HEADER OXIDOREDUCTASE 17-SEP-97 1OHJ
TITLE HUMAN DIHYDROFOLATE REDUCTASE, MONOCLINIC (P21) CRYSTAL FORM
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DIHYDROFOLATE REDUCTASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: DHFR;
COMPND 5 EC: 1.5.1.3;
COMPND 6 ENGINEERED: YES;
COMPND 7 OTHER_DETAILS: COMPLEXED WITH NADPH AND PT523 NA-(4-AMINO-4-
COMPND 8 DEOXYPTEROYL)-ND-HEMIPHTHALOYL-L-ORNITHINE
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: POTENTIAL;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: JM107
KEYWDS OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR V.CODY,N.GALITSKY,J.R.LUFT,W.PANGBORN
REVDAT 3 14-FEB-24 1OHJ 1 REMARK
REVDAT 2 24-FEB-09 1OHJ 1 VERSN
REVDAT 1 29-APR-98 1OHJ 0
JRNL AUTH V.CODY,N.GALITSKY,J.R.LUFT,W.PANGBORN,A.ROSOWSKY,R.L.BLAKLEY
JRNL TITL COMPARISON OF TWO INDEPENDENT CRYSTAL STRUCTURES OF HUMAN
JRNL TITL 2 DIHYDROFOLATE REDUCTASE TERNARY COMPLEXES REDUCED WITH
JRNL TITL 3 NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE AND THE VERY
JRNL TITL 4 TIGHT-BINDING INHIBITOR PT523.
JRNL REF BIOCHEMISTRY V. 36 13897 1997
JRNL REFN ISSN 0006-2960
JRNL PMID 9374868
JRNL DOI 10.1021/BI971711L
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH W.S.LEWIS,V.CODY,N.GALITSKY,J.R.LUFT,W.PANGBORN,
REMARK 1 AUTH 2 S.K.CHUNDURU,H.T.SPENCER,J.R.APPLEMAN,R.L.BLAKLEY
REMARK 1 TITL METHOTREXATE-RESISTANT VARIANTS OF HUMAN DIHYDROFOLATE
REMARK 1 TITL 2 REDUCTASE WITH SUBSTITUTIONS OF LEUCINE 22. KINETICS,
REMARK 1 TITL 3 CRYSTALLOGRAPHY, AND POTENTIAL AS SELECTABLE MARKERS
REMARK 1 REF J.BIOL.CHEM. V. 270 5057 1995
REMARK 1 REFN ISSN 0021-9258
REMARK 1 REFERENCE 2
REMARK 1 AUTH S.K.CHUNDURU,V.CODY,J.R.LUFT,W.PANGBORN,J.R.APPLEMAN,
REMARK 1 AUTH 2 R.L.BLAKLEY
REMARK 1 TITL METHOTREXATE-RESISTANT VARIANTS OF HUMAN DIHYDROFOLATE
REMARK 1 TITL 2 REDUCTASE. EFFECTS OF PHE31 SUBSTITUTIONS
REMARK 1 REF J.BIOL.CHEM. V. 269 9547 1994
REMARK 1 REFN ISSN 0021-9258
REMARK 1 REFERENCE 3
REMARK 1 AUTH V.CODY,J.R.LUFT,E.CISZAK,T.I.KALMAN,J.H.FREISHEIM
REMARK 1 TITL CRYSTAL STRUCTURE DETERMINATION AT 2.3 A OF RECOMBINANT
REMARK 1 TITL 2 HUMAN DIHYDROFOLATE REDUCTASE TERNARY COMPLEX WITH NADPH AND
REMARK 1 TITL 3 METHOTREXATE-GAMMA-TETRAZOLE
REMARK 1 REF ANTI-CANCER DRUG DES. V. 7 483 1992
REMARK 1 REFN ISSN 0266-9536
REMARK 2
REMARK 2 RESOLUTION. 2.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PROFFT
REMARK 3 AUTHORS : KONNERT,HENDRICKSON,FINZEL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 8.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 93.4
REMARK 3 NUMBER OF REFLECTIONS : 5276
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING + TEST SET) : NULL
REMARK 3 R VALUE (WORKING SET) : 0.208
REMARK 3 FREE R VALUE : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : NULL
REMARK 3
REMARK 3 FIT/AGREEMENT OF MODEL WITH ALL DATA.
REMARK 3 R VALUE (WORKING + TEST SET, NO CUTOFF) : NULL
REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : NULL
REMARK 3 FREE R VALUE (NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : NULL
REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1502
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 90
REMARK 3 SOLVENT ATOMS : 10
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 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 DISTANCE RESTRAINTS. RMS SIGMA
REMARK 3 BOND LENGTH (A) : 0.014 ; 0.020
REMARK 3 ANGLE DISTANCE (A) : 0.052 ; 0.040
REMARK 3 INTRAPLANAR 1-4 DISTANCE (A) : 0.045 ; 0.050
REMARK 3 H-BOND OR METAL COORDINATION (A) : NULL ; NULL
REMARK 3
REMARK 3 PLANE RESTRAINT (A) : 0.011 ; 0.020
REMARK 3 CHIRAL-CENTER RESTRAINT (A**3) : 0.189 ; 0.150
REMARK 3
REMARK 3 NON-BONDED CONTACT RESTRAINTS.
REMARK 3 SINGLE TORSION (A) : 0.237 ; 0.500
REMARK 3 MULTIPLE TORSION (A) : 0.307 ; 0.500
REMARK 3 H-BOND (X...Y) (A) : 0.346 ; 0.500
REMARK 3 H-BOND (X-H...Y) (A) : NULL ; NULL
REMARK 3
REMARK 3 CONFORMATIONAL TORSION ANGLE RESTRAINTS.
REMARK 3 SPECIFIED (DEGREES) : 0.000 ; 10.000
REMARK 3 PLANAR (DEGREES) : 2.100 ; 3.000
REMARK 3 STAGGERED (DEGREES) : 23.000; 15.000
REMARK 3 TRANSVERSE (DEGREES) : 19.500; 15.000
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 0.690 ; 1.000
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 1.233 ; 1.500
REMARK 3 SIDE-CHAIN BOND (A**2) : 0.578 ; 1.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 1.018 ; 1.500
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1OHJ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000175451.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : NULL
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : NULL
REMARK 200 RADIATION SOURCE : NULL
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : NULL
REMARK 200 WAVELENGTH OR RANGE (A) : NULL
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : NULL
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 5276
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.500
REMARK 200 RESOLUTION RANGE LOW (A) : 8.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 93.4
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
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: NULL
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 (%): 48.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.54
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
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 20.17500
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: 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 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 LEU A 79 NH2 ARG A 91 1.81
REMARK 500 O GLN A 35 OG1 THR A 39 1.94
REMARK 500 OE2 GLU A 62 NH2 ARG A 65 2.03
REMARK 500 OG SER A 42 OD2 ASP A 110 2.13
REMARK 500 NH2 ARG A 70 O24 COP A 188 2.13
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 SER A 3 N - CA - CB ANGL. DEV. = -10.7 DEGREES
REMARK 500 LEU A 22 CB - CA - C ANGL. DEV. = 12.1 DEGREES
REMARK 500 ARG A 28 CD - NE - CZ ANGL. DEV. = 11.1 DEGREES
REMARK 500 ARG A 28 NH1 - CZ - NH2 ANGL. DEV. = -6.8 DEGREES
REMARK 500 ARG A 28 NE - CZ - NH1 ANGL. DEV. = 5.9 DEGREES
REMARK 500 PHE A 31 CA - CB - CG ANGL. DEV. = 17.3 DEGREES
REMARK 500 ARG A 32 NH1 - CZ - NH2 ANGL. DEV. = 9.1 DEGREES
REMARK 500 ARG A 32 NE - CZ - NH2 ANGL. DEV. = -6.4 DEGREES
REMARK 500 TYR A 33 CB - CG - CD1 ANGL. DEV. = -3.6 DEGREES
REMARK 500 ARG A 36 CD - NE - CZ ANGL. DEV. = 9.1 DEGREES
REMARK 500 ARG A 36 NE - CZ - NH1 ANGL. DEV. = 9.1 DEGREES
REMARK 500 ARG A 36 NE - CZ - NH2 ANGL. DEV. = -5.5 DEGREES
REMARK 500 GLU A 44 CB - CG - CD ANGL. DEV. = 16.3 DEGREES
REMARK 500 LYS A 63 C - N - CA ANGL. DEV. = 21.8 DEGREES
REMARK 500 ARG A 65 NH1 - CZ - NH2 ANGL. DEV. = 6.8 DEGREES
REMARK 500 ARG A 65 NE - CZ - NH2 ANGL. DEV. = -3.9 DEGREES
REMARK 500 ARG A 70 CD - NE - CZ ANGL. DEV. = -12.2 DEGREES
REMARK 500 ARG A 77 CD - NE - CZ ANGL. DEV. = -11.3 DEGREES
REMARK 500 ARG A 77 NE - CZ - NH1 ANGL. DEV. = -6.9 DEGREES
REMARK 500 ARG A 77 NE - CZ - NH2 ANGL. DEV. = 6.8 DEGREES
REMARK 500 GLU A 78 C - N - CA ANGL. DEV. = 17.2 DEGREES
REMARK 500 GLU A 78 CB - CA - C ANGL. DEV. = -13.5 DEGREES
REMARK 500 GLU A 78 OE1 - CD - OE2 ANGL. DEV. = 8.7 DEGREES
REMARK 500 GLU A 78 N - CA - C ANGL. DEV. = 17.7 DEGREES
REMARK 500 GLU A 81 CA - CB - CG ANGL. DEV. = 14.5 DEGREES
REMARK 500 GLN A 84 CA - CB - CG ANGL. DEV. = 16.1 DEGREES
REMARK 500 ARG A 91 CD - NE - CZ ANGL. DEV. = -8.4 DEGREES
REMARK 500 ASP A 94 CB - CG - OD2 ANGL. DEV. = -6.3 DEGREES
REMARK 500 ASP A 95 CB - CG - OD1 ANGL. DEV. = 5.7 DEGREES
REMARK 500 VAL A 109 CB - CA - C ANGL. DEV. = -12.9 DEGREES
REMARK 500 GLU A 123 OE1 - CD - OE2 ANGL. DEV. = 8.2 DEGREES
REMARK 500 GLU A 123 CG - CD - OE1 ANGL. DEV. = -13.1 DEGREES
REMARK 500 LYS A 132 N - CA - CB ANGL. DEV. = 11.9 DEGREES
REMARK 500 LEU A 133 CA - CB - CG ANGL. DEV. = 16.2 DEGREES
REMARK 500 ARG A 137 NH1 - CZ - NH2 ANGL. DEV. = -8.4 DEGREES
REMARK 500 ARG A 137 NE - CZ - NH1 ANGL. DEV. = 7.6 DEGREES
REMARK 500 GLN A 140 N - CA - CB ANGL. DEV. = 10.9 DEGREES
REMARK 500 GLN A 140 CA - CB - CG ANGL. DEV. = 17.4 DEGREES
REMARK 500 ASP A 141 CB - CG - OD1 ANGL. DEV. = 13.2 DEGREES
REMARK 500 ASP A 141 CB - CG - OD2 ANGL. DEV. = -7.7 DEGREES
REMARK 500 ASP A 145 CB - CG - OD1 ANGL. DEV. = 12.0 DEGREES
REMARK 500 ASP A 145 CB - CG - OD2 ANGL. DEV. = -7.8 DEGREES
REMARK 500 GLU A 150 CB - CG - CD ANGL. DEV. = 18.1 DEGREES
REMARK 500 GLU A 154 CA - CB - CG ANGL. DEV. = 14.4 DEGREES
REMARK 500 ASP A 168 CA - C - O ANGL. DEV. = 12.7 DEGREES
REMARK 500 GLU A 172 CA - CB - CG ANGL. DEV. = 15.6 DEGREES
REMARK 500 TYR A 177 CB - CG - CD2 ANGL. DEV. = -3.7 DEGREES
REMARK 500 GLU A 183 OE1 - CD - OE2 ANGL. DEV. = 10.2 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 LYS A 18 113.05 -164.02
REMARK 500 ASN A 19 36.83 73.20
REMARK 500 SER A 42 -84.99 -74.75
REMARK 500 PHE A 58 4.19 -69.82
REMARK 500 GLU A 62 -31.84 -22.07
REMARK 500 PRO A 103 -14.43 -44.49
REMARK 500 ASP A 110 -88.36 -106.37
REMARK 500 LEU A 153 1.63 -51.12
REMARK 500 GLU A 161 85.81 54.02
REMARK 500 LYS A 173 44.34 38.61
REMARK 500 ASN A 185 69.64 -155.40
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 ARG A 70 0.11 SIDE CHAIN
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 NDP A 187
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE COP A 188
DBREF 1OHJ A 1 186 UNP P00374 DYR_HUMAN 1 186
SEQRES 1 A 186 VAL GLY SER LEU ASN CYS ILE VAL ALA VAL SER GLN ASN
SEQRES 2 A 186 MET GLY ILE GLY LYS ASN GLY ASP LEU PRO TRP PRO PRO
SEQRES 3 A 186 LEU ARG ASN GLU PHE ARG TYR PHE GLN ARG MET THR THR
SEQRES 4 A 186 THR SER SER VAL GLU GLY LYS GLN ASN LEU VAL ILE MET
SEQRES 5 A 186 GLY LYS LYS THR TRP PHE SER ILE PRO GLU LYS ASN ARG
SEQRES 6 A 186 PRO LEU LYS GLY ARG ILE ASN LEU VAL LEU SER ARG GLU
SEQRES 7 A 186 LEU LYS GLU PRO PRO GLN GLY ALA HIS PHE LEU SER ARG
SEQRES 8 A 186 SER LEU ASP ASP ALA LEU LYS LEU THR GLU GLN PRO GLU
SEQRES 9 A 186 LEU ALA ASN LYS VAL ASP MET VAL TRP ILE VAL GLY GLY
SEQRES 10 A 186 SER SER VAL TYR LYS GLU ALA MET ASN HIS PRO GLY HIS
SEQRES 11 A 186 LEU LYS LEU PHE VAL THR ARG ILE MET GLN ASP PHE GLU
SEQRES 12 A 186 SER ASP THR PHE PHE PRO GLU ILE ASP LEU GLU LYS TYR
SEQRES 13 A 186 LYS LEU LEU PRO GLU TYR PRO GLY VAL LEU SER ASP VAL
SEQRES 14 A 186 GLN GLU GLU LYS GLY ILE LYS TYR LYS PHE GLU VAL TYR
SEQRES 15 A 186 GLU LYS ASN ASP
HET NDP A 187 48
HET COP A 188 56
HETNAM NDP NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE
HETNAM 2 NDP PHOSPHATE
HETNAM COP N-(4-CARBOXY-4-{4-[(2,4-DIAMINO-PTERIDIN-6-YLMETHYL)-
HETNAM 2 COP AMINO]-BENZOYLAMINO}-BUTYL)-PHTHALAMIC ACID
HETSYN COP PT523
FORMUL 2 NDP C21 H30 N7 O17 P3
FORMUL 3 COP C27 H27 N9 O6
FORMUL 4 HOH *10(H2 O)
HELIX 1 1 ARG A 28 THR A 39 1 12
HELIX 2 2 LYS A 54 SER A 59 1 6
HELIX 3 3 GLU A 62 ASN A 64 5 3
HELIX 4 4 LEU A 93 GLU A 101 1 9
HELIX 5 5 PRO A 103 ALA A 106 1 4
HELIX 6 6 SER A 118 ALA A 124 1 7
SHEET 1 A 8 GLN A 170 GLU A 172 0
SHEET 2 A 8 ILE A 175 ASN A 185 -1 N TYR A 177 O GLN A 170
SHEET 3 A 8 HIS A 130 ILE A 138 -1 N ARG A 137 O LYS A 178
SHEET 4 A 8 LEU A 4 VAL A 10 1 N CYS A 6 O LYS A 132
SHEET 5 A 8 VAL A 112 ILE A 114 1 N VAL A 112 O ASN A 5
SHEET 6 A 8 LEU A 49 GLY A 53 1 N LEU A 49 O TRP A 113
SHEET 7 A 8 ILE A 71 LEU A 75 1 N ILE A 71 O VAL A 50
SHEET 8 A 8 PHE A 88 SER A 90 1 N PHE A 88 O VAL A 74
CISPEP 1 ARG A 65 PRO A 66 0 -0.88
CISPEP 2 GLY A 116 GLY A 117 0 0.53
SITE 1 AC1 24 ALA A 9 ILE A 16 GLY A 17 GLY A 20
SITE 2 AC1 24 ASP A 21 LEU A 22 TRP A 24 GLY A 53
SITE 3 AC1 24 LYS A 54 LYS A 55 THR A 56 SER A 59
SITE 4 AC1 24 LEU A 75 SER A 76 ARG A 77 GLU A 78
SITE 5 AC1 24 ARG A 91 GLY A 117 SER A 118 SER A 119
SITE 6 AC1 24 TYR A 121 GLU A 123 COP A 188 HOH A 189
SITE 1 AC2 15 ILE A 7 VAL A 8 GLU A 30 PHE A 31
SITE 2 AC2 15 ARG A 32 PHE A 34 GLN A 35 ILE A 60
SITE 3 AC2 15 ASN A 64 LEU A 67 ARG A 70 VAL A 115
SITE 4 AC2 15 TYR A 121 PRO A 128 NDP A 187
CRYST1 65.822 40.350 75.150 90.00 109.74 90.00 P 1 21 1 2
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 0.015192 0.000000 0.005452 0.00000
SCALE2 0.000000 0.024783 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014138 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
