HEADER OXIDOREDUCTASE 21-OCT-88 6DFR
TITLE CRYSTAL STRUCTURES OF ESCHERICHIA COLI DIHYDROFOLATE REDUCTASE. THE
TITLE 2 NADP+ HOLOENZYME AND THE FOLATE(DOT)NADP+ TERNARY COMPLEX. SUBSTRATE
TITLE 3 BINDING AND A MODEL FOR THE TRANSITION STATE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DIHYDROFOLATE REDUCTASE;
COMPND 3 CHAIN: A;
COMPND 4 EC: 1.5.1.3;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID
KEYWDS OXIDO-REDUCTASE, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR C.BYSTROFF,S.J.OATLEY,J.KRAUT
REVDAT 5 13-MAR-24 6DFR 1 REMARK SEQADV
REVDAT 4 29-NOV-17 6DFR 1 KEYWDS HELIX
REVDAT 3 24-FEB-09 6DFR 1 VERSN
REVDAT 2 01-APR-03 6DFR 1 JRNL
REVDAT 1 15-JUL-90 6DFR 0
JRNL AUTH C.BYSTROFF,S.J.OATLEY,J.KRAUT
JRNL TITL CRYSTAL STRUCTURES OF ESCHERICHIA COLI DIHYDROFOLATE
JRNL TITL 2 REDUCTASE: THE NADP+ HOLOENZYME AND THE FOLATE.NADP+ TERNARY
JRNL TITL 3 COMPLEX. SUBSTRATE BINDING AND A MODEL FOR THE TRANSITION
JRNL TITL 4 STATE.
JRNL REF BIOCHEMISTRY V. 29 3263 1990
JRNL REFN ISSN 0006-2960
JRNL PMID 2185835
JRNL DOI 10.1021/BI00465A018
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH C.BYSTROFF,J.KRAUT
REMARK 1 TITL CRYSTAL STRUCTURE OF UNLIGANDED ESCHERICHIA COLI
REMARK 1 TITL 2 DIHYDROFOLATE REDUCTASE. LIGAND-INDUCED CONFORMATIONAL
REMARK 1 TITL 3 CHANGES AND COOPERATIVITY IN BINDING
REMARK 1 REF TO BE PUBLISHED
REMARK 1 REFN
REMARK 1 REFERENCE 2
REMARK 1 AUTH J.T.BOLIN,D.J.FILMAN,D.A.MATTHEWS,R.C.HAMLIN,J.KRAUT
REMARK 1 TITL CRYSTAL STRUCTURES OF ESCHERICHIA COLI AND LACTOBACILLUS
REMARK 1 TITL 2 CASEI DIHYDROFOLATE REDUCTASE REFINED AT 1.7 ANGSTROMS
REMARK 1 TITL 3 RESOLUTION. I. GENERAL FEATURES AND BINDING OF METHOTREXATE
REMARK 1 REF J.BIOL.CHEM. V. 257 13650 1982
REMARK 1 REFN ISSN 0021-9258
REMARK 1 REFERENCE 3
REMARK 1 AUTH K.M.PERRY,J.J.ONUFFER,N.A.TOUCHETTE,C.S.HERNDON,
REMARK 1 AUTH 2 M.S.GITTELMAN,C.R.MATTHEWS,J.-T.CHEN,R.J.MAYER,K.TAIRA,
REMARK 1 AUTH 3 S.J.BENKOVIC,E.E.HOWELL,J.KRAUT
REMARK 1 TITL EFFECT OF SINGLE AMINO ACID REPLACEMENTS ON THE FOLDING AND
REMARK 1 TITL 2 STABILITY OF DIHYDROFOLATE REDUCTASE FROM ESCHERICHIA COLI
REMARK 1 REF BIOCHEMISTRY V. 26 2674 1987
REMARK 1 REFN ISSN 0006-2960
REMARK 1 REFERENCE 4
REMARK 1 AUTH D.J.FILMAN,J.T.BOLIN,D.A.MATTHEWS,J.KRAUT
REMARK 1 TITL CRYSTAL STRUCTURES OF ESCHERICHIA COLI AND LACTOBACILLUS
REMARK 1 TITL 2 CASEI DIHYDROFOLATE REDUCTASE REFINED AT 1.7 ANGSTROMS
REMARK 1 TITL 3 RESOLUTION. II. ENVIRONMENT OF BOUND NADPH AND IMPLICATIONS
REMARK 1 TITL 4 FOR CATALYSIS
REMARK 1 REF J.BIOL.CHEM. V. 257 13663 1982
REMARK 1 REFN ISSN 0021-9258
REMARK 1 REFERENCE 5
REMARK 1 AUTH K.W.VOLZ,D.A.MATTHEWS,R.A.ALDEN,S.T.FREER,C.HANSCH,
REMARK 1 AUTH 2 B.T.KAUFMAN,J.KRAUT
REMARK 1 TITL CRYSTAL STRUCTURE OF AVIAN DIHYDROFOLATE REDUCTASE
REMARK 1 TITL 2 CONTAINING PHENYLTRIAZINE AND NADPH
REMARK 1 REF J.BIOL.CHEM. V. 257 2528 1982
REMARK 1 REFN ISSN 0021-9258
REMARK 1 REFERENCE 6
REMARK 1 AUTH D.A.MATTHEWS
REMARK 1 TITL INTERPRETATION OF NUCLEAR MAGNETIC RESONANCE SPECTRA FOR
REMARK 1 TITL 2 LACTOBACILLUS CASEI DIHYDROFOLATE REDUCTASE BASED ON THE
REMARK 1 TITL 3 X-RAY STRUCTURE OF THE ENZYME-METHOTREXATE-NADPH COMPLEX
REMARK 1 REF BIOCHEMISTRY V. 18 1602 1979
REMARK 1 REFN ISSN 0006-2960
REMARK 1 REFERENCE 7
REMARK 1 AUTH D.A.MATTHEWS,R.A.ALDEN,S.T.FREER,N.-H.XUONG,J.KRAUT
REMARK 1 TITL DIHYDROFOLATE REDUCTASE FROM LACTOBACILLUS CASEI.
REMARK 1 TITL 2 STEREOCHEMISTRY OF NADPH BINDING
REMARK 1 REF J.BIOL.CHEM. V. 254 4144 1979
REMARK 1 REFN ISSN 0021-9258
REMARK 1 REFERENCE 8
REMARK 1 AUTH M.POE,K.HOOGSTEEN,D.A.MATTHEWS
REMARK 1 TITL PROTON MAGNETIC RESONANCE STUDIES ON ESCHERICHIA COLI
REMARK 1 TITL 2 DIHYDROFOLATE REDUCTASE. ASSIGNMENT OF HISTIDINE C-2 PROTONS
REMARK 1 TITL 3 IN BINARY COMPLEXES WITH FOLATES ON THE BASIS OF THE CRYSTAL
REMARK 1 TITL 4 STRUCTURE WITH METHOTREXATE AND ON CHEMICAL MODIFICATIONS
REMARK 1 REF J.BIOL.CHEM. V. 254 8143 1979
REMARK 1 REFN ISSN 0021-9258
REMARK 1 REFERENCE 9
REMARK 1 AUTH D.A.MATTHEWS,R.A.ALDEN,J.T.BOLIN,D.J.FILMAN,S.T.FREER,
REMARK 1 AUTH 2 R.HAMLIN,W.G.J.HOL,R.L.KISLIUK,E.J.PASTORE,L.T.PLANTE,
REMARK 1 AUTH 3 N.-H.XUONG,J.KRAUT
REMARK 1 TITL DIHYDROFOLATE REDUCTASE FROM LACTOBACILLUS CASEI. X-RAY
REMARK 1 TITL 2 STRUCTURE OF THE ENZYME-METHOTREXATE-NADPH COMPLEX
REMARK 1 REF J.BIOL.CHEM. V. 253 6946 1978
REMARK 1 REFN ISSN 0021-9258
REMARK 1 REFERENCE 10
REMARK 1 AUTH C.D.BENNETT,J.A.RODKEY,J.M.SONDEY,R.HIRSCHMANN
REMARK 1 TITL DIHYDROFOLATE REDUCTASE. THE AMINO ACID SEQUENCE OF THE
REMARK 1 TITL 2 ENZYME FROM A METHOTREXATE-RESISTANT MUTANT OF ESCHERICHIA
REMARK 1 TITL 3 COLI
REMARK 1 REF BIOCHEMISTRY V. 17 1328 1978
REMARK 1 REFN ISSN 0006-2960
REMARK 1 REFERENCE 11
REMARK 1 AUTH D.A.MATTHEWS,R.A.ALDEN,J.T.BOLIN,S.T.FREER,R.HAMLIN,N.XUONG,
REMARK 1 AUTH 2 J.KRAUT,M.POE,M.WILLIAMS,K.HOOGSTEEN
REMARK 1 TITL DIHYDROFOLATE REDUCTASE. X-RAY STRUCTURE OF THE BINARY
REMARK 1 TITL 2 COMPLEX WITH METHOTREXATE
REMARK 1 REF SCIENCE V. 197 452 1977
REMARK 1 REFN ISSN 0036-8075
REMARK 1 REFERENCE 12
REMARK 1 AUTH M.POE,N.J.GREENFIELD,J.M.HIRSHFIELD,M.N.WILLIAMS,K.HOOGSTEEN
REMARK 1 TITL DIHYDROFOLATE REDUCTASE. PURIFICATION AND CHARACTERIZATION
REMARK 1 TITL 2 OF THE ENZYME FROM AN AMETHOPTERIN-RESISTANT MUTANT OF
REMARK 1 TITL 3 ESCHERICHIA COLI
REMARK 1 REF BIOCHEMISTRY V. 11 1023 1972
REMARK 1 REFN ISSN 0006-2960
REMARK 2
REMARK 2 RESOLUTION. 2.40 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) : 2.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : NULL
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : NULL
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) : 0.192
REMARK 3 R VALUE (WORKING SET) : NULL
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 : 1222
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 37
REMARK 3 SOLVENT ATOMS : 72
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) : 0.020 ; 0.018
REMARK 3 ANGLE DISTANCE (A) : 0.035 ; 0.023
REMARK 3 INTRAPLANAR 1-4 DISTANCE (A) : 0.045 ; 0.035
REMARK 3 H-BOND OR METAL COORDINATION (A) : NULL ; NULL
REMARK 3
REMARK 3 PLANE RESTRAINT (A) : 0.020 ; 0.017
REMARK 3 CHIRAL-CENTER RESTRAINT (A**3) : 0.288 ; 0.200
REMARK 3
REMARK 3 NON-BONDED CONTACT RESTRAINTS.
REMARK 3 SINGLE TORSION (A) : 0.204 ; 0.400
REMARK 3 MULTIPLE TORSION (A) : 0.260 ; 0.400
REMARK 3 H-BOND (X...Y) (A) : NULL ; NULL
REMARK 3 H-BOND (X-H...Y) (A) : 0.240 ; 0.400
REMARK 3
REMARK 3 CONFORMATIONAL TORSION ANGLE RESTRAINTS.
REMARK 3 SPECIFIED (DEGREES) : NULL ; NULL
REMARK 3 PLANAR (DEGREES) : 5.000 ; 5.000
REMARK 3 STAGGERED (DEGREES) : 24.700; 15.000
REMARK 3 TRANSVERSE (DEGREES) : NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 3.924 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 5.455 ; 3.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 4.893 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 6DFR 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_1000179813.
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 : NULL
REMARK 200 RESOLUTION RANGE HIGH (A) : NULL
REMARK 200 RESOLUTION RANGE LOW (A) : NULL
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : NULL
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 (%): 46.93
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.32
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 17.42650
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 40.64100
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 29.50000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 40.64100
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 17.42650
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 29.50000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A 16
REMARK 465 GLU A 17
REMARK 465 ASN A 18
REMARK 465 ALA A 19
REMARK 465 MET A 20
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 120 CG CD OE1 OE2
REMARK 470 ASP A 127 CG OD1 OD2
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 VAL A 136 O HOH A 222 2.02
REMARK 500 O HOH A 256 O HOH A 387 2.12
REMARK 500 O GLY A 15 N ASP A 122 2.13
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH A 219 O HOH A 386 3655 1.98
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 49 CB SER A 49 OG -0.094
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 ALA A 9 N - CA - CB ANGL. DEV. = 9.9 DEGREES
REMARK 500 ASP A 11 CB - CG - OD1 ANGL. DEV. = 5.8 DEGREES
REMARK 500 ARG A 44 NE - CZ - NH1 ANGL. DEV. = -4.2 DEGREES
REMARK 500 ARG A 44 NE - CZ - NH2 ANGL. DEV. = 3.9 DEGREES
REMARK 500 SER A 49 N - CA - CB ANGL. DEV. = 11.1 DEGREES
REMARK 500 ARG A 98 CA - CB - CG ANGL. DEV. = 15.2 DEGREES
REMARK 500 ARG A 98 CD - NE - CZ ANGL. DEV. = 14.2 DEGREES
REMARK 500 ARG A 98 NE - CZ - NH1 ANGL. DEV. = 7.5 DEGREES
REMARK 500 ARG A 98 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES
REMARK 500 VAL A 99 CA - CB - CG1 ANGL. DEV. = 9.7 DEGREES
REMARK 500 GLU A 101 CA - CB - CG ANGL. DEV. = 14.6 DEGREES
REMARK 500 ASP A 144 CB - CG - OD1 ANGL. DEV. = -8.0 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 LEU A 24 79.98 -113.62
REMARK 500 ALA A 117 92.70 -165.97
REMARK 500 ASP A 122 -72.75 -74.59
REMARK 500 PHE A 137 141.08 -172.07
REMARK 500 ASP A 144 -149.14 -148.31
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 52 0.14 SIDE CHAIN
REMARK 500 ARG A 57 0.12 SIDE CHAIN
REMARK 500 ARG A 98 0.11 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 600
REMARK 600 HETEROGEN
REMARK 600
REMARK 600 THE NMN MOIETY OF NADP+ APPEARS TO BE DISORDERED AND
REMARK 600 NO COORDINATES ARE INCLUDED FOR THESE ATOMS.
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 NAP A 164
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 350
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAP A 164
DBREF 6DFR A 1 159 UNP P0ABQ4 DYR_ECOLI 1 159
SEQADV 6DFR ASP A 37 UNP P0ABQ4 ASN 37 CONFLICT
SEQRES 1 A 159 MET ILE SER LEU ILE ALA ALA LEU ALA VAL ASP ARG VAL
SEQRES 2 A 159 ILE GLY MET GLU ASN ALA MET PRO TRP ASN LEU PRO ALA
SEQRES 3 A 159 ASP LEU ALA TRP PHE LYS ARG ASN THR LEU ASP LYS PRO
SEQRES 4 A 159 VAL ILE MET GLY ARG HIS THR TRP GLU SER ILE GLY ARG
SEQRES 5 A 159 PRO LEU PRO GLY ARG LYS ASN ILE ILE LEU SER SER GLN
SEQRES 6 A 159 PRO GLY THR ASP ASP ARG VAL THR TRP VAL LYS SER VAL
SEQRES 7 A 159 ASP GLU ALA ILE ALA ALA CYS GLY ASP VAL PRO GLU ILE
SEQRES 8 A 159 MET VAL ILE GLY GLY GLY ARG VAL TYR GLU GLN PHE LEU
SEQRES 9 A 159 PRO LYS ALA GLN LYS LEU TYR LEU THR HIS ILE ASP ALA
SEQRES 10 A 159 GLU VAL GLU GLY ASP THR HIS PHE PRO ASP TYR GLU PRO
SEQRES 11 A 159 ASP ASP TRP GLU SER VAL PHE SER GLU PHE HIS ASP ALA
SEQRES 12 A 159 ASP ALA GLN ASN SER HIS SER TYR CYS PHE GLU ILE LEU
SEQRES 13 A 159 GLU ARG ARG
HET CA A 350 1
HET NAP A 164 36
HETNAM CA CALCIUM ION
HETNAM NAP NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE
HETSYN NAP 2'-MONOPHOSPHOADENOSINE 5'-DIPHOSPHORIBOSE
FORMUL 2 CA CA 2+
FORMUL 3 NAP C21 H28 N7 O17 P3
FORMUL 4 HOH *72(H2 O)
HELIX 1 HB LEU A 24 THR A 35 1 12
HELIX 2 HC GLY A 43 ILE A 50 1 8
HELIX 3 HE SER A 77 GLY A 86 1 10
HELIX 4 HF GLY A 96 LEU A 104 1 9
SHEET 1 S1 8 THR A 73 VAL A 75 0
SHEET 2 S1 8 LYS A 58 SER A 63 1 O ASN A 59 N THR A 73
SHEET 3 S1 8 PRO A 39 GLY A 43 1 N VAL A 40 O LYS A 58
SHEET 4 S1 8 ILE A 91 GLY A 95 1 N MET A 92 O PRO A 39
SHEET 5 S1 8 MET A 1 LEU A 8 1 O MET A 1 N ILE A 91
SHEET 6 S1 8 GLN A 108 ASP A 116 1 O LYS A 109 N LEU A 4
SHEET 7 S1 8 SER A 150 ARG A 159 -1 N ARG A 158 O GLN A 108
SHEET 8 S1 8 ASP A 132 HIS A 141 -1 N GLU A 134 O GLU A 157
CISPEP 1 GLY A 95 GLY A 96 0 8.06
SITE 1 AC1 1 ILE A 94
SITE 1 AC2 17 ILE A 14 GLY A 43 ARG A 44 HIS A 45
SITE 2 AC2 17 THR A 46 LEU A 62 SER A 63 SER A 64
SITE 3 AC2 17 LYS A 76 GLY A 96 GLY A 97 ARG A 98
SITE 4 AC2 17 VAL A 99 GLN A 102 THR A 123 HOH A 248
SITE 5 AC2 17 HOH A 381
CRYST1 34.853 59.000 81.282 90.00 90.00 90.00 P 21 21 21 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 0.028692 0.000000 0.000000 0.00000
SCALE2 0.000000 0.016949 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012303 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
