HEADER OXIDOREDUCTASE 08-OCT-06 2INQ
TITLE NEUTRON CRYSTAL STRUCTURE OF ESCHERICHIA COLI DIHYDROFOLATE REDUCTASE
TITLE 2 BOUND TO THE ANTI-CANCER DRUG, 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;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI K12;
SOURCE 3 ORGANISM_TAXID: 83333;
SOURCE 4 STRAIN: K-12;
SOURCE 5 GENE: FOLA;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: SK383;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PUC8-ECDHFR
KEYWDS NEUTRON STRUCTURE; DEUTERIUM EXCHANGE; PSEUDO-ROSSMAN FOLD;
KEYWDS 2 NUCLEOTIDE BINDING DOMAIN; CHEMOTHERAPY, OXIDOREDUCTASE
EXPDTA NEUTRON DIFFRACTION
AUTHOR B.C.BENNETT,P.A.LANGAN,L.COATES,B.SCHOENBORN,C.G.DEALWIS
REVDAT 5 30-AUG-23 2INQ 1 REMARK
REVDAT 4 20-OCT-21 2INQ 1 SEQADV
REVDAT 3 13-JUL-11 2INQ 1 VERSN
REVDAT 2 24-FEB-09 2INQ 1 VERSN
REVDAT 1 06-FEB-07 2INQ 0
JRNL AUTH B.C.BENNETT,P.A.LANGAN,L.COATES,M.MUSTYAKIMOV,B.SCHOENBORN,
JRNL AUTH 2 E.E.HOWELL,C.G.DEALWIS
JRNL TITL NEUTRON DIFFRACTION STUDIES OF ESCHERICHIA COLI
JRNL TITL 2 DIHYDROFOLATE REDUCTASE COMPLEXED WITH METHOTREXATE.
JRNL REF PROC.NATL.ACAD.SCI.USA V. 103 18493 2006
JRNL REFN ISSN 0027-8424
JRNL PMID 17130456
JRNL DOI 10.1073/PNAS.0604977103
REMARK 2
REMARK 2 RESOLUTION. 2.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : SHELXL-97
REMARK 3 AUTHORS : G.M.SHELDRICK
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 6.50
REMARK 3 DATA CUTOFF (SIGMA(F)) : 3.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 79.7
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (NO CUTOFF).
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) : 0.233
REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : 5.500
REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : 702
REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : 14213
REMARK 3
REMARK 3 FIT/AGREEMENT OF MODEL FOR DATA WITH F>4SIG(F).
REMARK 3 R VALUE (WORKING + TEST SET, F>4SIG(F)) : NULL
REMARK 3 R VALUE (WORKING SET, F>4SIG(F)) : 0.176
REMARK 3 FREE R VALUE (F>4SIG(F)) : 0.232
REMARK 3 FREE R VALUE TEST SET SIZE (%, F>4SIG(F)) : 5.500
REMARK 3 FREE R VALUE TEST SET COUNT (F>4SIG(F)) : 700
REMARK 3 TOTAL NUMBER OF REFLECTIONS (F>4SIG(F)) : 12763
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2516
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 66
REMARK 3 SOLVENT ATOMS : 152
REMARK 3
REMARK 3 MODEL REFINEMENT.
REMARK 3 OCCUPANCY SUM OF NON-HYDROGEN ATOMS : NULL
REMARK 3 OCCUPANCY SUM OF HYDROGEN ATOMS : NULL
REMARK 3 NUMBER OF DISCRETELY DISORDERED RESIDUES : NULL
REMARK 3 NUMBER OF LEAST-SQUARES PARAMETERS : NULL
REMARK 3 NUMBER OF RESTRAINTS : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM RESTRAINT TARGET VALUES.
REMARK 3 BOND LENGTHS (A) : 0.046
REMARK 3 ANGLE DISTANCES (A) : 0.048
REMARK 3 SIMILAR DISTANCES (NO TARGET VALUES) (A) : NULL
REMARK 3 DISTANCES FROM RESTRAINT PLANES (A) : 0.016
REMARK 3 ZERO CHIRAL VOLUMES (A**3) : 0.059
REMARK 3 NON-ZERO CHIRAL VOLUMES (A**3) : 0.052
REMARK 3 ANTI-BUMPING DISTANCE RESTRAINTS (A) : 0.057
REMARK 3 RIGID-BOND ADP COMPONENTS (A**2) : NULL
REMARK 3 SIMILAR ADP COMPONENTS (A**2) : NULL
REMARK 3 APPROXIMATELY ISOTROPIC ADPS (A**2) : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED: NULL
REMARK 3
REMARK 3 STEREOCHEMISTRY TARGET VALUES : ENGH & HUBER
REMARK 3 SPECIAL CASE: NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2INQ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 24-OCT-06.
REMARK 100 THE DEPOSITION ID IS D_1000039793.
REMARK 230
REMARK 230 EXPERIMENTAL DETAILS
REMARK 230 EXPERIMENT TYPE : NEUTRON DIFFRACTION
REMARK 230 DATE OF DATA COLLECTION : 15-FEB-05
REMARK 230 TEMPERATURE (KELVIN) : 293.0
REMARK 230 PH : 7.50
REMARK 230 NUMBER OF CRYSTALS USED : 1
REMARK 230
REMARK 230 NEUTRON SOURCE : NULL
REMARK 230 BEAMLINE : NULL
REMARK 230 WAVELENGTH OR RANGE (A) : 0.6-7.0
REMARK 230 MONOCHROMATOR : CHOPPER
REMARK 230 OPTICS : NULL
REMARK 230
REMARK 230 DETECTOR TYPE : AREA DETECTOR
REMARK 230 DETECTOR MANUFACTURER : TIME-OF-FLIGHT MULTIWIRE HE3
REMARK 230 NEUTRON DETECTOR
REMARK 230 INTENSITY-INTEGRATION SOFTWARE : D*TREK MODIFIED FOR TIME-OF-
REMARK 230 FLIGHT SPOT INTEGRATION
REMARK 230 DATA SCALING SOFTWARE : D*TREK MODIFIED FOR TIME-OF
REMARK 230 -FLIGHT DATA COLLECTION, CCP4
REMARK 230 (SCALA)
REMARK 230
REMARK 230 NUMBER OF UNIQUE REFLECTIONS : 14213
REMARK 230 RESOLUTION RANGE HIGH (A) : 2.170
REMARK 230 RESOLUTION RANGE LOW (A) : 38.600
REMARK 230 REJECTION CRITERIA (SIGMA(I)) : 1.500
REMARK 230
REMARK 230 OVERALL.
REMARK 230 COMPLETENESS FOR RANGE (%) : 79.7
REMARK 230 DATA REDUNDANCY : 2.900
REMARK 230 R MERGE (I) : 0.13600
REMARK 230 R SYM (I) : 0.07000
REMARK 230 <I/SIGMA(I)> FOR THE DATA SET : 3.7000
REMARK 230
REMARK 230 IN THE HIGHEST RESOLUTION SHELL.
REMARK 230 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.17
REMARK 230 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.29
REMARK 230 COMPLETENESS FOR SHELL (%) : 63.7
REMARK 230 DATA REDUNDANCY IN SHELL : 1.70
REMARK 230 R MERGE FOR SHELL (I) : NULL
REMARK 230 R SYM FOR SHELL (I) : 0.32500
REMARK 230 <I/SIGMA(I)> FOR SHELL : 1.700
REMARK 230
REMARK 230 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS
REMARK 230 SOFTWARE USED : SHELXL-97
REMARK 230 STARTING MODEL: 3DRC (293 K E. COLI DHFR/MTX X-RAY STRUCTURE, 1.7A
REMARK 230 RESOLUTION)
REMARK 230
REMARK 230 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 52.03
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.56
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 16% (V/V) POLYETHYLENE GLYCOL 400, 0.2
REMARK 280 M CACL2, 0.1 M NA-HEPES (PH = 7.5); COMPLEX [] = 50 MG/ML,
REMARK 280 MICROBATCH UNDER PARRAFIN OIL, TEMPERATURE 277K, PH 7.50
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 24.62333
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 49.24667
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 36.93500
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 61.55833
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 12.31167
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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 ASYMMETRIC UNIT IS A CRYSTALLOGRAPHIC DIMER, CONTAINING
REMARK 300 2 DISTINCT DHFR MONOMERS. HOWEVER, E. COLI DHFR FUNCTIONS AS A
REMARK 300 MONOMERIC UNIT.
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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 THR A 68 OG1 CG2
REMARK 470 ARG A 71 CA
REMARK 470 GLU A 129 CD OE1 OE2
REMARK 470 ASP A 131 CG OD1 OD2
REMARK 470 ARG A 159 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: 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 D ARG A 71 D ARG A 159 0.14
REMARK 500 NH2 ARG A 44 DG SER A 63 0.69
REMARK 500 DH21 ARG A 44 DG SER A 63 0.88
REMARK 500 N ARG B 158 D ARG B 159 0.96
REMARK 500 D ARG A 71 N ARG A 159 0.97
REMARK 500 CZ ARG A 44 DG SER A 63 1.20
REMARK 500 DE ARG B 44 HB2 GLN B 65 1.30
REMARK 500 OD2 ASP A 116 HB3 SER A 150 1.33
REMARK 500 O DOD B 1186 D2 DOD B 1207 1.44
REMARK 500 O ILE A 5 HA41 MT1 A 1146 1.48
REMARK 500 O GLU B 129 D ASP B 132 1.49
REMARK 500 OE1 GLU B 139 D2 DOD B 1208 1.50
REMARK 500 OE2 GLU A 90 DH TYR A 111 1.50
REMARK 500 DH11 ARG A 98 OE1 GLU A 101 1.51
REMARK 500 OD1 ASP A 142 HG SER A 150 1.55
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 OD2 ASP B 142 DH21 ARG B 159 3564 1.51
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 63 CB - CA - C ANGL. DEV. = 11.6 DEGREES
REMARK 500 ARG A 158 CD - NE - CZ ANGL. DEV. = 9.1 DEGREES
REMARK 500 ARG B 12 CD - NE - CZ ANGL. DEV. = 9.4 DEGREES
REMARK 500 ARG B 12 NE - CZ - NH1 ANGL. DEV. = -5.2 DEGREES
REMARK 500 ARG B 57 NE - CZ - NH1 ANGL. DEV. = -3.9 DEGREES
REMARK 500 ARG B 158 NH1 - CZ - NH2 ANGL. DEV. = 8.9 DEGREES
REMARK 500 ARG B 158 NE - CZ - NH1 ANGL. DEV. = -4.8 DEGREES
REMARK 500 ARG B 158 NE - CZ - NH2 ANGL. DEV. = -4.2 DEGREES
REMARK 500 ARG B 159 NE - CZ - NH2 ANGL. DEV. = -5.4 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 ASP A 11 -0.93 77.43
REMARK 500 ARG A 12 13.36 86.85
REMARK 500 MET A 16 -47.93 -140.91
REMARK 500 GLU A 17 -55.13 -179.16
REMARK 500 ASN A 23 66.73 -156.10
REMARK 500 ARG A 33 -53.87 -28.86
REMARK 500 SER A 63 -136.02 -142.85
REMARK 500 SER A 64 -38.19 -169.59
REMARK 500 PRO A 66 -179.15 -51.55
REMARK 500 THR A 68 -95.81 -58.44
REMARK 500 ASP A 69 162.27 -44.75
REMARK 500 ILE A 94 44.07 -92.00
REMARK 500 ASP A 116 47.36 -77.27
REMARK 500 ASP A 122 -70.74 -95.07
REMARK 500 PRO A 130 -73.24 -28.12
REMARK 500 VAL A 136 -84.22 -86.48
REMARK 500 SER A 138 85.05 -166.90
REMARK 500 ASP A 144 -98.41 -120.26
REMARK 500 SER A 148 6.37 -60.61
REMARK 500 ASP B 11 33.93 78.04
REMARK 500 ALA B 19 153.97 -40.79
REMARK 500 TRP B 22 168.45 177.43
REMARK 500 LEU B 24 77.25 -100.95
REMARK 500 LEU B 36 153.18 -43.63
REMARK 500 LEU B 54 109.27 -56.35
REMARK 500 PRO B 66 161.14 -49.76
REMARK 500 SER B 77 147.58 178.17
REMARK 500 GLU B 90 135.47 -179.84
REMARK 500 ASP B 116 61.44 -68.89
REMARK 500 PRO B 126 166.79 -39.63
REMARK 500 GLU B 129 81.72 -43.16
REMARK 500 PRO B 130 -35.85 -35.44
REMARK 500 ASP B 132 54.28 -113.77
REMARK 500 PHE B 137 116.55 -164.20
REMARK 500 ASP B 144 -158.78 -110.90
REMARK 500 TYR B 151 112.90 -168.09
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 SER A 63 SER A 64 -142.42
REMARK 500
REMARK 500 REMARK: NULL
DBREF 2INQ A 1 159 UNP P0ABQ4 DYR_ECOLI 1 159
DBREF 2INQ B 1 159 UNP P0ABQ4 DYR_ECOLI 1 159
SEQADV 2INQ ASP A 37 UNP P0ABQ4 ASN 37 ENGINEERED MUTATION
SEQADV 2INQ ASP B 37 UNP P0ABQ4 ASN 37 ENGINEERED MUTATION
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
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 GLU ILE LEU
SEQRES 13 B 159 GLU ARG ARG
HET MT1 A1146 53
HET MT1 B1147 53
HETNAM MT1 N-(4-{[(2,4-DIAMINOPTERIDIN-1-IUM-6-YL)METHYL](METHYL)
HETNAM 2 MT1 AMINO}BENZOYL)-L-GLUTAMIC ACID
HETSYN MT1 METHOTREXATE PROTONATED AT N1
FORMUL 3 MT1 2(C20 H23 N8 O5 1+)
FORMUL 5 HOH *152(H2 O)
HELIX 1 1 ASP A 11 VAL A 13 5 3
HELIX 2 2 LEU A 24 LEU A 36 1 13
HELIX 3 3 GLY A 43 GLY A 51 1 9
HELIX 4 4 SER A 77 GLY A 86 1 10
HELIX 5 5 GLY A 96 LEU A 104 1 9
HELIX 6 6 GLU A 129 ASP A 131 5 3
HELIX 7 7 LEU B 24 LEU B 36 1 13
HELIX 8 8 GLY B 43 GLY B 51 1 9
HELIX 9 9 SER B 77 ALA B 84 1 8
HELIX 10 10 GLY B 96 GLN B 102 1 7
HELIX 11 11 PHE B 103 PRO B 105 5 3
HELIX 12 12 GLU B 129 TRP B 133 5 5
SHEET 1 A 8 THR A 73 VAL A 75 0
SHEET 2 A 8 ASN A 59 LEU A 62 1 N ILE A 61 O VAL A 75
SHEET 3 A 8 VAL A 40 MET A 42 1 N MET A 42 O ILE A 60
SHEET 4 A 8 ILE A 91 VAL A 93 1 O MET A 92 N ILE A 41
SHEET 5 A 8 ILE A 2 ALA A 9 1 N SER A 3 O ILE A 91
SHEET 6 A 8 LYS A 109 ILE A 115 1 O TYR A 111 N LEU A 4
SHEET 7 A 8 TYR A 151 ARG A 158 -1 O LEU A 156 N LEU A 110
SHEET 8 A 8 TRP A 133 SER A 135 -1 N GLU A 134 O GLU A 157
SHEET 1 B 8 THR A 73 VAL A 75 0
SHEET 2 B 8 ASN A 59 LEU A 62 1 N ILE A 61 O VAL A 75
SHEET 3 B 8 VAL A 40 MET A 42 1 N MET A 42 O ILE A 60
SHEET 4 B 8 ILE A 91 VAL A 93 1 O MET A 92 N ILE A 41
SHEET 5 B 8 ILE A 2 ALA A 9 1 N SER A 3 O ILE A 91
SHEET 6 B 8 LYS A 109 ILE A 115 1 O TYR A 111 N LEU A 4
SHEET 7 B 8 TYR A 151 ARG A 158 -1 O LEU A 156 N LEU A 110
SHEET 8 B 8 GLU A 139 HIS A 141 -1 N GLU A 139 O PHE A 153
SHEET 1 C 8 THR B 73 VAL B 75 0
SHEET 2 C 8 ASN B 59 LEU B 62 1 N ASN B 59 O THR B 73
SHEET 3 C 8 VAL B 40 MET B 42 1 N VAL B 40 O ILE B 60
SHEET 4 C 8 ILE B 91 VAL B 93 1 O MET B 92 N ILE B 41
SHEET 5 C 8 ILE B 2 LEU B 8 1 N SER B 3 O ILE B 91
SHEET 6 C 8 ALA B 107 HIS B 114 1 O THR B 113 N LEU B 8
SHEET 7 C 8 CYS B 152 GLU B 157 -1 O GLU B 154 N LEU B 112
SHEET 8 C 8 GLU B 134 GLU B 139 -1 N GLU B 139 O PHE B 153
CISPEP 1 GLY A 95 GLY A 96 0 -0.63
CISPEP 2 GLY B 95 GLY B 96 0 2.14
CRYST1 93.120 93.120 73.870 90.00 90.00 120.00 P 61 12
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 0.010739 0.006200 0.000000 0.00000
SCALE2 0.000000 0.012400 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013537 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
