARG ARG VAL PRO PHE SER ALA ASP TYR VAL
SEQRES 13 A 221 VAL ALA ASN ILE PRO ASN ALA PHE VAL ILE GLY TYR GLY
SEQRES 14 A 221 LEU ASP TYR ASP ASP THR TYR ARG GLU LEU ARG ASP ILE
SEQRES 15 A 221 VAL VAL LEU ARG PRO GLU VAL TYR ALA GLU ARG GLU ALA
SEQRES 16 A 221 ALA ARG GLN LYS LYS GLN ARG ALA ILE GLY SER ALA ASP
SEQRES 17 A 221 THR ASP ARG ASP ALA LYS ARG GLU PHE HIS SER LYS TYR
SEQRES 1 B 221 MET PRO ARG GLU TYR GLU PHE ALA GLU LYS ILE LEU PHE
SEQRES 2 B 221 THR GLU GLU GLU ILE ARG THR ARG ILE LYS GLU VAL ALA
SEQRES 3 B 221 LYS ARG ILE ALA ASP ASP TYR LYS GLY LYS GLY LEU ARG
SEQRES 4 B 221 PRO TYR VAL ASN PRO LEU VAL LEU ILE SER VAL LEU LYS
SEQRES 5 B 221 GLY SER PHE MET PHE THR ALA ASP LEU CYS ARG ALA LEU
SEQRES 6 B 221 CYS ASP PHE ASN VAL PRO VAL ARG MET GLU PHE ILE CYS
SEQRES 7 B 221 VAL SER SER TYR GLY GLU GLY LEU THR SER SER GLY GLN
SEQRES 8 B 221 VAL ARG MET LEU LEU ASP THR ARG HIS SER ILE GLU GLY
SEQRES 9 B 221 HIS HIS VAL LEU ILE VAL GLU ASP ILE VAL ASP THR ALA
SEQRES 10 B 221 LEU THR LEU ASN TYR LEU TYR HIS MET TYR PHE THR ARG
SEQRES 11 B 221 ARG PRO ALA SER LEU LYS THR VAL VAL LEU LEU ASP LYS
SEQRES 12 B 221 ARG GLU GLY ARG ARG VAL PRO PHE SER ALA ASP TYR VAL
SEQRES 13 B 221 VAL ALA ASN ILE PRO ASN ALA PHE VAL ILE GLY TYR GLY
SEQRES 14 B 221 LEU ASP TYR ASP ASP THR TYR ARG GLU LEU ARG ASP ILE
SEQRES 15 B 221 VAL VAL LEU ARG PRO GLU VAL TYR ALA GLU ARG GLU ALA
SEQRES 16 B 221 ALA ARG GLN LYS LYS GLN ARG ALA ILE GLY SER ALA ASP
SEQRES 17 B 221 THR ASP ARG ASP ALA LYS ARG GLU PHE HIS SER LYS TYR
HET MG A 900 1
HET MG A 902 1
HET 7HP A 800 10
HET PRP A 801 22
HET MG B 912 1
HET MN B 910 1
HET 7HP B 810 10
HET PRP B 811 22
HETNAM MG MAGNESIUM ION
HETNAM 7HP 7-HYDROXY-PYRAZOLO[4,3-D]PYRIMIDINE
HETNAM PRP 1-O-PYROPHOSPHONO-5-O-PHOSPHONO-ALPHA-D-RIBOFURANOSE
HETNAM MN MANGANESE (II) ION
HETSYN PRP ALPHA-PHOSPHORIBOSYLPYROPHOSPHORIC ACID; 1-O-
HETSYN 2 PRP PYROPHOSPHONO-5-O-PHOSPHONO-ALPHA-D-RIBOSE; 1-O-
HETSYN 3 PRP PYROPHOSPHONO-5-O-PHOSPHONO-D-RIBOSE; 1-O-
HETSYN 4 PRP PYROPHOSPHONO-5-O-PHOSPHONO-RIBOSE
FORMUL 3 MG 3(MG 2+)
FORMUL 5 7HP 2(C5 H4 N4 O)
FORMUL 6 PRP 2(C5 H13 O14 P3)
FORMUL 8 MN MN 2+
FORMUL 11 HOH *193(H2 O)
HELIX 1 1 THR A 14 LYS A 34 1 21
HELIX 2 2 SER A 54 PHE A 68 1 15
HELIX 3 3 ALA A 117 THR A 129 1 13
HELIX 4 4 ARG A 144 ARG A 147 5 4
HELIX 5 5 THR B 514 LYS B 534 1 21
HELIX 6 6 GLY B 535 GLY B 537 5 3
HELIX 7 7 SER B 554 PHE B 568 1 15
HELIX 8 8 ALA B 617 THR B 629 1 13
HELIX 9 9 ARG B 686 GLN B 698 1 13
SHEET 1 A 3 ALA A 8 PHE A 13 0
SHEET 2 A 3 ILE A 182 LEU A 185 -1 N ILE A 182 O PHE A 13
SHEET 3 A 3 VAL A 165 ILE A 166 -1 O ILE A 166 N VAL A 183
SHEET 1 B 6 ARG A 93 LEU A 96 0
SHEET 2 B 6 VAL A 72 SER A 80 -1 O CYS A 78 N LEU A 95
SHEET 3 B 6 LEU A 45 VAL A 50 1 O LEU A 45 N ARG A 73
SHEET 4 B 6 HIS A 106 VAL A 114 1 O HIS A 106 N VAL A 46
SHEET 5 B 6 SER A 134 ASP A 142 1 O SER A 134 N VAL A 107
SHEET 6 B 6 TYR A 155 ASN A 159 1 O TYR A 155 N VAL A 139
SHEET 1 C 3 ALA B 508 PHE B 513 0
SHEET 2 C 3 ILE B 682 LEU B 685 -1 O ILE B 682 N LEU B 512
SHEET 3 C 3 VAL B 665 ILE B 666 -1 O ILE B 666 N VAL B 683
SHEET 1 D 6 ARG B 593 LEU B 596 0
SHEET 2 D 6 VAL B 572 SER B 580 -1 N CYS B 578 O LEU B 596
SHEET 3 D 6 LEU B 545 LEU B 551 1 O LEU B 545 N ARG B 573
SHEET 4 D 6 HIS B 606 VAL B 614 1 O HIS B 606 N VAL B 546
SHEET 5 D 6 SER B 634 ASP B 642 1 O SER B 634 N VAL B 607
SHEET 6 D 6 TYR B 655 ASN B 659 1 O TYR B 655 N VAL B 639
LINK OD1 ASP A 171 MG MG A 902 1555 1555 2.15
LINK O2 PRP A 801 MG MG A 900 1555 1555 2.17
LINK O1 PRP A 801 MG MG A 900 1555 1555 2.52
LINK O3 PRP A 801 MG MG A 900 1555 1555 2.29
LINK O3B PRP A 801 MG MG A 900 1555 1555 2.19
LINK O1B PRP A 801 MG MG A 902 1555 1555 2.17
LINK O2A PRP A 801 MG MG A 902 1555 1555 2.10
LINK MG MG A 900 O HOH A1282 1555 1555 1.96
LINK MG MG A 900 O HOH A1283 1555 1555 2.01
LINK MG MG A 902 O HOH A1284 1555 1555 2.12
LINK MG MG A 902 O HOH A1285 1555 1555 2.13
LINK MG MG A 902 O HOH A1286 1555 1555 2.03
LINK OD1 ASP B 671 MG MG B 912 1555 1555 2.11
LINK O2 PRP B 811 MN MN B 910 1555 1555 2.28
LINK O3 PRP B 811 MN MN B 910 1555 1555 2.32
LINK O3B PRP B 811 MN MN B 910 1555 1555 2.21
LINK O1 PRP B 811 MN MN B 910 1555 1555 2.62
LINK O2A PRP B 811 MG MG B 912 1555 1555 2.01
LINK O1B PRP B 811 MG MG B 912 1555 1555 2.21
LINK MN MN B 910 O HOH B1290 1555 1555 2.08
LINK MN MN B 910 O HOH B1291 1555 1555 2.14
LINK MG MG B 912 O HOH B1287 1555 1555 2.15
LINK MG MG B 912 O HOH B1288 1555 1555 2.11
LINK MG MG B 912 O HOH B1289 1555 1555 1.99
CISPEP 1 LEU A 51 LYS A 52 0 -0.34
CISPEP 2 LEU B 551 LYS B 552 0 1.53
CRYST1 39.420 101.760 51.920 90.00 94.23 90.00 P 1 21 1 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 0.025368 0.000000 0.001876 0.00000
SCALE2 0.000000 0.009827 0.000000 0.00000
SCALE3 0.000000 0.000000 0.019313 0.00000
MTRIX1 1 0.865547 0.408421 0.289862 -27.32940 1
MTRIX2 1 0.410351 -0.910140 0.057070 78.46110 1
MTRIX3 1 0.287123 0.069549 -0.955365 65.13820 1
(ATOM LINES ARE NOT SHOWN.)
END
