HEADER OXIDOREDUCTASE 02-AUG-04 1U71
TITLE UNDERSTANDING THE ROLE OF LEU22 VARIANTS IN METHOTREXATE RESISTANCE:
TITLE 2 COMPARISON OF WILD-TYPE AND LEU22ARG VARIANT MOUSE AND HUMAN
TITLE 3 DIHYDROFOLATE REDUCTASE TERNARY CRYSTAL COMPLEXES WITH METHOTREXATE
TITLE 4 AND NADPH
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DIHYDROFOLATE REDUCTASE;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: HUMAN DHFR;
COMPND 5 EC: 1.5.1.3;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: DHFR;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS HUMAN DHFR L22R VARIANT, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR V.CODY,J.R.LUFT,W.PANGBORN
REVDAT 5 03-APR-24 1U71 1 REMARK
REVDAT 4 14-FEB-24 1U71 1 REMARK
REVDAT 3 20-OCT-21 1U71 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1U71 1 VERSN
REVDAT 1 01-FEB-05 1U71 0
JRNL AUTH V.CODY,J.R.LUFT,W.PANGBORN
JRNL TITL UNDERSTANDING THE ROLE OF LEU22 VARIANTS IN METHOTREXATE
JRNL TITL 2 RESISTANCE: COMPARISON OF WILD-TYPE AND LEU22ARG VARIANT
JRNL TITL 3 MOUSE AND HUMAN DIHYDROFOLATE REDUCTASE TERNARY CRYSTAL
JRNL TITL 4 COMPLEXES WITH METHOTREXATE AND NADPH.
JRNL REF ACTA CRYSTALLOGR.,SECT.D V. 61 147 2005
JRNL REFN ISSN 0907-4449
JRNL PMID 15681865
JRNL DOI 10.1107/S0907444904030422
REMARK 2
REMARK 2 RESOLUTION. 2.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PROLSQ
REMARK 3 AUTHORS : KONNERT,HENDRICKSON
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 87.1
REMARK 3 NUMBER OF REFLECTIONS : 6383
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : 2 SIGMA CUTOFF
REMARK 3 R VALUE (WORKING + TEST SET) : NULL
REMARK 3 R VALUE (WORKING SET) : 0.211
REMARK 3 FREE R VALUE : 0.236
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 526
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) : 6909
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1505
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 34
REMARK 3 SOLVENT ATOMS : 68
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) : 0.018 ; NULL
REMARK 3 ANGLE DISTANCE (A) : 0.059 ; 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) : 0.064 ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 0.254 ; 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 1U71 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-AUG-04.
REMARK 100 THE DEPOSITION ID IS D_1000023325.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 18-JUL-94
REMARK 200 TEMPERATURE (KELVIN) : 298
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU RU200
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : GRAPHITE
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IIC
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 6383
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.200
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 87.1
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.05800
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) : 2.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.30
REMARK 200 COMPLETENESS FOR SHELL (%) : 60.5
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PROTEIN
REMARK 200 STARTING MODEL: WILD TYPE HDHFR
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 51.64
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.54
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 62% AS, PHOSPHATE, PH 7.0, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: H 3
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z
REMARK 290 3555 -X+Y,-X,Z
REMARK 290 4555 X+2/3,Y+1/3,Z+1/3
REMARK 290 5555 -Y+2/3,X-Y+1/3,Z+1/3
REMARK 290 6555 -X+Y+2/3,-X+1/3,Z+1/3
REMARK 290 7555 X+1/3,Y+2/3,Z+2/3
REMARK 290 8555 -Y+1/3,X-Y+2/3,Z+2/3
REMARK 290 9555 -X+Y+1/3,-X+2/3,Z+2/3
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 42.57200
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 24.57896
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 26.01400
REMARK 290 SMTRY1 5 -0.500000 -0.866025 0.000000 42.57200
REMARK 290 SMTRY2 5 0.866025 -0.500000 0.000000 24.57896
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 26.01400
REMARK 290 SMTRY1 6 -0.500000 0.866025 0.000000 42.57200
REMARK 290 SMTRY2 6 -0.866025 -0.500000 0.000000 24.57896
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 26.01400
REMARK 290 SMTRY1 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 49.15791
REMARK 290 SMTRY3 7 0.000000 0.000000 1.000000 52.02800
REMARK 290 SMTRY1 8 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 8 0.866025 -0.500000 0.000000 49.15791
REMARK 290 SMTRY3 8 0.000000 0.000000 1.000000 52.02800
REMARK 290 SMTRY1 9 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 -0.500000 0.000000 49.15791
REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 52.02800
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 GLN A 35 OG1 THR A 39 2.12
REMARK 500 OE2 GLU A 154 O HOH A 222 2.12
REMARK 500 O GLU A 161 O HOH A 228 2.17
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 SER A 119 CB SER A 119 OG 0.102
REMARK 500 GLU A 183 CD GLU A 183 OE1 -0.073
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 O - C - N ANGL. DEV. = 9.8 DEGREES
REMARK 500 ALA A 9 CA - C - N ANGL. DEV. = 14.1 DEGREES
REMARK 500 VAL A 10 CB - CA - C ANGL. DEV. = -11.7 DEGREES
REMARK 500 VAL A 10 CA - CB - CG1 ANGL. DEV. = 14.8 DEGREES
REMARK 500 GLN A 12 N - CA - CB ANGL. DEV. = 12.7 DEGREES
REMARK 500 GLN A 12 CA - CB - CG ANGL. DEV. = -13.3 DEGREES
REMARK 500 ASP A 21 CB - CG - OD1 ANGL. DEV. = 9.5 DEGREES
REMARK 500 ASP A 21 CB - CG - OD2 ANGL. DEV. = -8.4 DEGREES
REMARK 500 ARG A 22 NE - CZ - NH1 ANGL. DEV. = 4.1 DEGREES
REMARK 500 GLU A 30 OE1 - CD - OE2 ANGL. DEV. = -8.2 DEGREES
REMARK 500 GLU A 44 CB - CG - CD ANGL. DEV. = 18.4 DEGREES
REMARK 500 PHE A 58 O - C - N ANGL. DEV. = 9.9 DEGREES
REMARK 500 ARG A 65 NE - CZ - NH2 ANGL. DEV. = -5.9 DEGREES
REMARK 500 ARG A 77 NE - CZ - NH1 ANGL. DEV. = 5.7 DEGREES
REMARK 500 ARG A 77 NE - CZ - NH2 ANGL. DEV. = -4.2 DEGREES
REMARK 500 GLU A 81 CG - CD - OE1 ANGL. DEV. = 12.6 DEGREES
REMARK 500 HIS A 87 CE1 - NE2 - CD2 ANGL. DEV. = 4.6 DEGREES
REMARK 500 PHE A 88 O - C - N ANGL. DEV. = 11.5 DEGREES
REMARK 500 ARG A 91 CG - CD - NE ANGL. DEV. = 13.3 DEGREES
REMARK 500 ARG A 91 CD - NE - CZ ANGL. DEV. = 41.8 DEGREES
REMARK 500 ASP A 110 CB - CG - OD1 ANGL. DEV. = 7.1 DEGREES
REMARK 500 ASP A 110 CB - CG - OD2 ANGL. DEV. = -7.2 DEGREES
REMARK 500 GLU A 123 CA - CB - CG ANGL. DEV. = 14.2 DEGREES
REMARK 500 PHE A 134 CB - CG - CD2 ANGL. DEV. = -4.3 DEGREES
REMARK 500 ARG A 137 NE - CZ - NH1 ANGL. DEV. = -6.2 DEGREES
REMARK 500 ARG A 137 NE - CZ - NH2 ANGL. DEV. = 3.2 DEGREES
REMARK 500 ILE A 138 O - C - N ANGL. DEV. = 10.8 DEGREES
REMARK 500 GLN A 140 OE1 - CD - NE2 ANGL. DEV. = 19.6 DEGREES
REMARK 500 GLN A 140 CG - CD - OE1 ANGL. DEV. = -12.2 DEGREES
REMARK 500 ASP A 141 CB - CG - OD1 ANGL. DEV. = 6.8 DEGREES
REMARK 500 ASP A 145 CB - CA - C ANGL. DEV. = 14.7 DEGREES
REMARK 500 ASP A 145 CB - CG - OD1 ANGL. DEV. = 5.8 DEGREES
REMARK 500 ASP A 152 CB - CG - OD1 ANGL. DEV. = 5.7 DEGREES
REMARK 500 GLU A 161 CG - CD - OE2 ANGL. DEV. = -12.6 DEGREES
REMARK 500 TYR A 162 CB - CG - CD2 ANGL. DEV. = -4.6 DEGREES
REMARK 500 GLU A 171 OE1 - CD - OE2 ANGL. DEV. = 10.9 DEGREES
REMARK 500 GLU A 171 O - C - N ANGL. DEV. = 11.1 DEGREES
REMARK 500 GLU A 172 CG - CD - OE1 ANGL. DEV. = 17.4 DEGREES
REMARK 500 ILE A 175 C - N - CA ANGL. DEV. = 16.9 DEGREES
REMARK 500 TYR A 177 CB - CG - CD2 ANGL. DEV. = 5.2 DEGREES
REMARK 500 GLU A 180 OE1 - CD - OE2 ANGL. DEV. = -9.4 DEGREES
REMARK 500 GLU A 180 CG - CD - OE1 ANGL. DEV. = 13.6 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 VAL A 43 99.63 -161.73
REMARK 500 GLU A 44 142.90 -31.35
REMARK 500 PRO A 103 -5.85 -59.36
REMARK 500 GLU A 104 -76.45 -53.71
REMARK 500 ALA A 106 -63.21 -26.02
REMARK 500 ASP A 110 -97.68 -87.28
REMARK 500 ASN A 185 108.33 -165.42
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 SO4 A 188
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 189
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MXA A 187
DBREF 1U71 A 1 186 UNP P00374 DYR_HUMAN 1 186
SEQADV 1U71 ARG A 22 UNP P00374 LEU 22 ENGINEERED MUTATION
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 ARG 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 SO4 A 188 5
HET SO4 A 189 5
HET MXA A 187 24
HETNAM SO4 SULFATE ION
HETNAM MXA 6-(2,5-DIMETHOXY-BENZYL)-5-METHYL-PYRIDO[2,3-
HETNAM 2 MXA D]PYRIMIDINE-2,4-DIAMINE
FORMUL 2 SO4 2(O4 S 2-)
FORMUL 4 MXA C17 H19 N5 O2
FORMUL 5 HOH *68(H2 O)
HELIX 1 1 LEU A 27 THR A 40 1 14
HELIX 2 2 LYS A 54 SER A 59 1 6
HELIX 3 3 ILE A 60 ARG A 65 5 6
HELIX 4 4 SER A 92 GLN A 102 1 11
HELIX 5 5 GLY A 117 MET A 125 1 9
SHEET 1 A 8 PHE A 88 SER A 90 0
SHEET 2 A 8 ILE A 71 LEU A 75 1 N VAL A 74 O PHE A 88
SHEET 3 A 8 GLN A 47 GLY A 53 1 N VAL A 50 O ILE A 71
SHEET 4 A 8 VAL A 109 ILE A 114 1 O TRP A 113 N LEU A 49
SHEET 5 A 8 LEU A 4 VAL A 10 1 N ASN A 5 O VAL A 112
SHEET 6 A 8 HIS A 130 ILE A 138 1 O ILE A 138 N VAL A 10
SHEET 7 A 8 ILE A 175 ASN A 185 -1 O GLU A 180 N VAL A 135
SHEET 8 A 8 LYS A 157 LEU A 158 -1 N LYS A 157 O GLU A 183
SHEET 1 B 8 PHE A 88 SER A 90 0
SHEET 2 B 8 ILE A 71 LEU A 75 1 N VAL A 74 O PHE A 88
SHEET 3 B 8 GLN A 47 GLY A 53 1 N VAL A 50 O ILE A 71
SHEET 4 B 8 VAL A 109 ILE A 114 1 O TRP A 113 N LEU A 49
SHEET 5 B 8 LEU A 4 VAL A 10 1 N ASN A 5 O VAL A 112
SHEET 6 B 8 HIS A 130 ILE A 138 1 O ILE A 138 N VAL A 10
SHEET 7 B 8 ILE A 175 ASN A 185 -1 O GLU A 180 N VAL A 135
SHEET 8 B 8 GLN A 170 GLU A 172 -1 N GLN A 170 O TYR A 177
SHEET 1 C 2 GLY A 15 GLY A 17 0
SHEET 2 C 2 THR A 146 PHE A 147 -1 O THR A 146 N ILE A 16
CISPEP 1 ARG A 65 PRO A 66 0 -0.66
CISPEP 2 GLY A 116 GLY A 117 0 2.26
SITE 1 AC1 8 GLY A 53 LYS A 54 LYS A 55 THR A 56
SITE 2 AC1 8 GLY A 117 SER A 119 VAL A 120 HOH A 239
SITE 1 AC2 4 LYS A 54 SER A 76 ARG A 77 GLU A 78
SITE 1 AC3 15 ILE A 7 VAL A 8 ALA A 9 GLY A 20
SITE 2 AC3 15 ASP A 21 ARG A 22 GLU A 30 PHE A 31
SITE 3 AC3 15 PHE A 34 SER A 59 PRO A 61 ASN A 64
SITE 4 AC3 15 VAL A 115 TYR A 121 THR A 136
CRYST1 85.144 85.144 78.042 90.00 90.00 120.00 H 3 9
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 0.011745 0.006781 0.000000 0.00000
SCALE2 0.000000 0.013562 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012814 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
