HEADER OXIDOREDUCTASE 10-MAR-14 4P3Q
TITLE ROOM-TEMPERATURE WT DHFR, TIME-AVERAGED ENSEMBLE
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: 316385;
SOURCE 4 STRAIN: K12 / DH10B;
SOURCE 5 GENE: FOLA, ECDH10B_0049;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS ROSSMANN FOLD, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
NUMMDL 167
AUTHOR D.A.KEEDY,H.VAN DEN BEDEM,J.S.FRASER
REVDAT 6 27-DEC-23 4P3Q 1 LINK
REVDAT 5 22-NOV-17 4P3Q 1 COMPND REMARK
REVDAT 4 10-AUG-16 4P3Q 1 REMARK
REVDAT 3 12-NOV-14 4P3Q 1 KEYWDS
REVDAT 2 25-JUN-14 4P3Q 1 JRNL
REVDAT 1 14-MAY-14 4P3Q 0
JRNL AUTH D.A.KEEDY,H.VAN DEN BEDEM,D.A.SIVAK,G.A.PETSKO,D.RINGE,
JRNL AUTH 2 M.A.WILSON,J.S.FRASER
JRNL TITL CRYSTAL CRYOCOOLING DISTORTS CONFORMATIONAL HETEROGENEITY IN
JRNL TITL 2 A MODEL MICHAELIS COMPLEX OF DHFR.
JRNL REF STRUCTURE V. 22 899 2014
JRNL REFN ISSN 1878-4186
JRNL PMID 24882744
JRNL DOI 10.1016/J.STR.2014.04.016
REMARK 2
REMARK 2 RESOLUTION. 1.35 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.ENSEMBLE_REFINEMENT: 1.8.4_1496)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.35
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 41.34
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 91.6
REMARK 3 NUMBER OF REFLECTIONS : 31890
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.120
REMARK 3 R VALUE (WORKING SET) : 0.118
REMARK 3 FREE R VALUE : 0.153
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.080
REMARK 3 FREE R VALUE TEST SET COUNT : 1620
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 41.3629 - 3.0923 1.00 2943 159 0.1293 0.1555
REMARK 3 2 3.0923 - 2.4545 1.00 2818 139 0.1171 0.1514
REMARK 3 3 2.4545 - 2.1443 1.00 2748 162 0.1028 0.1389
REMARK 3 4 2.1443 - 1.9482 0.99 2766 131 0.0963 0.1389
REMARK 3 5 1.9482 - 1.8086 0.99 2679 159 0.0926 0.1207
REMARK 3 6 1.8086 - 1.7020 0.99 2705 146 0.1011 0.1424
REMARK 3 7 1.7020 - 1.6167 0.98 2692 147 0.1153 0.1681
REMARK 3 8 1.6167 - 1.5463 0.98 2654 145 0.1214 0.1666
REMARK 3 9 1.5463 - 1.4868 0.98 2668 146 0.1292 0.1777
REMARK 3 10 1.4868 - 1.4355 0.94 2519 138 0.1607 0.1917
REMARK 3 11 1.4355 - 1.3906 0.67 1818 83 0.1946 0.2343
REMARK 3 12 1.3906 - 1.3509 0.46 1260 65 0.2111 0.2688
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.00
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.080
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 14.400
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 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.066 NULL
REMARK 3 ANGLE : 4.072 NULL
REMARK 3 CHIRALITY : 0.116 NULL
REMARK 3 PLANARITY : 0.012 NULL
REMARK 3 DIHEDRAL : 19.080 NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4P3Q COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 10-MAR-14.
REMARK 100 THE DEPOSITION ID IS D_1000200641.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 20-AUG-11
REMARK 200 TEMPERATURE (KELVIN) : 273
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 8.3.1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.953724
REMARK 200 MONOCHROMATOR : KOHZU DUAL DOUBLE CRYSTAL
REMARK 200 MONOCHROMATOR
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 31891
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.350
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 91.6
REMARK 200 DATA REDUNDANCY : 7.600
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 21.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.35
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.40
REMARK 200 COMPLETENESS FOR SHELL (%) : 48.7
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: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 42.61
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.14
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100MM HEPES PH 7.5, 21% PEG8000, 200MM
REMARK 280 MGCL2, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
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 17.16000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 49.45500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 22.75500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 49.45500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 17.16000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 22.75500
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 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 4 GLU A 154 CB GLU A 154 CG 0.119
REMARK 500 6 VAL A 10 CB VAL A 10 CG2 -0.167
REMARK 500 6 GLU A 101 CB GLU A 101 CG -0.114
REMARK 500 6 CYS A 152 CB CYS A 152 SG 0.171
REMARK 500 7 TYR A 128 CB TYR A 128 CG -0.091
REMARK 500 8 GLU A 101 CB GLU A 101 CG -0.136
REMARK 500 14 GLU A 118 CB GLU A 118 CG 0.150
REMARK 500 17 GLU A 101 CB GLU A 101 CG 0.122
REMARK 500 18 GLU A 139 CB GLU A 139 CG 0.128
REMARK 500 20 GLU A 17 CG GLU A 17 CD -0.102
REMARK 500 21 PRO A 21 CA PRO A 21 C 0.145
REMARK 500 29 LYS A 38 CE LYS A 38 NZ -0.164
REMARK 500 29 GLU A 120 CB GLU A 120 CG 0.145
REMARK 500 29 GLU A 120 CG GLU A 120 CD 0.110
REMARK 500 30 CYS A 85 CB CYS A 85 SG -0.104
REMARK 500 31 LYS A 76 CE LYS A 76 NZ 0.154
REMARK 500 31 GLU A 101 CB GLU A 101 CG 0.117
REMARK 500 32 GLU A 17 CB GLU A 17 CG 0.189
REMARK 500 32 GLU A 101 CB GLU A 101 CG -0.137
REMARK 500 32 ASP A 142 CB ASP A 142 CG 0.127
REMARK 500 33 ARG A 158 CG ARG A 158 CD 0.182
REMARK 500 34 ARG A 158 CG ARG A 158 CD 0.232
REMARK 500 34 ARG A 158 CD ARG A 158 NE 0.115
REMARK 500 35 GLU A 129 CB GLU A 129 CG 0.134
REMARK 500 36 MET A 20 N MET A 20 CA 0.126
REMARK 500 36 GLU A 129 CB GLU A 129 CG 0.124
REMARK 500 39 GLU A 157 CB GLU A 157 CG 0.123
REMARK 500 40 CYS A 152 CB CYS A 152 SG 0.122
REMARK 500 46 CYS A 152 CB CYS A 152 SG 0.113
REMARK 500 50 CYS A 85 CB CYS A 85 SG -0.136
REMARK 500 51 CYS A 85 CB CYS A 85 SG -0.144
REMARK 500 52 CYS A 85 CB CYS A 85 SG -0.129
REMARK 500 56 VAL A 88 CB VAL A 88 CG1 -0.147
REMARK 500 56 ARG A 98 CG ARG A 98 CD -0.203
REMARK 500 57 ASP A 79 CB ASP A 79 CG 0.126
REMARK 500 58 CYS A 152 CB CYS A 152 SG 0.273
REMARK 500 59 LYS A 58 CE LYS A 58 NZ -0.180
REMARK 500 61 VAL A 88 CB VAL A 88 CG2 -0.126
REMARK 500 66 GLU A 157 CG GLU A 157 CD 0.128
REMARK 500 67 CYS A 152 CB CYS A 152 SG 0.175
REMARK 500 69 VAL A 88 CB VAL A 88 CG2 -0.176
REMARK 500 70 TRP A 22 CB TRP A 22 CG 0.146
REMARK 500 70 CYS A 152 CB CYS A 152 SG 0.412
REMARK 500 71 TRP A 22 CB TRP A 22 CG 0.114
REMARK 500 71 CYS A 152 CB CYS A 152 SG 0.310
REMARK 500 74 GLU A 101 CB GLU A 101 CG 0.143
REMARK 500 75 CYS A 152 CB CYS A 152 SG -0.127
REMARK 500 78 MET A 20 CG MET A 20 SD 0.200
REMARK 500 80 TYR A 128 CD1 TYR A 128 CE1 0.098
REMARK 500 81 CYS A 85 CB CYS A 85 SG -0.100
REMARK 500
REMARK 500 THIS ENTRY HAS 127 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 1 PRO A 130 C - N - CA ANGL. DEV. = 14.5 DEGREES
REMARK 500 1 PRO A 130 C - N - CD ANGL. DEV. = -14.5 DEGREES
REMARK 500 3 PRO A 130 C - N - CA ANGL. DEV. = 21.8 DEGREES
REMARK 500 3 PRO A 130 C - N - CD ANGL. DEV. = -28.8 DEGREES
REMARK 500 4 PRO A 21 C - N - CA ANGL. DEV. = 11.6 DEGREES
REMARK 500 4 ARG A 44 NE - CZ - NH2 ANGL. DEV. = -3.6 DEGREES
REMARK 500 4 PRO A 130 C - N - CA ANGL. DEV. = 21.9 DEGREES
REMARK 500 4 PRO A 130 C - N - CD ANGL. DEV. = -30.3 DEGREES
REMARK 500 5 MET A 20 CG - SD - CE ANGL. DEV. = 12.6 DEGREES
REMARK 500 5 PRO A 130 C - N - CA ANGL. DEV. = 26.4 DEGREES
REMARK 500 5 PRO A 130 C - N - CD ANGL. DEV. = -36.8 DEGREES
REMARK 500 6 ARG A 44 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 6 PRO A 130 C - N - CA ANGL. DEV. = 10.1 DEGREES
REMARK 500 6 PRO A 130 C - N - CD ANGL. DEV. = -17.3 DEGREES
REMARK 500 6 CYS A 152 CA - CB - SG ANGL. DEV. = 9.1 DEGREES
REMARK 500 6 LEU A 156 CA - CB - CG ANGL. DEV. = 16.2 DEGREES
REMARK 500 7 ARG A 12 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 7 ARG A 12 NE - CZ - NH2 ANGL. DEV. = -3.6 DEGREES
REMARK 500 7 ARG A 44 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 7 ARG A 44 NE - CZ - NH2 ANGL. DEV. = -3.7 DEGREES
REMARK 500 8 LEU A 4 CB - CG - CD1 ANGL. DEV. = -10.5 DEGREES
REMARK 500 8 ARG A 12 NE - CZ - NH2 ANGL. DEV. = -3.6 DEGREES
REMARK 500 8 MET A 16 CG - SD - CE ANGL. DEV. = 17.2 DEGREES
REMARK 500 8 PRO A 21 C - N - CA ANGL. DEV. = 37.3 DEGREES
REMARK 500 8 PRO A 21 C - N - CD ANGL. DEV. = -37.5 DEGREES
REMARK 500 9 PRO A 21 C - N - CA ANGL. DEV. = 22.5 DEGREES
REMARK 500 9 PRO A 21 C - N - CD ANGL. DEV. = -21.8 DEGREES
REMARK 500 9 PRO A 21 N - CA - C ANGL. DEV. = 18.8 DEGREES
REMARK 500 9 LEU A 104 CB - CG - CD1 ANGL. DEV. = 10.7 DEGREES
REMARK 500 9 VAL A 119 CB - CA - C ANGL. DEV. = -11.9 DEGREES
REMARK 500 11 PRO A 21 C - N - CA ANGL. DEV. = 9.5 DEGREES
REMARK 500 11 PRO A 21 N - CA - C ANGL. DEV. = 17.2 DEGREES
REMARK 500 11 PRO A 130 C - N - CA ANGL. DEV. = -11.0 DEGREES
REMARK 500 12 GLU A 17 N - CA - C ANGL. DEV. = 19.1 DEGREES
REMARK 500 12 PRO A 21 C - N - CA ANGL. DEV. = 11.4 DEGREES
REMARK 500 12 VAL A 119 CB - CA - C ANGL. DEV. = -12.9 DEGREES
REMARK 500 12 VAL A 119 N - CA - C ANGL. DEV. = 16.4 DEGREES
REMARK 500 13 PRO A 21 C - N - CA ANGL. DEV. = 12.6 DEGREES
REMARK 500 13 PRO A 21 C - N - CD ANGL. DEV. = -14.7 DEGREES
REMARK 500 14 LEU A 104 CB - CG - CD2 ANGL. DEV. = 13.1 DEGREES
REMARK 500 14 PRO A 130 C - N - CA ANGL. DEV. = 11.9 DEGREES
REMARK 500 15 ASP A 11 CB - CG - OD1 ANGL. DEV. = 7.4 DEGREES
REMARK 500 15 PRO A 21 C - N - CA ANGL. DEV. = 16.9 DEGREES
REMARK 500 15 PRO A 21 C - N - CD ANGL. DEV. = -14.4 DEGREES
REMARK 500 15 PRO A 130 C - N - CA ANGL. DEV. = 9.5 DEGREES
REMARK 500 16 ASN A 18 N - CA - C ANGL. DEV. = 17.8 DEGREES
REMARK 500 16 LYS A 38 CD - CE - NZ ANGL. DEV. = -15.0 DEGREES
REMARK 500 16 PRO A 130 C - N - CA ANGL. DEV. = 16.3 DEGREES
REMARK 500 16 PRO A 130 C - N - CD ANGL. DEV. = -29.0 DEGREES
REMARK 500 16 ARG A 159 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 569 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 1 GLU A 17 -19.88 58.65
REMARK 500 1 ASN A 18 3.92 147.59
REMARK 500 1 ASP A 87 35.51 -79.13
REMARK 500 1 VAL A 119 121.13 27.52
REMARK 500 1 GLU A 129 65.29 -104.78
REMARK 500 1 PRO A 130 -41.11 -9.87
REMARK 500 1 PHE A 137 131.74 -172.89
REMARK 500 2 ASN A 18 10.87 100.45
REMARK 500 2 TRP A 22 175.87 -59.84
REMARK 500 2 ARG A 52 147.41 177.20
REMARK 500 2 THR A 68 -1.76 -143.05
REMARK 500 2 CYS A 85 -72.05 -57.88
REMARK 500 2 ASP A 87 34.39 -81.26
REMARK 500 2 PRO A 130 -30.96 -27.63
REMARK 500 3 GLU A 17 61.37 14.51
REMARK 500 3 ASN A 18 28.61 44.39
REMARK 500 3 ASP A 69 120.51 -175.72
REMARK 500 3 ASP A 87 69.63 -108.06
REMARK 500 3 PRO A 130 -20.28 7.38
REMARK 500 4 MET A 16 -91.71 -147.24
REMARK 500 4 ASN A 18 52.68 -22.84
REMARK 500 4 ALA A 19 -163.17 -172.37
REMARK 500 4 PRO A 21 -9.73 -45.59
REMARK 500 4 ASP A 69 113.01 -160.92
REMARK 500 4 PRO A 130 -27.44 22.20
REMARK 500 4 PHE A 137 125.87 177.81
REMARK 500 4 SER A 148 42.75 -103.25
REMARK 500 5 MET A 16 -56.84 -137.19
REMARK 500 5 GLU A 17 75.92 -117.60
REMARK 500 5 ASN A 18 5.51 45.78
REMARK 500 5 ARG A 52 157.43 164.09
REMARK 500 5 ASP A 87 13.18 -64.97
REMARK 500 5 GLU A 120 58.30 -94.56
REMARK 500 5 ASP A 127 -118.86 -79.54
REMARK 500 5 TYR A 128 164.15 179.97
REMARK 500 5 PRO A 130 -12.68 5.53
REMARK 500 5 SER A 148 31.32 -88.36
REMARK 500 6 MET A 16 -70.91 -158.38
REMARK 500 6 GLU A 17 47.76 -109.33
REMARK 500 6 ASP A 69 115.86 -167.61
REMARK 500 6 ASP A 87 43.23 -89.01
REMARK 500 6 GLU A 120 45.54 -91.02
REMARK 500 6 ASP A 127 -139.31 -66.84
REMARK 500 6 TYR A 128 138.48 -177.57
REMARK 500 6 GLU A 129 52.02 -104.34
REMARK 500 6 PRO A 130 -56.66 -13.32
REMARK 500 7 MET A 16 -57.65 -150.48
REMARK 500 7 TRP A 22 177.73 -38.02
REMARK 500 7 GLU A 120 40.12 -105.58
REMARK 500 7 PHE A 137 133.17 167.53
REMARK 500
REMARK 500 THIS ENTRY HAS 1410 RAMACHANDRAN OUTLIERS.
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 TYR A 128 GLU A 129 1 -143.05
REMARK 500 MET A 20 PRO A 21 2 -149.14
REMARK 500 GLU A 129 PRO A 130 3 -142.27
REMARK 500 GLY A 86 ASP A 87 4 -147.70
REMARK 500 ASP A 127 TYR A 128 4 -131.05
REMARK 500 GLU A 129 PRO A 130 4 -140.03
REMARK 500 GLU A 17 ASN A 18 5 -138.57
REMARK 500 ASN A 18 ALA A 19 5 -138.04
REMARK 500 GLU A 129 PRO A 130 5 -139.90
REMARK 500 MET A 16 GLU A 17 6 -137.94
REMARK 500 GLU A 17 ASN A 18 6 -145.43
REMARK 500 MET A 16 GLU A 17 7 -126.98
REMARK 500 ASN A 18 ALA A 19 7 -146.00
REMARK 500 ALA A 19 MET A 20 7 -149.95
REMARK 500 MET A 20 PRO A 21 7 -101.52
REMARK 500 ASP A 127 TYR A 128 7 -133.95
REMARK 500 MET A 16 GLU A 17 8 -132.23
REMARK 500 MET A 20 PRO A 21 8 -149.10
REMARK 500 VAL A 119 GLU A 120 8 145.99
REMARK 500 ASP A 127 TYR A 128 8 -129.92
REMARK 500 GLY A 15 MET A 16 9 145.39
REMARK 500 ASN A 18 ALA A 19 9 -149.80
REMARK 500 ALA A 19 MET A 20 9 -146.59
REMARK 500 GLY A 67 THR A 68 9 -145.56
REMARK 500 VAL A 119 GLU A 120 9 130.69
REMARK 500 GLU A 17 ASN A 18 10 -149.79
REMARK 500 MET A 20 PRO A 21 10 -147.99
REMARK 500 PRO A 21 TRP A 22 10 -144.58
REMARK 500 GLY A 67 THR A 68 10 -146.43
REMARK 500 VAL A 119 GLU A 120 10 142.87
REMARK 500 MET A 16 GLU A 17 11 -147.53
REMARK 500 VAL A 119 GLU A 120 11 134.31
REMARK 500 MET A 16 GLU A 17 12 -145.28
REMARK 500 PRO A 21 TRP A 22 12 143.47
REMARK 500 VAL A 119 GLU A 120 12 144.43
REMARK 500 MET A 16 GLU A 17 13 -143.35
REMARK 500 GLU A 17 ASN A 18 13 -143.58
REMARK 500 PRO A 21 TRP A 22 13 136.11
REMARK 500 GLU A 17 ASN A 18 14 -149.93
REMARK 500 ALA A 19 MET A 20 14 139.44
REMARK 500 PRO A 21 TRP A 22 14 145.81
REMARK 500 TYR A 128 GLU A 129 15 -146.63
REMARK 500 MET A 16 GLU A 17 16 140.87
REMARK 500 ASN A 18 ALA A 19 16 137.62
REMARK 500 TYR A 128 GLU A 129 16 -146.28
REMARK 500 MET A 16 GLU A 17 17 139.52
REMARK 500 GLU A 17 ASN A 18 17 -140.41
REMARK 500 ASN A 18 ALA A 19 17 148.65
REMARK 500 MET A 20 PRO A 21 17 135.83
REMARK 500 MET A 16 GLU A 17 18 144.32
REMARK 500
REMARK 500 THIS ENTRY HAS 311 NON CIS, NON-TRANS OMEGA OUTLIERS.
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 17 ASN A 18 -10.07
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A 378 DISTANCE = 6.15 ANGSTROMS
REMARK 525 HOH A 371 DISTANCE = 7.11 ANGSTROMS
REMARK 525 HOH A 394 DISTANCE = 6.85 ANGSTROMS
REMARK 525 HOH A 385 DISTANCE = 7.04 ANGSTROMS
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 A 203 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 11 OD1
REMARK 620 2 GLU A 118 O 160.2
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 202 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 116 O
REMARK 620 2 ARG A 159 O 11.3
REMARK 620 3 HOH A 311 O 38.0 49.3
REMARK 620 4 HOH A 334 O 35.4 46.6 7.0
REMARK 620 5 HOH A 345 O 37.4 48.6 6.1 2.0
REMARK 620 N 1 2 3 4
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue FOL A 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 203
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NAP A 204
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4KJK RELATED DB: PDB
REMARK 900 CORRESPONDING MULTICONFORMER MODEL.
REMARK 900 RELATED ID: 4P3R RELATED DB: PDB
REMARK 900 TIME-AVERAGED ENSEMBLE MODEL
DBREF 4P3Q A 1 159 UNP B1XC49 B1XC49_ECODH 1 159
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 ASN 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 FOL A 201 49
HET CA A 202 1
HET CA A 203 1
HET NAP A 204 72
HETNAM FOL FOLIC ACID
HETNAM CA CALCIUM ION
HETNAM NAP NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE
HETSYN NAP 2'-MONOPHOSPHOADENOSINE 5'-DIPHOSPHORIBOSE
FORMUL 2 FOL C19 H19 N7 O6
FORMUL 3 CA 2(CA 2+)
FORMUL 5 NAP C21 H28 N7 O17 P3
FORMUL 6 HOH *83(H2 O)
HELIX 1 AA1 ALA A 9 ASP A 11 5 3
HELIX 2 AA2 LEU A 24 LEU A 36 1 13
HELIX 3 AA3 ARG A 44 GLY A 51 1 8
HELIX 4 AA4 SER A 77 GLY A 86 1 10
HELIX 5 AA5 GLY A 96 LEU A 104 1 9
HELIX 6 AA6 PRO A 105 ALA A 107 5 3
HELIX 7 AA7 GLU A 129 ASP A 131 5 3
SHEET 1 AA1 8 THR A 73 VAL A 75 0
SHEET 2 AA1 8 LYS A 58 LEU A 62 1 N ILE A 61 O THR A 73
SHEET 3 AA1 8 PRO A 39 GLY A 43 1 N MET A 42 O LEU A 62
SHEET 4 AA1 8 ILE A 91 VAL A 93 1 O MET A 92 N ILE A 41
SHEET 5 AA1 8 ILE A 2 LEU A 8 1 N SER A 3 O ILE A 91
SHEET 6 AA1 8 LYS A 109 ILE A 115 1 O ILE A 115 N LEU A 8
SHEET 7 AA1 8 TYR A 151 ARG A 158 -1 O GLU A 154 N LEU A 112
SHEET 8 AA1 8 TRP A 133 HIS A 141 -1 N VAL A 136 O ILE A 155
SHEET 1 AA2 2 VAL A 13 GLY A 15 0
SHEET 2 AA2 2 THR A 123 HIS A 124 -1 O THR A 123 N ILE A 14
LINK OD1 ASP A 11 CA CA A 203 1555 1555 2.99
LINK O ASP A 116 CA CA A 202 1555 3544 2.36
LINK O GLU A 118 CA CA A 203 1555 1555 3.12
LINK O ARG A 159 CA CA A 202 1555 3644 2.33
LINK CA CA A 202 O HOH A 311 1555 3554 2.27
LINK CA CA A 202 O HOH A 334 1555 3554 2.33
LINK CA CA A 202 O HOH A 345 1555 3554 2.60
SITE 1 AC1 12 ILE A 5 ALA A 6 ALA A 7 ASP A 27
SITE 2 AC1 12 LEU A 28 PHE A 31 ILE A 50 ARG A 52
SITE 3 AC1 12 ARG A 57 ILE A 94 THR A 113 NAP A 204
SITE 1 AC2 3 ASP A 116 HIS A 149 ARG A 159
SITE 1 AC3 3 VAL A 10 ASP A 11 GLU A 118
SITE 1 AC4 27 ALA A 6 ALA A 7 ILE A 14 GLY A 15
SITE 2 AC4 27 MET A 16 ASN A 18 ALA A 19 GLY A 43
SITE 3 AC4 27 ARG A 44 HIS A 45 THR A 46 SER A 49
SITE 4 AC4 27 LEU A 62 SER A 63 SER A 64 GLN A 65
SITE 5 AC4 27 LYS A 76 ILE A 94 GLY A 96 GLY A 97
SITE 6 AC4 27 ARG A 98 VAL A 99 TYR A 100 GLN A 102
SITE 7 AC4 27 THR A 123 ASP A 131 FOL A 201
CRYST1 34.320 45.510 98.910 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 0.029138 0.000000 0.000000 0.00000
SCALE2 0.000000 0.021973 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010110 0.00000
MODEL 1
(ATOM LINES ARE NOT SHOWN.)
END