HEADER OXIDOREDUCTASE 25-JUN-82 4DFR
TITLE CRYSTAL STRUCTURES OF ESCHERICHIA COLI AND LACTOBACILLUS CASEI
TITLE 2 DIHYDROFOLATE REDUCTASE REFINED AT 1.7 ANGSTROMS RESOLUTION. I.
TITLE 3 GENERAL FEATURES AND BINDING OF METHOTREXATE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DIHYDROFOLATE REDUCTASE;
COMPND 3 CHAIN: A, B;
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: 37762;
SOURCE 4 STRAIN: B
KEYWDS OXIDO-REDUCTASE, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR D.J.FILMAN,D.A.MATTHEWS,J.T.BOLIN,J.KRAUT
REVDAT 15 28-FEB-24 4DFR 1 REMARK SEQADV LINK
REVDAT 14 29-NOV-17 4DFR 1 KEYWDS HELIX
REVDAT 13 13-JUL-11 4DFR 1 VERSN
REVDAT 12 26-JAN-10 4DFR 1 ATOM REMARK
REVDAT 11 24-FEB-09 4DFR 1 VERSN
REVDAT 10 01-APR-03 4DFR 1 JRNL
REVDAT 9 15-JUL-92 4DFR 1 FORMUL
REVDAT 8 15-APR-91 4DFR 1 FORMUL
REVDAT 7 16-JUL-87 4DFR 1 SOURCE REMARK
REVDAT 6 12-JUL-85 4DFR 2 CONECT
REVDAT 5 22-FEB-84 4DFR 1 REMARK
REVDAT 4 31-JAN-84 4DFR 1 REMARK
REVDAT 3 30-SEP-83 4DFR 1 REVDAT
REVDAT 2 07-MAR-83 4DFR 1 JRNL REMARK
REVDAT 1 21-OCT-82 4DFR 0
SPRSDE 21-OCT-82 4DFR 2DFR
JRNL AUTH J.T.BOLIN,D.J.FILMAN,D.A.MATTHEWS,R.C.HAMLIN,J.KRAUT
JRNL TITL CRYSTAL STRUCTURES OF ESCHERICHIA COLI AND LACTOBACILLUS
JRNL TITL 2 CASEI DIHYDROFOLATE REDUCTASE REFINED AT 1.7 A RESOLUTION.
JRNL TITL 3 I. GENERAL FEATURES AND BINDING OF METHOTREXATE.
JRNL REF J.BIOL.CHEM. V. 257 13650 1982
JRNL REFN ISSN 0021-9258
JRNL PMID 6815178
REMARK 1
REMARK 1 REFERENCE 1
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 2
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 3
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 4
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 5
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 6
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 7
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 8
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 9
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 10
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. 1.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : NULL
REMARK 3 AUTHORS : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : NULL
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) (%) : 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 SET) : 0.155
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 ESTIMATED ERROR OF FREE R VALUE : NULL
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) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
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 : 2508
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 69
REMARK 3 SOLVENT ATOMS : 428
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) : 0.070
REMARK 3 BOND ANGLES (DEGREES) : NULL
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
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 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 MOLECULE DESIGNATED AS CHAIN B BELOW IS PREFERRED FOR
REMARK 3 STRUCTURAL COMPARISONS BECAUSE IT IS MORE COMPLETE AND LESS
REMARK 3 PERTURBED BY INTERMOLECULAR CONTACTS.
REMARK 3
REMARK 3 ALTERNATE LOCATIONS *A* AND *B* ARE PARTIALLY OCCUPIED
REMARK 3 CONFORMATIONS FOR RESIDUES SER A 64, SER A 150,
REMARK 3 HIS B 45, SER B 64 AND ASP B 122. IN ALL CASES, *A* IS
REMARK 3 BELIEVED TO BE THE MAJOR CONFORMER. NEITHER THE
REMARK 3 OCCUPANCIES NOR THE THERMAL PARAMETERS SHOULD BE
REMARK 3 CONSIDERED AS RELIABLE.
REMARK 4
REMARK 4 4DFR 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_1000179300.
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 (%): 51.93
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.56
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+5/6
REMARK 290 6555 X-Y,X,Z+1/6
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 24.52000
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 49.04000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 36.78000
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 61.30000
REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 12.26000
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 300 REMARK: THE MTRIX TRANSFORMATION PRESENTED BELOW WILL SUPERIMPOSE
REMARK 300 MOLECULE B ON MOLECULE A.
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 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 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 PRO A 66 CB CG CD
REMARK 470 THR A 68 OG1 CG2
REMARK 470 LYS A 76 CG CD CE NZ
REMARK 470 LYS A 106 CE NZ
REMARK 470 GLU A 129 CD OE1 OE2
REMARK 470 ASP A 131 CG OD1 OD2
REMARK 470 ARG A 159 CD NE CZ NH1 NH2
REMARK 470 GLU B 129 CD OE1 OE2
REMARK 470 ASP B 131 CG OD1 OD2
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 MET A 1 CA MET A 1 CB -0.162
REMARK 500 SER A 3 CB SER A 3 OG 0.100
REMARK 500 ALA A 6 CA ALA A 6 CB 0.158
REMARK 500 ALA A 6 C ALA A 6 O 0.127
REMARK 500 ALA A 9 C ALA A 9 O 0.140
REMARK 500 ARG A 12 CZ ARG A 12 NH1 0.084
REMARK 500 ARG A 12 CZ ARG A 12 NH2 0.085
REMARK 500 TRP A 22 CE2 TRP A 22 CD2 -0.148
REMARK 500 TRP A 22 CZ3 TRP A 22 CH2 -0.150
REMARK 500 TRP A 30 CE2 TRP A 30 CD2 -0.111
REMARK 500 TRP A 30 C PHE A 31 N -0.138
REMARK 500 ARG A 33 CZ ARG A 33 NH1 0.109
REMARK 500 ARG A 33 CZ ARG A 33 NH2 0.170
REMARK 500 GLY A 43 C GLY A 43 O 0.169
REMARK 500 ARG A 44 CG ARG A 44 CD -0.166
REMARK 500 ARG A 44 CD ARG A 44 NE 0.130
REMARK 500 ARG A 44 C HIS A 45 N -0.162
REMARK 500 TRP A 47 CD2 TRP A 47 CE3 -0.124
REMARK 500 GLU A 48 CB GLU A 48 CG -0.186
REMARK 500 GLU A 48 CD GLU A 48 OE2 0.162
REMARK 500 SER A 49 CB SER A 49 OG 0.093
REMARK 500 GLY A 51 N GLY A 51 CA -0.128
REMARK 500 ARG A 52 CZ ARG A 52 NH1 0.116
REMARK 500 PRO A 53 C PRO A 53 O -0.139
REMARK 500 GLY A 56 N GLY A 56 CA -0.109
REMARK 500 ARG A 57 CD ARG A 57 NE -0.107
REMARK 500 ARG A 57 CZ ARG A 57 NH2 0.116
REMARK 500 LYS A 58 CD LYS A 58 CE 0.243
REMARK 500 SER A 64 CB SER A 64 OG 0.156
REMARK 500 GLN A 65 C GLN A 65 O 0.143
REMARK 500 ARG A 71 NE ARG A 71 CZ -0.110
REMARK 500 TRP A 74 CB TRP A 74 CG -0.116
REMARK 500 SER A 77 CA SER A 77 CB 0.120
REMARK 500 VAL A 78 CB VAL A 78 CG2 0.172
REMARK 500 VAL A 78 C VAL A 78 O 0.158
REMARK 500 GLU A 90 CA GLU A 90 CB -0.165
REMARK 500 GLU A 90 CG GLU A 90 CD -0.106
REMARK 500 GLU A 90 CD GLU A 90 OE1 -0.066
REMARK 500 VAL A 93 C VAL A 93 O 0.139
REMARK 500 ARG A 98 CD ARG A 98 NE 0.120
REMARK 500 TYR A 100 C TYR A 100 O -0.150
REMARK 500 PHE A 103 CA PHE A 103 C -0.202
REMARK 500 PRO A 105 CD PRO A 105 N 0.101
REMARK 500 LYS A 109 CB LYS A 109 CG -0.216
REMARK 500 LYS A 109 CE LYS A 109 NZ 0.215
REMARK 500 LYS A 109 C LEU A 110 N -0.224
REMARK 500 TYR A 111 C TYR A 111 O 0.201
REMARK 500 TYR A 111 C LEU A 112 N -0.206
REMARK 500 THR A 113 CB THR A 113 OG1 -0.157
REMARK 500 ILE A 115 CA ILE A 115 CB 0.182
REMARK 500
REMARK 500 THIS ENTRY HAS 183 BOND DEVIATIONS.
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 MET A 1 CG - SD - CE ANGL. DEV. = 15.2 DEGREES
REMARK 500 LEU A 4 CB - CG - CD1 ANGL. DEV. = 16.6 DEGREES
REMARK 500 ALA A 6 O - C - N ANGL. DEV. = -15.1 DEGREES
REMARK 500 LEU A 8 CB - CG - CD2 ANGL. DEV. = 21.5 DEGREES
REMARK 500 VAL A 10 CG1 - CB - CG2 ANGL. DEV. = -16.6 DEGREES
REMARK 500 VAL A 10 CA - CB - CG1 ANGL. DEV. = 12.4 DEGREES
REMARK 500 VAL A 10 O - C - N ANGL. DEV. = -11.1 DEGREES
REMARK 500 ASP A 11 OD1 - CG - OD2 ANGL. DEV. = -11.8 DEGREES
REMARK 500 ASP A 11 CB - CG - OD1 ANGL. DEV. = 15.9 DEGREES
REMARK 500 ARG A 12 CG - CD - NE ANGL. DEV. = 16.2 DEGREES
REMARK 500 ARG A 12 CD - NE - CZ ANGL. DEV. = 11.2 DEGREES
REMARK 500 ARG A 12 NE - CZ - NH2 ANGL. DEV. = 8.4 DEGREES
REMARK 500 MET A 16 CG - SD - CE ANGL. DEV. = 30.5 DEGREES
REMARK 500 GLU A 17 O - C - N ANGL. DEV. = 9.7 DEGREES
REMARK 500 ASN A 18 OD1 - CG - ND2 ANGL. DEV. = 15.8 DEGREES
REMARK 500 PRO A 21 CA - N - CD ANGL. DEV. = -10.9 DEGREES
REMARK 500 PRO A 21 N - CD - CG ANGL. DEV. = 12.7 DEGREES
REMARK 500 TRP A 22 CD1 - CG - CD2 ANGL. DEV. = -8.9 DEGREES
REMARK 500 TRP A 22 CG - CD1 - NE1 ANGL. DEV. = 6.8 DEGREES
REMARK 500 TRP A 22 CD1 - NE1 - CE2 ANGL. DEV. = -10.5 DEGREES
REMARK 500 TRP A 22 NE1 - CE2 - CZ2 ANGL. DEV. = -16.5 DEGREES
REMARK 500 TRP A 22 CD2 - CE2 - CZ2 ANGL. DEV. = 12.3 DEGREES
REMARK 500 TRP A 22 CE2 - CD2 - CG ANGL. DEV. = 8.4 DEGREES
REMARK 500 TRP A 22 CG - CD2 - CE3 ANGL. DEV. = -8.6 DEGREES
REMARK 500 TRP A 22 CD2 - CE3 - CZ3 ANGL. DEV. = -11.0 DEGREES
REMARK 500 TRP A 22 CE3 - CZ3 - CH2 ANGL. DEV. = 9.3 DEGREES
REMARK 500 TRP A 22 CH2 - CZ2 - CE2 ANGL. DEV. = -16.5 DEGREES
REMARK 500 ASN A 23 CB - CG - OD1 ANGL. DEV. = 17.1 DEGREES
REMARK 500 PRO A 25 O - C - N ANGL. DEV. = -9.9 DEGREES
REMARK 500 ALA A 29 O - C - N ANGL. DEV. = -10.6 DEGREES
REMARK 500 TRP A 30 CG - CD1 - NE1 ANGL. DEV. = -6.5 DEGREES
REMARK 500 TRP A 30 CG - CD2 - CE3 ANGL. DEV. = -6.5 DEGREES
REMARK 500 TRP A 30 CE3 - CZ3 - CH2 ANGL. DEV. = -7.7 DEGREES
REMARK 500 TRP A 30 CZ3 - CH2 - CZ2 ANGL. DEV. = 8.7 DEGREES
REMARK 500 TRP A 30 CA - C - O ANGL. DEV. = -17.0 DEGREES
REMARK 500 TRP A 30 CA - C - N ANGL. DEV. = 17.4 DEGREES
REMARK 500 PHE A 31 CB - CG - CD2 ANGL. DEV. = -9.6 DEGREES
REMARK 500 PHE A 31 CD1 - CG - CD2 ANGL. DEV. = 8.4 DEGREES
REMARK 500 PHE A 31 CG - CD2 - CE2 ANGL. DEV. = -10.7 DEGREES
REMARK 500 LYS A 32 O - C - N ANGL. DEV. = 9.8 DEGREES
REMARK 500 ARG A 33 NE - CZ - NH2 ANGL. DEV. = 4.3 DEGREES
REMARK 500 ASN A 34 CA - C - N ANGL. DEV. = 14.8 DEGREES
REMARK 500 LEU A 36 CB - CG - CD1 ANGL. DEV. = 11.7 DEGREES
REMARK 500 ASP A 37 CB - CG - OD1 ANGL. DEV. = -5.6 DEGREES
REMARK 500 ASP A 37 CB - CG - OD2 ANGL. DEV. = 7.5 DEGREES
REMARK 500 LYS A 38 CA - CB - CG ANGL. DEV. = 16.4 DEGREES
REMARK 500 GLY A 43 CA - C - N ANGL. DEV. = 15.5 DEGREES
REMARK 500 GLY A 43 O - C - N ANGL. DEV. = -12.9 DEGREES
REMARK 500 ARG A 44 CB - CG - CD ANGL. DEV. = 27.9 DEGREES
REMARK 500 ARG A 44 CD - NE - CZ ANGL. DEV. = -12.7 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 461 ANGLE DEVIATIONS.
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 GLU A 17 -59.56 -145.93
REMARK 500 ASP A 37 11.00 82.49
REMARK 500 PRO A 126 152.49 -44.98
REMARK 500 PRO A 130 1.40 -55.48
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 GLN A 65 PRO A 66 -143.13
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 33 0.13 SIDE CHAIN
REMARK 500 ARG A 44 0.12 SIDE CHAIN
REMARK 500 ARG A 52 0.23 SIDE CHAIN
REMARK 500 ARG A 98 0.16 SIDE CHAIN
REMARK 500 ARG B 12 0.18 SIDE CHAIN
REMARK 500 ARG B 33 0.15 SIDE CHAIN
REMARK 500 ARG B 44 0.13 SIDE CHAIN
REMARK 500 ARG B 52 0.12 SIDE CHAIN
REMARK 500 ARG B 71 0.09 SIDE CHAIN
REMARK 500 ARG B 98 0.09 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 GLN A 65 26.12
REMARK 500 ALA A 117 -10.52
REMARK 500 ALA B 7 -15.62
REMARK 500 ARG B 12 -10.06
REMARK 500 ALA B 29 -10.27
REMARK 500 ILE B 41 -12.81
REMARK 500 HIS B 45 13.58
REMARK 500 PRO B 55 12.67
REMARK 500 ILE B 60 -10.02
REMARK 500 SER B 64 14.61
REMARK 500 GLU B 101 -10.25
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 CA B 161 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A 250 O
REMARK 620 2 SER B 135 O 86.9
REMARK 620 3 HOH B 205 O 86.5 83.1
REMARK 620 4 HOH B 206 O 86.8 167.2 85.3
REMARK 620 5 HOH B 207 O 175.4 96.3 90.4 89.5
REMARK 620 6 HOH B 221 O 85.3 108.9 165.0 81.7 96.9
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: APT
REMARK 800 EVIDENCE_CODE: AUTHOR
REMARK 800 SITE_DESCRIPTION: RESIDUES INTERACTING WITH THE PTERIDINE OF THE
REMARK 800 METHOTREXATE INHIBITOR. INCLUDE WATER MOLECULES WHICH ARE BOUND
REMARK 800 EITHER TO INVARIANT SIDE CHAINS OR TO STRUCTURALLY INVARIANT
REMARK 800 MAIN CHAIN SEGMENTS.
REMARK 800
REMARK 800 SITE_IDENTIFIER: ANM
REMARK 800 EVIDENCE_CODE: AUTHOR
REMARK 800 SITE_DESCRIPTION: RESIDUES INTERACTING WITH THE N(10) METHYL OF
REMARK 800 THE METHOTREXATE INHIBITOR
REMARK 800
REMARK 800 SITE_IDENTIFIER: AAB
REMARK 800 EVIDENCE_CODE: AUTHOR
REMARK 800 SITE_DESCRIPTION: RESIDUES INTERACTING WITH THE P-AMINO BENZOYL OF
REMARK 800 THE METHOTREXATE INHIBITOR
REMARK 800
REMARK 800 SITE_IDENTIFIER: AGL
REMARK 800 EVIDENCE_CODE: AUTHOR
REMARK 800 SITE_DESCRIPTION: RESIDUES INTERACTING WITH THE GLUTAMATE OF THE
REMARK 800 METHOTREXATE INHIBITOR
REMARK 800
REMARK 800 SITE_IDENTIFIER: BPT
REMARK 800 EVIDENCE_CODE: AUTHOR
REMARK 800 SITE_DESCRIPTION: RESIDUES INTERACTING WITH THE PTERIDINE OF THE
REMARK 800 METHOTREXATE INHIBITOR. INCLUDE WATER MOLECULES WHICH ARE BOUND
REMARK 800 EITHER TO INVARIANT SIDE CHAINS OR TO STRUCTURALLY INVARIANT
REMARK 800 MAIN CHAIN SEGMENTS.
REMARK 800
REMARK 800 SITE_IDENTIFIER: BNM
REMARK 800 EVIDENCE_CODE: AUTHOR
REMARK 800 SITE_DESCRIPTION: RESIDUES INTERACTING WITH THE N(10) METHYL OF
REMARK 800 THE METHOTREXATE INHIBITOR
REMARK 800
REMARK 800 SITE_IDENTIFIER: BAB
REMARK 800 EVIDENCE_CODE: AUTHOR
REMARK 800 SITE_DESCRIPTION: RESIDUES INTERACTING WITH THE P-AMINO BENZOYL OF
REMARK 800 THE METHOTREXATE INHIBITOR
REMARK 800
REMARK 800 SITE_IDENTIFIER: BGL
REMARK 800 EVIDENCE_CODE: AUTHOR
REMARK 800 SITE_DESCRIPTION: RESIDUES INTERACTING WITH THE GLUTAMATE OF THE
REMARK 800 METHOTREXATE INHIBITOR
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 160
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 160
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 161
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MTX A 161
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MTX B 162
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 RESIDUE 142 IS LISTED AS ASN IN THE SEQUENCE PAPER
REMARK 999 (SEE REFERENCE 9 ABOVE). THE X-RAY STRUCTURE SUGGESTS IT
REMARK 999 IS ASP (EVIDENCE IS INTERMOLECULAR SALT-LINKAGE TO AN ARG).
DBREF 4DFR A 1 159 UNP P0ABQ4 DYR_ECOLI 1 159
DBREF 4DFR B 1 159 UNP P0ABQ4 DYR_ECOLI 1 159
SEQADV 4DFR ASP A 37 UNP P0ABQ4 ASN 37 CONFLICT
SEQADV 4DFR LYS A 154 UNP P0ABQ4 GLU 154 CONFLICT
SEQADV 4DFR ASP B 37 UNP P0ABQ4 ASN 37 CONFLICT
SEQADV 4DFR LYS B 154 UNP P0ABQ4 GLU 154 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 LYS ILE LEU
SEQRES 13 A 159 GLU ARG ARG
SEQRES 1 B 159 MET ILE SER LEU ILE ALA ALA LEU ALA VAL ASP ARG VAL
SEQRES 2 B 159 ILE GLY MET GLU ASN ALA MET PRO TRP ASN LEU PRO ALA
SEQRES 3 B 159 ASP LEU ALA TRP PHE LYS ARG ASN THR LEU ASP LYS PRO
SEQRES 4 B 159 VAL ILE MET GLY ARG HIS THR TRP GLU SER ILE GLY ARG
SEQRES 5 B 159 PRO LEU PRO GLY ARG LYS ASN ILE ILE LEU SER SER GLN
SEQRES 6 B 159 PRO GLY THR ASP ASP ARG VAL THR TRP VAL LYS SER VAL
SEQRES 7 B 159 ASP GLU ALA ILE ALA ALA CYS GLY ASP VAL PRO GLU ILE
SEQRES 8 B 159 MET VAL ILE GLY GLY GLY ARG VAL TYR GLU GLN PHE LEU
SEQRES 9 B 159 PRO LYS ALA GLN LYS LEU TYR LEU THR HIS ILE ASP ALA
SEQRES 10 B 159 GLU VAL GLU GLY ASP THR HIS PHE PRO ASP TYR GLU PRO
SEQRES 11 B 159 ASP ASP TRP GLU SER VAL PHE SER GLU PHE HIS ASP ALA
SEQRES 12 B 159 ASP ALA GLN ASN SER HIS SER TYR CYS PHE LYS ILE LEU
SEQRES 13 B 159 GLU ARG ARG
HET CL A 160 1
HET MTX A 161 33
HET CL B 160 1
HET CA B 161 1
HET MTX B 162 33
HETNAM CL CHLORIDE ION
HETNAM MTX METHOTREXATE
HETNAM CA CALCIUM ION
FORMUL 3 CL 2(CL 1-)
FORMUL 4 MTX 2(C20 H22 N8 O5)
FORMUL 6 CA CA 2+
FORMUL 8 HOH *428(H2 O)
HELIX 1 HBA LEU A 24 THR A 35 1 12
HELIX 2 HCA GLY A 43 ILE A 50 1 8
HELIX 3 HEA SER A 77 GLY A 86 1 10
HELIX 4 HFA GLY A 96 LEU A 104 1 9
HELIX 5 HBB LEU B 24 THR B 35 1 12
HELIX 6 HCB GLY B 43 ILE B 50 1 8
HELIX 7 HEB SER B 77 GLY B 86 1 10
HELIX 8 HFB GLY B 96 LEU B 104 1 9
SHEET 1 S1A 8 THR A 73 VAL A 75 0
SHEET 2 S1A 8 LYS A 58 SER A 63 1 O ASN A 59 N THR A 73
SHEET 3 S1A 8 PRO A 39 GLY A 43 1 N VAL A 40 O LYS A 58
SHEET 4 S1A 8 ILE A 91 GLY A 95 1 N MET A 92 O PRO A 39
SHEET 5 S1A 8 MET A 1 LEU A 8 1 O MET A 1 N ILE A 91
SHEET 6 S1A 8 GLN A 108 ASP A 116 1 O LYS A 109 N LEU A 4
SHEET 7 S1A 8 SER A 150 ARG A 159 -1 N ARG A 158 O GLN A 108
SHEET 8 S1A 8 ASP A 132 HIS A 141 -1 N GLU A 134 O GLU A 157
SHEET 1 S1B 8 THR B 73 VAL B 75 0
SHEET 2 S1B 8 LYS B 58 SER B 63 1 O ASN B 59 N THR B 73
SHEET 3 S1B 8 PRO B 39 GLY B 43 1 N VAL B 40 O LYS B 58
SHEET 4 S1B 8 PRO B 89 GLY B 95 1 N MET B 92 O PRO B 39
SHEET 5 S1B 8 MET B 1 LEU B 8 1 O MET B 1 N ILE B 91
SHEET 6 S1B 8 GLN B 108 ASP B 116 1 O LYS B 109 N LEU B 4
SHEET 7 S1B 8 SER B 150 ARG B 159 -1 N ARG B 158 O GLN B 108
SHEET 8 S1B 8 ASP B 132 HIS B 141 -1 N GLU B 134 O GLU B 157
LINK O HOH A 250 CA CA B 161 2665 1555 2.56
LINK O SER B 135 CA CA B 161 1555 1555 2.45
LINK CA CA B 161 O HOH B 205 1555 1555 2.47
LINK CA CA B 161 O HOH B 206 1555 2665 2.43
LINK CA CA B 161 O HOH B 207 1555 2665 2.49
LINK CA CA B 161 O HOH B 221 1555 1555 2.59
CISPEP 1 GLY A 95 GLY A 96 0 1.50
CISPEP 2 GLY B 95 GLY B 96 0 -2.65
SITE 1 APT 12 ILE A 5 ALA A 6 ALA A 7 TRP A 22
SITE 2 APT 12 ASP A 27 LEU A 28 PHE A 31 ILE A 94
SITE 3 APT 12 THR A 113 HOH A 163 HOH A 165 HOH A 172
SITE 1 ANM 1 SER A 49
SITE 1 AAB 5 LEU A 28 PHE A 31 ILE A 50 ARG A 52
SITE 2 AAB 5 LEU A 54
SITE 1 AGL 5 LEU A 28 PHE A 31 LYS A 32 LEU A 54
SITE 2 AGL 5 ARG A 57
SITE 1 BPT 12 ILE B 5 ALA B 6 ALA B 7 TRP B 22
SITE 2 BPT 12 ASP B 27 LEU B 28 PHE B 31 ILE B 94
SITE 3 BPT 12 THR B 113 HOH B 170 HOH B 171 HOH B 202
SITE 1 BNM 1 SER B 49
SITE 1 BAB 5 LEU B 28 PHE B 31 ILE B 50 ARG B 52
SITE 2 BAB 5 LEU B 54
SITE 1 BGL 5 LEU B 28 PHE B 31 LYS B 32 LEU B 54
SITE 2 BGL 5 ARG B 57
SITE 1 AC1 6 GLY A 43 HIS A 45 THR A 46 GLY A 96
SITE 2 AC1 6 HOH A 230 HOH A 374
SITE 1 AC2 4 GLY B 43 THR B 46 GLY B 96 HOH B 285
SITE 1 AC3 6 HOH A 250 SER B 135 HOH B 205 HOH B 206
SITE 2 AC3 6 HOH B 207 HOH B 221
SITE 1 AC4 14 ILE A 5 ALA A 6 ASP A 27 PHE A 31
SITE 2 AC4 14 LYS A 32 ARG A 52 ARG A 57 ILE A 94
SITE 3 AC4 14 TYR A 100 THR A 113 HOH A 263 HOH A 296
SITE 4 AC4 14 HOH A 323 HOH A 328
SITE 1 AC5 17 ILE B 5 ALA B 6 ALA B 7 ASP B 27
SITE 2 AC5 17 LEU B 28 PHE B 31 LYS B 32 ILE B 50
SITE 3 AC5 17 ARG B 52 LEU B 54 ARG B 57 ILE B 94
SITE 4 AC5 17 TYR B 100 THR B 113 HOH B 202 HOH B 242
SITE 5 AC5 17 HOH B 260
CRYST1 93.220 93.220 73.560 90.00 90.00 120.00 P 61 12
ORIGX1 0.010727 0.006193 0.000000 0.00000
ORIGX2 0.000000 0.012387 0.000000 0.00000
ORIGX3 0.000000 0.000000 0.013594 0.00000
SCALE1 0.010727 0.006193 0.000000 0.00000
SCALE2 0.000000 0.012387 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013594 0.00000
MTRIX1 1 -0.921160 -0.379660 0.636818 59.21707 1
MTRIX2 1 -0.346230 0.699130 -0.625580 47.40033 1
MTRIX3 1 0.177743 -0.605172 -0.775593 96.59826 1
(ATOM LINES ARE NOT SHOWN.)
END
