HEADER OXIDOREDUCTASE 09-APR-01 1IEI
TITLE CRYSTAL STRUCTURE OF HUMAN ALDOSE REDUCTASE COMPLEXED WITH THE
TITLE 2 INHIBITOR ZENARESTAT.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ALDOSE REDUCTASE;
COMPND 3 CHAIN: A;
COMPND 4 EC: 1.1.1.21;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS PROTEIN-INHIBITOR COMPLEX, NADP, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR T.KINOSHITA,H.MIYAKE,T.FUJII,S.TAKAKURA,T.GOTO
REVDAT 4 13-MAR-24 1IEI 1 REMARK
REVDAT 3 24-FEB-09 1IEI 1 VERSN
REVDAT 2 25-DEC-02 1IEI 1 REMARK
REVDAT 1 10-APR-02 1IEI 0
JRNL AUTH T.KINOSHITA,H.MIYAKE,T.FUJII,S.TAKAKURA,T.GOTO
JRNL TITL THE STRUCTURE OF HUMAN RECOMBINANT ALDOSE REDUCTASE
JRNL TITL 2 COMPLEXED WITH THE POTENT INHIBITOR ZENARESTAT.
JRNL REF ACTA CRYSTALLOGR.,SECT.D V. 58 622 2002
JRNL REFN ISSN 0907-4449
JRNL PMID 11914486
JRNL DOI 10.1107/S0907444902002378
REMARK 2
REMARK 2 RESOLUTION. 2.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 98.1
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 10.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000
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 : 9340
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.178
REMARK 3 FREE R VALUE : 0.199
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 491
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 : 2513
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 74
REMARK 3 SOLVENT ATOMS : 186
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 11.60
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) : 0.039
REMARK 3 BOND ANGLES (DEGREES) : NULL
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 29.80
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: NULL
REMARK 4
REMARK 4 1IEI COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 12-APR-01.
REMARK 100 THE DEPOSITION ID IS D_1000013208.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PHOTON FACTORY
REMARK 200 BEAMLINE : BL-6B
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.000
REMARK 200 MONOCHROMATOR : SILLICON
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : DIFFRACTOMETER
REMARK 200 DETECTOR MANUFACTURER : WEISSENBERG
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 9831
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.500
REMARK 200 RESOLUTION RANGE LOW (A) : 10.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 94.6
REMARK 200 DATA REDUNDANCY : 2.200
REMARK 200 R MERGE (I) : 0.06000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 17.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.59
REMARK 200 COMPLETENESS FOR SHELL (%) : 83.7
REMARK 200 DATA REDUNDANCY IN SHELL : 2.10
REMARK 200 R MERGE FOR SHELL (I) : 0.09100
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: AMORE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 46.04
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.28
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG6000, SODIUM CITRATE, PH 5.0, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,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
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 0
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 ASN A 129 CB CG OD1 ND2
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 TYR A 48 O HOH A 518 2.14
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 TYR A 39 CZ TYR A 39 CE2 0.090
REMARK 500 ILE A 58 CB ILE A 58 CG2 -0.197
REMARK 500 HIS A 83 CG HIS A 83 CD2 0.070
REMARK 500 LEU A 101 CG LEU A 101 CD2 -0.821
REMARK 500 GLY A 151 CA GLY A 151 C 0.128
REMARK 500 PRO A 222 CD PRO A 222 N 0.088
REMARK 500 HIS A 306 CA HIS A 306 CB -0.240
REMARK 500 HIS A 312 CG HIS A 312 CD2 0.073
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ARG A 3 CD - NE - CZ ANGL. DEV. = -12.8 DEGREES
REMARK 500 MET A 12 CG - SD - CE ANGL. DEV. = -15.2 DEGREES
REMARK 500 ARG A 40 NE - CZ - NH2 ANGL. DEV. = -3.8 DEGREES
REMARK 500 ILE A 42 CA - CB - CG2 ANGL. DEV. = -13.4 DEGREES
REMARK 500 VAL A 47 CG1 - CB - CG2 ANGL. DEV. = 10.3 DEGREES
REMARK 500 GLU A 64 CA - CB - CG ANGL. DEV. = 17.1 DEGREES
REMARK 500 GLU A 64 OE1 - CD - OE2 ANGL. DEV. = -7.7 DEGREES
REMARK 500 GLN A 65 N - CA - C ANGL. DEV. = 16.2 DEGREES
REMARK 500 ARG A 69 NE - CZ - NH2 ANGL. DEV. = -4.7 DEGREES
REMARK 500 TYR A 82 CB - CG - CD2 ANGL. DEV. = -4.7 DEGREES
REMARK 500 CYS A 92 CA - CB - SG ANGL. DEV. = 7.3 DEGREES
REMARK 500 LEU A 101 CB - CG - CD2 ANGL. DEV. = -35.5 DEGREES
REMARK 500 ASP A 105 CB - CG - OD2 ANGL. DEV. = 7.2 DEGREES
REMARK 500 PHE A 115 CB - CG - CD1 ANGL. DEV. = -5.8 DEGREES
REMARK 500 GLY A 128 N - CA - C ANGL. DEV. = 16.7 DEGREES
REMARK 500 TRP A 141 N - CA - CB ANGL. DEV. = -12.2 DEGREES
REMARK 500 ALA A 143 N - CA - CB ANGL. DEV. = -9.0 DEGREES
REMARK 500 GLY A 151 C - N - CA ANGL. DEV. = -13.3 DEGREES
REMARK 500 PHE A 161 C - N - CA ANGL. DEV. = 17.5 DEGREES
REMARK 500 CYS A 186 CA - CB - SG ANGL. DEV. = 9.5 DEGREES
REMARK 500 TYR A 189 C - N - CA ANGL. DEV. = -16.1 DEGREES
REMARK 500 TYR A 189 CD1 - CE1 - CZ ANGL. DEV. = -5.5 DEGREES
REMARK 500 TYR A 198 CB - CG - CD2 ANGL. DEV. = -4.0 DEGREES
REMARK 500 TYR A 198 CG - CD1 - CE1 ANGL. DEV. = -5.9 DEGREES
REMARK 500 SER A 201 N - CA - CB ANGL. DEV. = 13.2 DEGREES
REMARK 500 ASP A 216 CA - CB - CG ANGL. DEV. = 15.8 DEGREES
REMARK 500 ARG A 217 CD - NE - CZ ANGL. DEV. = 10.4 DEGREES
REMARK 500 ARG A 217 NE - CZ - NH1 ANGL. DEV. = 9.2 DEGREES
REMARK 500 ARG A 217 NE - CZ - NH2 ANGL. DEV. = -6.2 DEGREES
REMARK 500 LYS A 221 C - N - CA ANGL. DEV. = -16.5 DEGREES
REMARK 500 ASP A 224 CB - CA - C ANGL. DEV. = 17.8 DEGREES
REMARK 500 ARG A 232 NE - CZ - NH1 ANGL. DEV. = -5.7 DEGREES
REMARK 500 ARG A 232 NE - CZ - NH2 ANGL. DEV. = 3.4 DEGREES
REMARK 500 VAL A 259 CG1 - CB - CG2 ANGL. DEV. = 9.6 DEGREES
REMARK 500 ILE A 260 C - N - CA ANGL. DEV. = -15.8 DEGREES
REMARK 500 GLU A 267 CA - CB - CG ANGL. DEV. = 17.0 DEGREES
REMARK 500 THR A 287 CA - CB - CG2 ANGL. DEV. = 8.8 DEGREES
REMARK 500 ARG A 296 NE - CZ - NH2 ANGL. DEV. = 5.7 DEGREES
REMARK 500 VAL A 297 CA - CB - CG1 ANGL. DEV. = 12.0 DEGREES
REMARK 500 ALA A 299 N - CA - C ANGL. DEV. = 18.5 DEGREES
REMARK 500 TYR A 309 CB - CG - CD1 ANGL. DEV. = -6.9 DEGREES
REMARK 500 TYR A 309 CG - CD2 - CE2 ANGL. DEV. = -5.0 DEGREES
REMARK 500 PHE A 315 CB - CG - CD2 ANGL. DEV. = -4.9 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 SER A 2 37.33 -73.59
REMARK 500 ARG A 3 106.73 -170.09
REMARK 500 LYS A 21 -1.60 100.68
REMARK 500 GLU A 51 -55.95 -28.82
REMARK 500 LEU A 62 -75.93 -45.66
REMARK 500 GLN A 65 2.56 121.47
REMARK 500 GLU A 70 -39.05 -38.43
REMARK 500 LEU A 78 104.48 -59.08
REMARK 500 TYR A 82 43.48 -141.85
REMARK 500 LYS A 89 -68.93 -19.15
REMARK 500 PRO A 112 21.82 -62.80
REMARK 500 GLU A 120 100.98 -54.83
REMARK 500 PHE A 121 -7.20 -34.20
REMARK 500 PHE A 122 88.94 -163.90
REMARK 500 ASP A 125 -39.47 -25.91
REMARK 500 GLU A 126 -37.96 88.99
REMARK 500 SER A 127 -135.09 -102.78
REMARK 500 THR A 135 -179.77 -32.96
REMARK 500 ILE A 137 -76.26 -40.86
REMARK 500 THR A 140 -31.59 -141.04
REMARK 500 LEU A 152 -39.16 -36.64
REMARK 500 ALA A 155 166.50 178.96
REMARK 500 ASN A 160 83.11 47.95
REMARK 500 PHE A 161 87.90 111.39
REMARK 500 LEU A 164 -68.51 -13.18
REMARK 500 LEU A 175 95.80 -66.94
REMARK 500 GLN A 183 99.24 -69.98
REMARK 500 HIS A 187 169.18 174.05
REMARK 500 GLN A 192 60.43 39.72
REMARK 500 GLN A 197 33.14 -92.44
REMARK 500 GLN A 200 80.30 109.91
REMARK 500 SER A 201 -10.22 171.47
REMARK 500 LYS A 202 106.49 95.59
REMARK 500 ALA A 208 95.21 -68.49
REMARK 500 SER A 214 78.96 47.79
REMARK 500 PRO A 218 -35.61 -11.65
REMARK 500 PRO A 222 -51.15 -24.02
REMARK 500 GLU A 223 95.27 59.94
REMARK 500 ASP A 224 -139.59 98.92
REMARK 500 SER A 226 74.65 -155.92
REMARK 500 LYS A 234 -42.10 -28.30
REMARK 500 ASN A 241 33.05 31.85
REMARK 500 ASN A 256 32.87 82.32
REMARK 500 ILE A 260 76.44 -102.77
REMARK 500 GLU A 267 -66.25 -20.05
REMARK 500 LYS A 274 46.48 -75.57
REMARK 500 SER A 282 -28.13 -36.25
REMARK 500 ASN A 292 95.23 -58.61
REMARK 500 ALA A 299 -36.54 44.22
REMARK 500 LEU A 300 121.21 16.80
REMARK 500
REMARK 500 THIS ENTRY HAS 52 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 ALA A 1 SER A 2 137.51
REMARK 500 PRO A 112 THR A 113 -148.21
REMARK 500 GLU A 126 SER A 127 144.69
REMARK 500 ASN A 160 PHE A 161 -30.47
REMARK 500 HIS A 163 LEU A 164 145.09
REMARK 500 TYR A 189 LEU A 190 124.59
REMARK 500 LEU A 195 ILE A 196 140.69
REMARK 500 CYS A 199 GLN A 200 -83.18
REMARK 500 SER A 201 LYS A 202 -81.06
REMARK 500 LYS A 202 GLY A 203 -99.39
REMARK 500 LYS A 221 PRO A 222 -113.97
REMARK 500 PRO A 222 GLU A 223 -129.62
REMARK 500 ASP A 224 PRO A 225 -124.65
REMARK 500 CYS A 298 ALA A 299 137.26
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 3 0.33 SIDE CHAIN
REMARK 500 ARG A 63 0.12 SIDE CHAIN
REMARK 500 TYR A 82 0.08 SIDE CHAIN
REMARK 500 PHE A 121 0.11 SIDE CHAIN
REMARK 500 TYR A 189 0.15 SIDE CHAIN
REMARK 500 TYR A 198 0.26 SIDE CHAIN
REMARK 500 TYR A 209 0.10 SIDE CHAIN
REMARK 500 TYR A 291 0.09 SIDE CHAIN
REMARK 500 TYR A 309 0.17 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAP A 350
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZES A 351
DBREF 1IEI A 0 315 UNP P15121 ALDR_HUMAN 1 316
SEQRES 1 A 316 MET ALA SER ARG LEU LEU LEU ASN ASN GLY ALA LYS MET
SEQRES 2 A 316 PRO ILE LEU GLY LEU GLY THR TRP LYS SER PRO PRO GLY
SEQRES 3 A 316 GLN VAL THR GLU ALA VAL LYS VAL ALA ILE ASP VAL GLY
SEQRES 4 A 316 TYR ARG HIS ILE ASP CYS ALA HIS VAL TYR GLN ASN GLU
SEQRES 5 A 316 ASN GLU VAL GLY VAL ALA ILE GLN GLU LYS LEU ARG GLU
SEQRES 6 A 316 GLN VAL VAL LYS ARG GLU GLU LEU PHE ILE VAL SER LYS
SEQRES 7 A 316 LEU TRP CYS THR TYR HIS GLU LYS GLY LEU VAL LYS GLY
SEQRES 8 A 316 ALA CYS GLN LYS THR LEU SER ASP LEU LYS LEU ASP TYR
SEQRES 9 A 316 LEU ASP LEU TYR LEU ILE HIS TRP PRO THR GLY PHE LYS
SEQRES 10 A 316 PRO GLY LYS GLU PHE PHE PRO LEU ASP GLU SER GLY ASN
SEQRES 11 A 316 VAL VAL PRO SER ASP THR ASN ILE LEU ASP THR TRP ALA
SEQRES 12 A 316 ALA MET GLU GLU LEU VAL ASP GLU GLY LEU VAL LYS ALA
SEQRES 13 A 316 ILE GLY ILE SER ASN PHE ASN HIS LEU GLN VAL GLU MET
SEQRES 14 A 316 ILE LEU ASN LYS PRO GLY LEU LYS TYR LYS PRO ALA VAL
SEQRES 15 A 316 ASN GLN ILE GLU CYS HIS PRO TYR LEU THR GLN GLU LYS
SEQRES 16 A 316 LEU ILE GLN TYR CYS GLN SER LYS GLY ILE VAL VAL THR
SEQRES 17 A 316 ALA TYR SER PRO LEU GLY SER PRO ASP ARG PRO TRP ALA
SEQRES 18 A 316 LYS PRO GLU ASP PRO SER LEU LEU GLU ASP PRO ARG ILE
SEQRES 19 A 316 LYS ALA ILE ALA ALA LYS HIS ASN LYS THR THR ALA GLN
SEQRES 20 A 316 VAL LEU ILE ARG PHE PRO MET GLN ARG ASN LEU VAL VAL
SEQRES 21 A 316 ILE PRO LYS SER VAL THR PRO GLU ARG ILE ALA GLU ASN
SEQRES 22 A 316 PHE LYS VAL PHE ASP PHE GLU LEU SER SER GLN ASP MET
SEQRES 23 A 316 THR THR LEU LEU SER TYR ASN ARG ASN TRP ARG VAL CYS
SEQRES 24 A 316 ALA LEU LEU SER CYS THR SER HIS LYS ASP TYR PRO PHE
SEQRES 25 A 316 HIS GLU GLU PHE
HET NAP A 350 48
HET ZES A 351 26
HETNAM NAP NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE
HETNAM ZES [3-(4-BROMO-2-FLUORO-BENZYL)-7-CHLORO-2,4-DIOXO-3,4-
HETNAM 2 ZES DIHYDRO-2H-QUINAZOLIN-1-YL]-ACETIC ACID
HETSYN NAP 2'-MONOPHOSPHOADENOSINE 5'-DIPHOSPHORIBOSE
FORMUL 2 NAP C21 H28 N7 O17 P3
FORMUL 3 ZES C17 H11 BR CL F N2 O4
FORMUL 4 HOH *186(H2 O)
HELIX 1 1 GLN A 26 GLY A 38 1 13
HELIX 2 2 ASN A 50 GLN A 65 1 16
HELIX 3 3 LYS A 68 LEU A 72 5 5
HELIX 4 4 TRP A 79 HIS A 83 5 5
HELIX 5 5 GLU A 84 LYS A 100 1 17
HELIX 6 6 ILE A 137 ALA A 142 1 6
HELIX 7 7 ALA A 142 GLU A 150 1 9
HELIX 8 8 ASN A 162 LEU A 170 1 9
HELIX 9 9 GLN A 192 GLN A 197 1 6
HELIX 10 10 SER A 226 GLU A 229 5 4
HELIX 11 11 ASP A 230 HIS A 240 1 11
HELIX 12 12 THR A 243 GLN A 254 1 12
HELIX 13 13 THR A 265 PHE A 273 1 9
HELIX 14 14 SER A 281 TYR A 291 1 11
SHEET 1 A 2 ARG A 3 LEU A 5 0
SHEET 2 A 2 LYS A 11 PRO A 13 -1 N MET A 12 O LEU A 4
SHEET 1 B 8 GLY A 16 GLY A 18 0
SHEET 2 B 8 HIS A 41 ASP A 43 1 O HIS A 41 N LEU A 17
SHEET 3 B 8 PHE A 73 LEU A 78 1 O PHE A 73 N ILE A 42
SHEET 4 B 8 LEU A 106 ILE A 109 1 N LEU A 106 O ILE A 74
SHEET 5 B 8 ILE A 156 SER A 159 1 N GLY A 157 O TYR A 107
SHEET 6 B 8 VAL A 181 GLU A 185 1 O VAL A 181 N ILE A 158
SHEET 7 B 8 VAL A 205 TYR A 209 1 O VAL A 205 N ASN A 182
SHEET 8 B 8 VAL A 258 VAL A 259 1 O VAL A 258 N ALA A 208
SITE 1 AC1 28 GLY A 18 THR A 19 TRP A 20 LYS A 21
SITE 2 AC1 28 ASP A 43 TYR A 48 LYS A 77 HIS A 110
SITE 3 AC1 28 TRP A 111 SER A 159 ASN A 160 GLN A 183
SITE 4 AC1 28 TYR A 209 SER A 210 PRO A 211 LEU A 212
SITE 5 AC1 28 SER A 214 ASP A 216 ALA A 245 ILE A 260
SITE 6 AC1 28 LYS A 262 SER A 263 VAL A 264 THR A 265
SITE 7 AC1 28 ARG A 268 GLU A 271 ASN A 272 ZES A 351
SITE 1 AC2 13 TRP A 20 VAL A 47 TYR A 48 HIS A 110
SITE 2 AC2 13 TRP A 111 THR A 113 PHE A 122 CYS A 298
SITE 3 AC2 13 ALA A 299 LEU A 300 TYR A 309 NAP A 350
SITE 4 AC2 13 HOH A 477
CRYST1 40.400 47.970 47.660 76.20 76.70 67.50 P 1 1
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 0.024752 -0.010253 -0.004194 0.00000
SCALE2 0.000000 0.022564 -0.003831 0.00000
SCALE3 0.000000 0.000000 0.021869 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
