HEADER OXIDOREDUCTASE 23-JAN-03 1NR1
TITLE CRYSTAL STRUCTURE OF THE R463A MUTANT OF HUMAN GLUTAMATE DEHYDROGENASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GLUTAMATE DEHYDROGENASE 1;
COMPND 3 CHAIN: A, B, C, D, E, F;
COMPND 4 EC: 1.4.1.3;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: 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 GLUTAMATE DEHYDROGENASE, HEXAMER, REGULATION, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR S.BANERJEE,T.SCHMIDT,J.FANG,C.A.STANLEY,T.J.SMITH
REVDAT 6 14-FEB-24 1NR1 1 REMARK
REVDAT 5 27-OCT-21 1NR1 1 SEQADV
REVDAT 4 11-OCT-17 1NR1 1 REMARK
REVDAT 3 08-FEB-17 1NR1 1 AUTHOR VERSN
REVDAT 2 24-FEB-09 1NR1 1 VERSN
REVDAT 1 06-MAY-03 1NR1 0
JRNL AUTH S.BANERJEE,T.SCHMIDT,J.FANG,C.A.STANLEY,T.J.SMITH
JRNL TITL STRUCTURAL STUDIES ON ADP ACTIVATION OF MAMMALIAN GLUTAMATE
JRNL TITL 2 DEHYDROGENASE AND THE EVOLUTION OF REGULATION
JRNL REF BIOCHEMISTRY V. 42 3446 2003
JRNL REFN ISSN 0006-2960
JRNL PMID 12653548
JRNL DOI 10.1021/BI0206917
REMARK 2
REMARK 2 RESOLUTION. 3.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.99
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 90.9
REMARK 3 NUMBER OF REFLECTIONS : 50903
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.222
REMARK 3 FREE R VALUE : 0.284
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.000
REMARK 3 FREE R VALUE TEST SET COUNT : 5072
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.006
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 3.30
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.51
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 84.60
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 7555
REMARK 3 BIN R VALUE (WORKING SET) : 0.2650
REMARK 3 BIN FREE R VALUE : 0.3500
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.00
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 314
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.020
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 23208
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 0
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 46.60
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 10.63000
REMARK 3 B22 (A**2) : -6.27000
REMARK 3 B33 (A**2) : -4.37000
REMARK 3 B12 (A**2) : 2.27000
REMARK 3 B13 (A**2) : -16.05000
REMARK 3 B23 (A**2) : -1.50000
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) : 0.51
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.53
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.014
REMARK 3 BOND ANGLES (DEGREES) : 1.800
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 22.90
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.240
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 5.180 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 7.830 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 7.550 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 10.010; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.26
REMARK 3 BSOL : 33.61
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 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : ADP.PARAM
REMARK 3 PARAMETER FILE 3 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 4 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : ADP.TOP
REMARK 3 TOPOLOGY FILE 3 : NULL
REMARK 3 TOPOLOGY FILE 4 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1NR1 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 29-JAN-03.
REMARK 100 THE DEPOSITION ID IS D_1000018131.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 06-JUN-00
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.8
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IV
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : R-AXIS
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 50903
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.300
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 91.0
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) : 3.30
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.45
REMARK 200 COMPLETENESS FOR SHELL (%) : 63.0
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: CNS
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 57.89
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.92
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: SODIUM PHOSPHATE, PEG 8000, BOG,
REMARK 280 SODIUM CHLORIDE, MPD, SODIUM AZIDE, PH 6.8, VAPOR DIFFUSION,
REMARK 280 SITTING DROP, TEMPERATURE 298K
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: HEXAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 31560 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 106250 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -140.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F
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: 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 PRO C 433 N VAL C 435 2.09
REMARK 500 O PRO E 433 N VAL E 435 2.09
REMARK 500 O PRO F 433 N VAL F 435 2.12
REMARK 500 O ASP B 172 N SER B 174 2.14
REMARK 500 O ASP D 172 N SER D 174 2.15
REMARK 500 OXT THR B 505 NH2 ARG F 150 2.18
REMARK 500 O ASP E 172 N SER E 174 2.19
REMARK 500 O SER B 104 N GLU B 107 2.19
REMARK 500 O THR C 505 OD1 ASP D 185 2.19
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 CYS A 59 CB CYS A 59 SG 0.161
REMARK 500 CYS C 59 CB CYS C 59 SG 0.148
REMARK 500 CYS C 93 CB CYS C 93 SG -0.097
REMARK 500 CYS D 59 CB CYS D 59 SG 0.130
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 PHE A 504 N - CA - C ANGL. DEV. = -16.5 DEGREES
REMARK 500 PRO B 58 C - N - CA ANGL. DEV. = 10.9 DEGREES
REMARK 500 PRO B 92 C - N - CA ANGL. DEV. = -13.8 DEGREES
REMARK 500 PRO B 137 C - N - CA ANGL. DEV. = 9.5 DEGREES
REMARK 500 CYS C 59 CB - CA - C ANGL. DEV. = 7.6 DEGREES
REMARK 500 SER C 66 N - CA - C ANGL. DEV. = -16.3 DEGREES
REMARK 500 PRO C 92 C - N - CA ANGL. DEV. = -9.1 DEGREES
REMARK 500 PRO C 125 C - N - CA ANGL. DEV. = 12.6 DEGREES
REMARK 500 PRO C 137 C - N - CA ANGL. DEV. = 10.0 DEGREES
REMARK 500 PRO C 244 C - N - CA ANGL. DEV. = 9.7 DEGREES
REMARK 500 PRO C 292 C - N - CA ANGL. DEV. = 9.3 DEGREES
REMARK 500 GLY C 316 N - CA - C ANGL. DEV. = -15.8 DEGREES
REMARK 500 PRO C 373 C - N - CA ANGL. DEV. = 11.6 DEGREES
REMARK 500 THR C 503 N - CA - C ANGL. DEV. = -16.3 DEGREES
REMARK 500 PRO D 169 C - N - CA ANGL. DEV. = 9.6 DEGREES
REMARK 500 LEU D 240 CA - CB - CG ANGL. DEV. = 15.5 DEGREES
REMARK 500 LEU D 326 CA - CB - CG ANGL. DEV. = 15.5 DEGREES
REMARK 500 PHE D 504 N - CA - C ANGL. DEV. = -16.2 DEGREES
REMARK 500 PRO E 244 C - N - CA ANGL. DEV. = 9.2 DEGREES
REMARK 500 PRO F 58 C - N - CA ANGL. DEV. = 11.2 DEGREES
REMARK 500 PRO F 164 C - N - CA ANGL. DEV. = 11.0 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 PRO A 11 174.71 -57.01
REMARK 500 VAL A 33 -77.58 -62.13
REMARK 500 GLU A 34 -131.91 -47.46
REMARK 500 ASP A 35 26.44 -44.78
REMARK 500 ARG A 37 13.21 -157.98
REMARK 500 SER A 41 60.75 -66.35
REMARK 500 LYS A 45 46.51 -87.76
REMARK 500 VAL A 49 16.59 -69.20
REMARK 500 ILE A 52 -56.06 -26.43
REMARK 500 SER A 66 77.71 -166.22
REMARK 500 THR A 91 -70.09 -48.14
REMARK 500 ASP A 123 74.74 35.31
REMARK 500 PRO A 125 66.66 -69.93
REMARK 500 LYS A 130 146.78 -172.23
REMARK 500 LYS A 134 62.23 -16.25
REMARK 500 PRO A 137 -39.91 -37.03
REMARK 500 LYS A 147 -72.14 -38.38
REMARK 500 ILE A 162 106.15 -172.98
REMARK 500 ILE A 166 -60.20 -102.61
REMARK 500 ASP A 172 98.18 -172.58
REMARK 500 MET A 173 -80.82 36.72
REMARK 500 GLU A 177 -2.77 -53.32
REMARK 500 THR A 190 -107.37 -120.87
REMARK 500 ASP A 195 99.33 -64.20
REMARK 500 ILE A 196 -9.38 -53.75
REMARK 500 HIS A 199 -7.33 -56.70
REMARK 500 ALA A 218 -75.81 -26.42
REMARK 500 ALA A 234 -77.78 -67.79
REMARK 500 SER A 235 -41.19 -27.01
REMARK 500 MET A 242 -154.69 -90.75
REMARK 500 PRO A 244 -165.33 -66.27
REMARK 500 PHE A 246 -17.09 -142.77
REMARK 500 ASP A 248 -88.32 3.08
REMARK 500 LEU A 261 -79.00 -57.49
REMARK 500 HIS A 268 -72.89 -52.98
REMARK 500 ARG A 269 -30.53 -34.94
REMARK 500 PHE A 270 59.02 -109.66
REMARK 500 ASP A 281 -123.04 -99.88
REMARK 500 ASN A 286 97.74 165.12
REMARK 500 PRO A 287 -8.69 -59.75
REMARK 500 GLN A 301 -36.88 -34.67
REMARK 500 SER A 304 -158.83 -122.56
REMARK 500 LYS A 310 26.45 110.35
REMARK 500 PRO A 313 104.34 -45.68
REMARK 500 SER A 317 99.24 30.07
REMARK 500 ALA A 321 138.80 -16.51
REMARK 500 ALA A 329 55.63 -101.57
REMARK 500 ALA A 330 172.20 168.42
REMARK 500 SER A 331 115.47 43.78
REMARK 500 LYS A 333 81.06 20.51
REMARK 500
REMARK 500 THIS ENTRY HAS 377 RAMACHANDRAN OUTLIERS.
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 TYR D 266 0.07 SIDE CHAIN
REMARK 500 TYR D 459 0.08 SIDE CHAIN
REMARK 500 TYR E 187 0.09 SIDE CHAIN
REMARK 500 TYR E 398 0.08 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1L1F RELATED DB: PDB
REMARK 900 STRUCTURE OF APO-HUMAN GLUTAMATE DEHYDROGENASE
REMARK 900 RELATED ID: 1NQT RELATED DB: PDB
REMARK 900 RELATED ID: 1NR7 RELATED DB: PDB
DBREF 1NR1 A 10 505 UNP P00367 DHE3_HUMAN 63 558
DBREF 1NR1 B 10 505 UNP P00367 DHE3_HUMAN 63 558
DBREF 1NR1 C 10 505 UNP P00367 DHE3_HUMAN 63 558
DBREF 1NR1 D 10 505 UNP P00367 DHE3_HUMAN 63 558
DBREF 1NR1 E 10 505 UNP P00367 DHE3_HUMAN 63 558
DBREF 1NR1 F 10 505 UNP P00367 DHE3_HUMAN 63 558
SEQADV 1NR1 GLN A 88 UNP P00367 HIS 141 CONFLICT
SEQADV 1NR1 HIS A 89 UNP P00367 GLN 142 CONFLICT
SEQADV 1NR1 ALA A 463 UNP P00367 ARG 516 ENGINEERED MUTATION
SEQADV 1NR1 GLN B 88 UNP P00367 HIS 141 CONFLICT
SEQADV 1NR1 HIS B 89 UNP P00367 GLN 142 CONFLICT
SEQADV 1NR1 ALA B 463 UNP P00367 ARG 516 ENGINEERED MUTATION
SEQADV 1NR1 GLN C 88 UNP P00367 HIS 141 CONFLICT
SEQADV 1NR1 HIS C 89 UNP P00367 GLN 142 CONFLICT
SEQADV 1NR1 ALA C 463 UNP P00367 ARG 516 ENGINEERED MUTATION
SEQADV 1NR1 GLN D 88 UNP P00367 HIS 141 CONFLICT
SEQADV 1NR1 HIS D 89 UNP P00367 GLN 142 CONFLICT
SEQADV 1NR1 ALA D 463 UNP P00367 ARG 516 ENGINEERED MUTATION
SEQADV 1NR1 GLN E 88 UNP P00367 HIS 141 CONFLICT
SEQADV 1NR1 HIS E 89 UNP P00367 GLN 142 CONFLICT
SEQADV 1NR1 ALA E 463 UNP P00367 ARG 516 ENGINEERED MUTATION
SEQADV 1NR1 GLN F 88 UNP P00367 HIS 141 CONFLICT
SEQADV 1NR1 HIS F 89 UNP P00367 GLN 142 CONFLICT
SEQADV 1NR1 ALA F 463 UNP P00367 ARG 516 ENGINEERED MUTATION
SEQRES 1 A 496 ASP PRO ASN PHE PHE LYS MET VAL GLU GLY PHE PHE ASP
SEQRES 2 A 496 ARG GLY ALA SER ILE VAL GLU ASP LYS LEU VAL GLU ASP
SEQRES 3 A 496 LEU ARG THR ARG GLU SER GLU GLU GLN LYS ARG ASN ARG
SEQRES 4 A 496 VAL ARG GLY ILE LEU ARG ILE ILE LYS PRO CYS ASN HIS
SEQRES 5 A 496 VAL LEU SER LEU SER PHE PRO ILE ARG ARG ASP ASP GLY
SEQRES 6 A 496 SER TRP GLU VAL ILE GLU GLY TYR ARG ALA GLN HIS SER
SEQRES 7 A 496 GLN HIS ARG THR PRO CYS LYS GLY GLY ILE ARG TYR SER
SEQRES 8 A 496 THR ASP VAL SER VAL ASP GLU VAL LYS ALA LEU ALA SER
SEQRES 9 A 496 LEU MET THR TYR LYS CYS ALA VAL VAL ASP VAL PRO PHE
SEQRES 10 A 496 GLY GLY ALA LYS ALA GLY VAL LYS ILE ASN PRO LYS ASN
SEQRES 11 A 496 TYR THR ASP ASN GLU LEU GLU LYS ILE THR ARG ARG PHE
SEQRES 12 A 496 THR MET GLU LEU ALA LYS LYS GLY PHE ILE GLY PRO GLY
SEQRES 13 A 496 ILE ASP VAL PRO ALA PRO ASP MET SER THR GLY GLU ARG
SEQRES 14 A 496 GLU MET SER TRP ILE ALA ASP THR TYR ALA SER THR ILE
SEQRES 15 A 496 GLY HIS TYR ASP ILE ASN ALA HIS ALA CYS VAL THR GLY
SEQRES 16 A 496 LYS PRO ILE SER GLN GLY GLY ILE HIS GLY ARG ILE SER
SEQRES 17 A 496 ALA THR GLY ARG GLY VAL PHE HIS GLY ILE GLU ASN PHE
SEQRES 18 A 496 ILE ASN GLU ALA SER TYR MET SER ILE LEU GLY MET THR
SEQRES 19 A 496 PRO GLY PHE GLY ASP LYS THR PHE VAL VAL GLN GLY PHE
SEQRES 20 A 496 GLY ASN VAL GLY LEU HIS SER MET ARG TYR LEU HIS ARG
SEQRES 21 A 496 PHE GLY ALA LYS CYS ILE ALA VAL GLY GLU SER ASP GLY
SEQRES 22 A 496 SER ILE TRP ASN PRO ASP GLY ILE ASP PRO LYS GLU LEU
SEQRES 23 A 496 GLU ASP PHE LYS LEU GLN HIS GLY SER ILE LEU GLY PHE
SEQRES 24 A 496 PRO LYS ALA LYS PRO TYR GLU GLY SER ILE LEU GLU ALA
SEQRES 25 A 496 ASP CYS ASP ILE LEU ILE PRO ALA ALA SER GLU LYS GLN
SEQRES 26 A 496 LEU THR LYS SER ASN ALA PRO ARG VAL LYS ALA LYS ILE
SEQRES 27 A 496 ILE ALA GLU GLY ALA ASN GLY PRO THR THR PRO GLU ALA
SEQRES 28 A 496 ASP LYS ILE PHE LEU GLU ARG ASN ILE MET VAL ILE PRO
SEQRES 29 A 496 ASP LEU TYR LEU ASN ALA GLY GLY VAL THR VAL SER TYR
SEQRES 30 A 496 PHE GLU TRP LEU LYS ASN LEU ASN HIS VAL SER TYR GLY
SEQRES 31 A 496 ARG LEU THR PHE LYS TYR GLU ARG ASP SER ASN TYR HIS
SEQRES 32 A 496 LEU LEU MET SER VAL GLN GLU SER LEU GLU ARG LYS PHE
SEQRES 33 A 496 GLY LYS HIS GLY GLY THR ILE PRO ILE VAL PRO THR ALA
SEQRES 34 A 496 GLU PHE GLN ASP ARG ILE SER GLY ALA SER GLU LYS ASP
SEQRES 35 A 496 ILE VAL HIS SER GLY LEU ALA TYR THR MET GLU ALA SER
SEQRES 36 A 496 ALA ARG GLN ILE MET ARG THR ALA MET LYS TYR ASN LEU
SEQRES 37 A 496 GLY LEU ASP LEU ARG THR ALA ALA TYR VAL ASN ALA ILE
SEQRES 38 A 496 GLU LYS VAL PHE LYS VAL TYR ASN GLU ALA GLY VAL THR
SEQRES 39 A 496 PHE THR
SEQRES 1 B 496 ASP PRO ASN PHE PHE LYS MET VAL GLU GLY PHE PHE ASP
SEQRES 2 B 496 ARG GLY ALA SER ILE VAL GLU ASP LYS LEU VAL GLU ASP
SEQRES 3 B 496 LEU ARG THR ARG GLU SER GLU GLU GLN LYS ARG ASN ARG
SEQRES 4 B 496 VAL ARG GLY ILE LEU ARG ILE ILE LYS PRO CYS ASN HIS
SEQRES 5 B 496 VAL LEU SER LEU SER PHE PRO ILE ARG ARG ASP ASP GLY
SEQRES 6 B 496 SER TRP GLU VAL ILE GLU GLY TYR ARG ALA GLN HIS SER
SEQRES 7 B 496 GLN HIS ARG THR PRO CYS LYS GLY GLY ILE ARG TYR SER
SEQRES 8 B 496 THR ASP VAL SER VAL ASP GLU VAL LYS ALA LEU ALA SER
SEQRES 9 B 496 LEU MET THR TYR LYS CYS ALA VAL VAL ASP VAL PRO PHE
SEQRES 10 B 496 GLY GLY ALA LYS ALA GLY VAL LYS ILE ASN PRO LYS ASN
SEQRES 11 B 496 TYR THR ASP ASN GLU LEU GLU LYS ILE THR ARG ARG PHE
SEQRES 12 B 496 THR MET GLU LEU ALA LYS LYS GLY PHE ILE GLY PRO GLY
SEQRES 13 B 496 ILE ASP VAL PRO ALA PRO ASP MET SER THR GLY GLU ARG
SEQRES 14 B 496 GLU MET SER TRP ILE ALA ASP THR TYR ALA SER THR ILE
SEQRES 15 B 496 GLY HIS TYR ASP ILE ASN ALA HIS ALA CYS VAL THR GLY
SEQRES 16 B 496 LYS PRO ILE SER GLN GLY GLY ILE HIS GLY ARG ILE SER
SEQRES 17 B 496 ALA THR GLY ARG GLY VAL PHE HIS GLY ILE GLU ASN PHE
SEQRES 18 B 496 ILE ASN GLU ALA SER TYR MET SER ILE LEU GLY MET THR
SEQRES 19 B 496 PRO GLY PHE GLY ASP LYS THR PHE VAL VAL GLN GLY PHE
SEQRES 20 B 496 GLY ASN VAL GLY LEU HIS SER MET ARG TYR LEU HIS ARG
SEQRES 21 B 496 PHE GLY ALA LYS CYS ILE ALA VAL GLY GLU SER ASP GLY
SEQRES 22 B 496 SER ILE TRP ASN PRO ASP GLY ILE ASP PRO LYS GLU LEU
SEQRES 23 B 496 GLU ASP PHE LYS LEU GLN HIS GLY SER ILE LEU GLY PHE
SEQRES 24 B 496 PRO LYS ALA LYS PRO TYR GLU GLY SER ILE LEU GLU ALA
SEQRES 25 B 496 ASP CYS ASP ILE LEU ILE PRO ALA ALA SER GLU LYS GLN
SEQRES 26 B 496 LEU THR LYS SER ASN ALA PRO ARG VAL LYS ALA LYS ILE
SEQRES 27 B 496 ILE ALA GLU GLY ALA ASN GLY PRO THR THR PRO GLU ALA
SEQRES 28 B 496 ASP LYS ILE PHE LEU GLU ARG ASN ILE MET VAL ILE PRO
SEQRES 29 B 496 ASP LEU TYR LEU ASN ALA GLY GLY VAL THR VAL SER TYR
SEQRES 30 B 496 PHE GLU TRP LEU LYS ASN LEU ASN HIS VAL SER TYR GLY
SEQRES 31 B 496 ARG LEU THR PHE LYS TYR GLU ARG ASP SER ASN TYR HIS
SEQRES 32 B 496 LEU LEU MET SER VAL GLN GLU SER LEU GLU ARG LYS PHE
SEQRES 33 B 496 GLY LYS HIS GLY GLY THR ILE PRO ILE VAL PRO THR ALA
SEQRES 34 B 496 GLU PHE GLN ASP ARG ILE SER GLY ALA SER GLU LYS ASP
SEQRES 35 B 496 ILE VAL HIS SER GLY LEU ALA TYR THR MET GLU ALA SER
SEQRES 36 B 496 ALA ARG GLN ILE MET ARG THR ALA MET LYS TYR ASN LEU
SEQRES 37 B 496 GLY LEU ASP LEU ARG THR ALA ALA TYR VAL ASN ALA ILE
SEQRES 38 B 496 GLU LYS VAL PHE LYS VAL TYR ASN GLU ALA GLY VAL THR
SEQRES 39 B 496 PHE THR
SEQRES 1 C 496 ASP PRO ASN PHE PHE LYS MET VAL GLU GLY PHE PHE ASP
SEQRES 2 C 496 ARG GLY ALA SER ILE VAL GLU ASP LYS LEU VAL GLU ASP
SEQRES 3 C 496 LEU ARG THR ARG GLU SER GLU GLU GLN LYS ARG ASN ARG
SEQRES 4 C 496 VAL ARG GLY ILE LEU ARG ILE ILE LYS PRO CYS ASN HIS
SEQRES 5 C 496 VAL LEU SER LEU SER PHE PRO ILE ARG ARG ASP ASP GLY
SEQRES 6 C 496 SER TRP GLU VAL ILE GLU GLY TYR ARG ALA GLN HIS SER
SEQRES 7 C 496 GLN HIS ARG THR PRO CYS LYS GLY GLY ILE ARG TYR SER
SEQRES 8 C 496 THR ASP VAL SER VAL ASP GLU VAL LYS ALA LEU ALA SER
SEQRES 9 C 496 LEU MET THR TYR LYS CYS ALA VAL VAL ASP VAL PRO PHE
SEQRES 10 C 496 GLY GLY ALA LYS ALA GLY VAL LYS ILE ASN PRO LYS ASN
SEQRES 11 C 496 TYR THR ASP ASN GLU LEU GLU LYS ILE THR ARG ARG PHE
SEQRES 12 C 496 THR MET GLU LEU ALA LYS LYS GLY PHE ILE GLY PRO GLY
SEQRES 13 C 496 ILE ASP VAL PRO ALA PRO ASP MET SER THR GLY GLU ARG
SEQRES 14 C 496 GLU MET SER TRP ILE ALA ASP THR TYR ALA SER THR ILE
SEQRES 15 C 496 GLY HIS TYR ASP ILE ASN ALA HIS ALA CYS VAL THR GLY
SEQRES 16 C 496 LYS PRO ILE SER GLN GLY GLY ILE HIS GLY ARG ILE SER
SEQRES 17 C 496 ALA THR GLY ARG GLY VAL PHE HIS GLY ILE GLU ASN PHE
SEQRES 18 C 496 ILE ASN GLU ALA SER TYR MET SER ILE LEU GLY MET THR
SEQRES 19 C 496 PRO GLY PHE GLY ASP LYS THR PHE VAL VAL GLN GLY PHE
SEQRES 20 C 496 GLY ASN VAL GLY LEU HIS SER MET ARG TYR LEU HIS ARG
SEQRES 21 C 496 PHE GLY ALA LYS CYS ILE ALA VAL GLY GLU SER ASP GLY
SEQRES 22 C 496 SER ILE TRP ASN PRO ASP GLY ILE ASP PRO LYS GLU LEU
SEQRES 23 C 496 GLU ASP PHE LYS LEU GLN HIS GLY SER ILE LEU GLY PHE
SEQRES 24 C 496 PRO LYS ALA LYS PRO TYR GLU GLY SER ILE LEU GLU ALA
SEQRES 25 C 496 ASP CYS ASP ILE LEU ILE PRO ALA ALA SER GLU LYS GLN
SEQRES 26 C 496 LEU THR LYS SER ASN ALA PRO ARG VAL LYS ALA LYS ILE
SEQRES 27 C 496 ILE ALA GLU GLY ALA ASN GLY PRO THR THR PRO GLU ALA
SEQRES 28 C 496 ASP LYS ILE PHE LEU GLU ARG ASN ILE MET VAL ILE PRO
SEQRES 29 C 496 ASP LEU TYR LEU ASN ALA GLY GLY VAL THR VAL SER TYR
SEQRES 30 C 496 PHE GLU TRP LEU LYS ASN LEU ASN HIS VAL SER TYR GLY
SEQRES 31 C 496 ARG LEU THR PHE LYS TYR GLU ARG ASP SER ASN TYR HIS
SEQRES 32 C 496 LEU LEU MET SER VAL GLN GLU SER LEU GLU ARG LYS PHE
SEQRES 33 C 496 GLY LYS HIS GLY GLY THR ILE PRO ILE VAL PRO THR ALA
SEQRES 34 C 496 GLU PHE GLN ASP ARG ILE SER GLY ALA SER GLU LYS ASP
SEQRES 35 C 496 ILE VAL HIS SER GLY LEU ALA TYR THR MET GLU ALA SER
SEQRES 36 C 496 ALA ARG GLN ILE MET ARG THR ALA MET LYS TYR ASN LEU
SEQRES 37 C 496 GLY LEU ASP LEU ARG THR ALA ALA TYR VAL ASN ALA ILE
SEQRES 38 C 496 GLU LYS VAL PHE LYS VAL TYR ASN GLU ALA GLY VAL THR
SEQRES 39 C 496 PHE THR
SEQRES 1 D 496 ASP PRO ASN PHE PHE LYS MET VAL GLU GLY PHE PHE ASP
SEQRES 2 D 496 ARG GLY ALA SER ILE VAL GLU ASP LYS LEU VAL GLU ASP
SEQRES 3 D 496 LEU ARG THR ARG GLU SER GLU GLU GLN LYS ARG ASN ARG
SEQRES 4 D 496 VAL ARG GLY ILE LEU ARG ILE ILE LYS PRO CYS ASN HIS
SEQRES 5 D 496 VAL LEU SER LEU SER PHE PRO ILE ARG ARG ASP ASP GLY
SEQRES 6 D 496 SER TRP GLU VAL ILE GLU GLY TYR ARG ALA GLN HIS SER
SEQRES 7 D 496 GLN HIS ARG THR PRO CYS LYS GLY GLY ILE ARG TYR SER
SEQRES 8 D 496 THR ASP VAL SER VAL ASP GLU VAL LYS ALA LEU ALA SER
SEQRES 9 D 496 LEU MET THR TYR LYS CYS ALA VAL VAL ASP VAL PRO PHE
SEQRES 10 D 496 GLY GLY ALA LYS ALA GLY VAL LYS ILE ASN PRO LYS ASN
SEQRES 11 D 496 TYR THR ASP ASN GLU LEU GLU LYS ILE THR ARG ARG PHE
SEQRES 12 D 496 THR MET GLU LEU ALA LYS LYS GLY PHE ILE GLY PRO GLY
SEQRES 13 D 496 ILE ASP VAL PRO ALA PRO ASP MET SER THR GLY GLU ARG
SEQRES 14 D 496 GLU MET SER TRP ILE ALA ASP THR TYR ALA SER THR ILE
SEQRES 15 D 496 GLY HIS TYR ASP ILE ASN ALA HIS ALA CYS VAL THR GLY
SEQRES 16 D 496 LYS PRO ILE SER GLN GLY GLY ILE HIS GLY ARG ILE SER
SEQRES 17 D 496 ALA THR GLY ARG GLY VAL PHE HIS GLY ILE GLU ASN PHE
SEQRES 18 D 496 ILE ASN GLU ALA SER TYR MET SER ILE LEU GLY MET THR
SEQRES 19 D 496 PRO GLY PHE GLY ASP LYS THR PHE VAL VAL GLN GLY PHE
SEQRES 20 D 496 GLY ASN VAL GLY LEU HIS SER MET ARG TYR LEU HIS ARG
SEQRES 21 D 496 PHE GLY ALA LYS CYS ILE ALA VAL GLY GLU SER ASP GLY
SEQRES 22 D 496 SER ILE TRP ASN PRO ASP GLY ILE ASP PRO LYS GLU LEU
SEQRES 23 D 496 GLU ASP PHE LYS LEU GLN HIS GLY SER ILE LEU GLY PHE
SEQRES 24 D 496 PRO LYS ALA LYS PRO TYR GLU GLY SER ILE LEU GLU ALA
SEQRES 25 D 496 ASP CYS ASP ILE LEU ILE PRO ALA ALA SER GLU LYS GLN
SEQRES 26 D 496 LEU THR LYS SER ASN ALA PRO ARG VAL LYS ALA LYS ILE
SEQRES 27 D 496 ILE ALA GLU GLY ALA ASN GLY PRO THR THR PRO GLU ALA
SEQRES 28 D 496 ASP LYS ILE PHE LEU GLU ARG ASN ILE MET VAL ILE PRO
SEQRES 29 D 496 ASP LEU TYR LEU ASN ALA GLY GLY VAL THR VAL SER TYR
SEQRES 30 D 496 PHE GLU TRP LEU LYS ASN LEU ASN HIS VAL SER TYR GLY
SEQRES 31 D 496 ARG LEU THR PHE LYS TYR GLU ARG ASP SER ASN TYR HIS
SEQRES 32 D 496 LEU LEU MET SER VAL GLN GLU SER LEU GLU ARG LYS PHE
SEQRES 33 D 496 GLY LYS HIS GLY GLY THR ILE PRO ILE VAL PRO THR ALA
SEQRES 34 D 496 GLU PHE GLN ASP ARG ILE SER GLY ALA SER GLU LYS ASP
SEQRES 35 D 496 ILE VAL HIS SER GLY LEU ALA TYR THR MET GLU ALA SER
SEQRES 36 D 496 ALA ARG GLN ILE MET ARG THR ALA MET LYS TYR ASN LEU
SEQRES 37 D 496 GLY LEU ASP LEU ARG THR ALA ALA TYR VAL ASN ALA ILE
SEQRES 38 D 496 GLU LYS VAL PHE LYS VAL TYR ASN GLU ALA GLY VAL THR
SEQRES 39 D 496 PHE THR
SEQRES 1 E 496 ASP PRO ASN PHE PHE LYS MET VAL GLU GLY PHE PHE ASP
SEQRES 2 E 496 ARG GLY ALA SER ILE VAL GLU ASP LYS LEU VAL GLU ASP
SEQRES 3 E 496 LEU ARG THR ARG GLU SER GLU GLU GLN LYS ARG ASN ARG
SEQRES 4 E 496 VAL ARG GLY ILE LEU ARG ILE ILE LYS PRO CYS ASN HIS
SEQRES 5 E 496 VAL LEU SER LEU SER PHE PRO ILE ARG ARG ASP ASP GLY
SEQRES 6 E 496 SER TRP GLU VAL ILE GLU GLY TYR ARG ALA GLN HIS SER
SEQRES 7 E 496 GLN HIS ARG THR PRO CYS LYS GLY GLY ILE ARG TYR SER
SEQRES 8 E 496 THR ASP VAL SER VAL ASP GLU VAL LYS ALA LEU ALA SER
SEQRES 9 E 496 LEU MET THR TYR LYS CYS ALA VAL VAL ASP VAL PRO PHE
SEQRES 10 E 496 GLY GLY ALA LYS ALA GLY VAL LYS ILE ASN PRO LYS ASN
SEQRES 11 E 496 TYR THR ASP ASN GLU LEU GLU LYS ILE THR ARG ARG PHE
SEQRES 12 E 496 THR MET GLU LEU ALA LYS LYS GLY PHE ILE GLY PRO GLY
SEQRES 13 E 496 ILE ASP VAL PRO ALA PRO ASP MET SER THR GLY GLU ARG
SEQRES 14 E 496 GLU MET SER TRP ILE ALA ASP THR TYR ALA SER THR ILE
SEQRES 15 E 496 GLY HIS TYR ASP ILE ASN ALA HIS ALA CYS VAL THR GLY
SEQRES 16 E 496 LYS PRO ILE SER GLN GLY GLY ILE HIS GLY ARG ILE SER
SEQRES 17 E 496 ALA THR GLY ARG GLY VAL PHE HIS GLY ILE GLU ASN PHE
SEQRES 18 E 496 ILE ASN GLU ALA SER TYR MET SER ILE LEU GLY MET THR
SEQRES 19 E 496 PRO GLY PHE GLY ASP LYS THR PHE VAL VAL GLN GLY PHE
SEQRES 20 E 496 GLY ASN VAL GLY LEU HIS SER MET ARG TYR LEU HIS ARG
SEQRES 21 E 496 PHE GLY ALA LYS CYS ILE ALA VAL GLY GLU SER ASP GLY
SEQRES 22 E 496 SER ILE TRP ASN PRO ASP GLY ILE ASP PRO LYS GLU LEU
SEQRES 23 E 496 GLU ASP PHE LYS LEU GLN HIS GLY SER ILE LEU GLY PHE
SEQRES 24 E 496 PRO LYS ALA LYS PRO TYR GLU GLY SER ILE LEU GLU ALA
SEQRES 25 E 496 ASP CYS ASP ILE LEU ILE PRO ALA ALA SER GLU LYS GLN
SEQRES 26 E 496 LEU THR LYS SER ASN ALA PRO ARG VAL LYS ALA LYS ILE
SEQRES 27 E 496 ILE ALA GLU GLY ALA ASN GLY PRO THR THR PRO GLU ALA
SEQRES 28 E 496 ASP LYS ILE PHE LEU GLU ARG ASN ILE MET VAL ILE PRO
SEQRES 29 E 496 ASP LEU TYR LEU ASN ALA GLY GLY VAL THR VAL SER TYR
SEQRES 30 E 496 PHE GLU TRP LEU LYS ASN LEU ASN HIS VAL SER TYR GLY
SEQRES 31 E 496 ARG LEU THR PHE LYS TYR GLU ARG ASP SER ASN TYR HIS
SEQRES 32 E 496 LEU LEU MET SER VAL GLN GLU SER LEU GLU ARG LYS PHE
SEQRES 33 E 496 GLY LYS HIS GLY GLY THR ILE PRO ILE VAL PRO THR ALA
SEQRES 34 E 496 GLU PHE GLN ASP ARG ILE SER GLY ALA SER GLU LYS ASP
SEQRES 35 E 496 ILE VAL HIS SER GLY LEU ALA TYR THR MET GLU ALA SER
SEQRES 36 E 496 ALA ARG GLN ILE MET ARG THR ALA MET LYS TYR ASN LEU
SEQRES 37 E 496 GLY LEU ASP LEU ARG THR ALA ALA TYR VAL ASN ALA ILE
SEQRES 38 E 496 GLU LYS VAL PHE LYS VAL TYR ASN GLU ALA GLY VAL THR
SEQRES 39 E 496 PHE THR
SEQRES 1 F 496 ASP PRO ASN PHE PHE LYS MET VAL GLU GLY PHE PHE ASP
SEQRES 2 F 496 ARG GLY ALA SER ILE VAL GLU ASP LYS LEU VAL GLU ASP
SEQRES 3 F 496 LEU ARG THR ARG GLU SER GLU GLU GLN LYS ARG ASN ARG
SEQRES 4 F 496 VAL ARG GLY ILE LEU ARG ILE ILE LYS PRO CYS ASN HIS
SEQRES 5 F 496 VAL LEU SER LEU SER PHE PRO ILE ARG ARG ASP ASP GLY
SEQRES 6 F 496 SER TRP GLU VAL ILE GLU GLY TYR ARG ALA GLN HIS SER
SEQRES 7 F 496 GLN HIS ARG THR PRO CYS LYS GLY GLY ILE ARG TYR SER
SEQRES 8 F 496 THR ASP VAL SER VAL ASP GLU VAL LYS ALA LEU ALA SER
SEQRES 9 F 496 LEU MET THR TYR LYS CYS ALA VAL VAL ASP VAL PRO PHE
SEQRES 10 F 496 GLY GLY ALA LYS ALA GLY VAL LYS ILE ASN PRO LYS ASN
SEQRES 11 F 496 TYR THR ASP ASN GLU LEU GLU LYS ILE THR ARG ARG PHE
SEQRES 12 F 496 THR MET GLU LEU ALA LYS LYS GLY PHE ILE GLY PRO GLY
SEQRES 13 F 496 ILE ASP VAL PRO ALA PRO ASP MET SER THR GLY GLU ARG
SEQRES 14 F 496 GLU MET SER TRP ILE ALA ASP THR TYR ALA SER THR ILE
SEQRES 15 F 496 GLY HIS TYR ASP ILE ASN ALA HIS ALA CYS VAL THR GLY
SEQRES 16 F 496 LYS PRO ILE SER GLN GLY GLY ILE HIS GLY ARG ILE SER
SEQRES 17 F 496 ALA THR GLY ARG GLY VAL PHE HIS GLY ILE GLU ASN PHE
SEQRES 18 F 496 ILE ASN GLU ALA SER TYR MET SER ILE LEU GLY MET THR
SEQRES 19 F 496 PRO GLY PHE GLY ASP LYS THR PHE VAL VAL GLN GLY PHE
SEQRES 20 F 496 GLY ASN VAL GLY LEU HIS SER MET ARG TYR LEU HIS ARG
SEQRES 21 F 496 PHE GLY ALA LYS CYS ILE ALA VAL GLY GLU SER ASP GLY
SEQRES 22 F 496 SER ILE TRP ASN PRO ASP GLY ILE ASP PRO LYS GLU LEU
SEQRES 23 F 496 GLU ASP PHE LYS LEU GLN HIS GLY SER ILE LEU GLY PHE
SEQRES 24 F 496 PRO LYS ALA LYS PRO TYR GLU GLY SER ILE LEU GLU ALA
SEQRES 25 F 496 ASP CYS ASP ILE LEU ILE PRO ALA ALA SER GLU LYS GLN
SEQRES 26 F 496 LEU THR LYS SER ASN ALA PRO ARG VAL LYS ALA LYS ILE
SEQRES 27 F 496 ILE ALA GLU GLY ALA ASN GLY PRO THR THR PRO GLU ALA
SEQRES 28 F 496 ASP LYS ILE PHE LEU GLU ARG ASN ILE MET VAL ILE PRO
SEQRES 29 F 496 ASP LEU TYR LEU ASN ALA GLY GLY VAL THR VAL SER TYR
SEQRES 30 F 496 PHE GLU TRP LEU LYS ASN LEU ASN HIS VAL SER TYR GLY
SEQRES 31 F 496 ARG LEU THR PHE LYS TYR GLU ARG ASP SER ASN TYR HIS
SEQRES 32 F 496 LEU LEU MET SER VAL GLN GLU SER LEU GLU ARG LYS PHE
SEQRES 33 F 496 GLY LYS HIS GLY GLY THR ILE PRO ILE VAL PRO THR ALA
SEQRES 34 F 496 GLU PHE GLN ASP ARG ILE SER GLY ALA SER GLU LYS ASP
SEQRES 35 F 496 ILE VAL HIS SER GLY LEU ALA TYR THR MET GLU ALA SER
SEQRES 36 F 496 ALA ARG GLN ILE MET ARG THR ALA MET LYS TYR ASN LEU
SEQRES 37 F 496 GLY LEU ASP LEU ARG THR ALA ALA TYR VAL ASN ALA ILE
SEQRES 38 F 496 GLU LYS VAL PHE LYS VAL TYR ASN GLU ALA GLY VAL THR
SEQRES 39 F 496 PHE THR
HELIX 1 1 ASN A 12 THR A 38 1 27
HELIX 2 2 ARG A 39 LYS A 45 5 7
HELIX 3 3 ASN A 47 VAL A 49 5 3
HELIX 4 4 ARG A 50 LYS A 57 1 8
HELIX 5 5 SER A 104 VAL A 122 1 19
HELIX 6 6 ASN A 136 TYR A 140 5 5
HELIX 7 7 THR A 141 LYS A 158 1 18
HELIX 8 8 GLY A 176 THR A 190 1 15
HELIX 9 9 ILE A 191 TYR A 194 5 4
HELIX 10 10 ASN A 197 CYS A 201 5 5
HELIX 11 11 PRO A 206 GLY A 210 5 5
HELIX 12 12 GLY A 214 ASN A 232 1 19
HELIX 13 13 GLU A 233 SER A 238 1 6
HELIX 14 14 GLY A 257 PHE A 270 1 14
HELIX 15 15 ASP A 291 HIS A 302 1 12
HELIX 16 16 THR A 357 ARG A 367 1 11
HELIX 17 17 PRO A 373 ASN A 378 1 6
HELIX 18 18 ALA A 379 HIS A 395 1 17
HELIX 19 19 THR A 402 GLU A 422 1 21
HELIX 20 20 THR A 437 GLY A 446 1 10
HELIX 21 21 SER A 448 ASN A 476 1 29
HELIX 22 22 ASP A 480 GLU A 499 1 20
HELIX 23 23 ASN B 12 THR B 38 1 27
HELIX 24 24 ASN B 47 VAL B 49 5 3
HELIX 25 25 ARG B 50 LYS B 57 1 8
HELIX 26 26 VAL B 105 VAL B 122 1 18
HELIX 27 27 ASN B 136 TYR B 140 5 5
HELIX 28 28 THR B 141 LYS B 159 1 19
HELIX 29 29 GLY B 176 THR B 190 1 15
HELIX 30 30 ASN B 197 CYS B 201 5 5
HELIX 31 31 PRO B 206 GLY B 210 5 5
HELIX 32 32 SER B 217 ASN B 232 1 16
HELIX 33 33 GLU B 233 GLY B 241 1 9
HELIX 34 34 GLY B 257 PHE B 270 1 14
HELIX 35 35 ASP B 291 HIS B 302 1 12
HELIX 36 36 SER B 317 ALA B 321 5 5
HELIX 37 37 ASN B 339 VAL B 343 5 5
HELIX 38 38 THR B 357 ARG B 367 1 11
HELIX 39 39 PRO B 373 ASN B 378 1 6
HELIX 40 40 ALA B 379 HIS B 395 1 17
HELIX 41 41 THR B 402 GLU B 422 1 21
HELIX 42 42 THR B 437 ALA B 447 1 11
HELIX 43 43 SER B 448 TYR B 475 1 28
HELIX 44 44 ASP B 480 GLU B 499 1 20
HELIX 45 45 ASN C 12 GLU C 34 1 23
HELIX 46 46 ARG C 37 SER C 41 5 5
HELIX 47 47 ARG C 50 LYS C 57 1 8
HELIX 48 48 SER C 104 VAL C 122 1 19
HELIX 49 49 ASN C 136 TYR C 140 5 5
HELIX 50 50 THR C 141 LYS C 158 1 18
HELIX 51 51 GLY C 176 THR C 190 1 15
HELIX 52 52 ASN C 197 VAL C 202 5 6
HELIX 53 53 PRO C 206 GLY C 210 5 5
HELIX 54 54 GLY C 214 ASN C 232 1 19
HELIX 55 55 GLU C 233 LEU C 240 1 8
HELIX 56 56 GLY C 257 PHE C 270 1 14
HELIX 57 57 ASP C 291 HIS C 302 1 12
HELIX 58 58 SER C 317 ALA C 321 5 5
HELIX 59 59 ASN C 339 VAL C 343 5 5
HELIX 60 60 THR C 357 ARG C 367 1 11
HELIX 61 61 PRO C 373 ASN C 378 1 6
HELIX 62 62 ALA C 379 HIS C 395 1 17
HELIX 63 63 THR C 402 GLU C 422 1 21
HELIX 64 64 THR C 437 GLY C 446 1 10
HELIX 65 65 SER C 448 ASN C 476 1 29
HELIX 66 66 ASP C 480 GLU C 499 1 20
HELIX 67 67 ASN D 12 THR D 38 1 27
HELIX 68 68 ARG D 39 SER D 41 5 3
HELIX 69 69 ARG D 50 LYS D 57 1 8
HELIX 70 70 SER D 104 ALA D 120 1 17
HELIX 71 71 THR D 141 GLY D 160 1 20
HELIX 72 72 GLY D 176 THR D 190 1 15
HELIX 73 73 ASN D 197 VAL D 202 5 6
HELIX 74 74 SER D 217 ASN D 232 1 16
HELIX 75 75 GLY D 257 PHE D 270 1 14
HELIX 76 76 ASP D 291 GLN D 301 1 11
HELIX 77 77 ASN D 339 VAL D 343 5 5
HELIX 78 78 THR D 357 ARG D 367 1 11
HELIX 79 79 PRO D 373 ASN D 378 1 6
HELIX 80 80 GLY D 380 HIS D 395 1 16
HELIX 81 81 THR D 402 ARG D 423 1 22
HELIX 82 82 THR D 437 SER D 445 1 9
HELIX 83 83 GLU D 449 TYR D 475 1 27
HELIX 84 84 ASP D 480 GLU D 499 1 20
HELIX 85 85 ASN E 12 THR E 38 1 27
HELIX 86 86 ASN E 47 ARG E 50 5 4
HELIX 87 87 GLY E 51 LYS E 57 1 7
HELIX 88 88 SER E 104 VAL E 122 1 19
HELIX 89 89 THR E 141 LYS E 159 1 19
HELIX 90 90 GLY E 176 THR E 190 1 15
HELIX 91 91 ASN E 197 CYS E 201 5 5
HELIX 92 92 PRO E 206 GLY E 210 5 5
HELIX 93 93 GLY E 214 ASN E 232 1 19
HELIX 94 94 GLU E 233 LEU E 240 1 8
HELIX 95 95 GLY E 257 PHE E 270 1 14
HELIX 96 96 ASP E 291 HIS E 302 1 12
HELIX 97 97 SER E 317 ALA E 321 5 5
HELIX 98 98 ASN E 339 VAL E 343 5 5
HELIX 99 99 THR E 357 ARG E 367 1 11
HELIX 100 100 PRO E 373 ASN E 378 1 6
HELIX 101 101 ALA E 379 HIS E 395 1 17
HELIX 102 102 THR E 402 GLU E 422 1 21
HELIX 103 103 THR E 437 ALA E 447 1 11
HELIX 104 104 SER E 448 TYR E 475 1 28
HELIX 105 105 ASP E 480 GLU E 499 1 20
HELIX 106 106 ASN F 12 THR F 38 1 27
HELIX 107 107 ARG F 39 LYS F 45 5 7
HELIX 108 108 GLY F 51 LYS F 57 1 7
HELIX 109 109 SER F 104 VAL F 122 1 19
HELIX 110 110 ASN F 136 TYR F 140 5 5
HELIX 111 111 THR F 141 LYS F 159 1 19
HELIX 112 112 GLY F 176 SER F 189 1 14
HELIX 113 113 ASN F 197 VAL F 202 5 6
HELIX 114 114 PRO F 206 GLY F 210 5 5
HELIX 115 115 SER F 217 ASN F 232 1 16
HELIX 116 116 GLU F 233 ILE F 239 1 7
HELIX 117 117 GLY F 257 PHE F 270 1 14
HELIX 118 118 ASP F 291 HIS F 302 1 12
HELIX 119 119 SER F 317 ALA F 321 5 5
HELIX 120 120 ASN F 339 VAL F 343 5 5
HELIX 121 121 THR F 357 ARG F 367 1 11
HELIX 122 122 PRO F 373 ASN F 378 1 6
HELIX 123 123 ALA F 379 HIS F 395 1 17
HELIX 124 124 THR F 402 GLU F 422 1 21
HELIX 125 125 THR F 437 GLY F 446 1 10
HELIX 126 126 SER F 448 TYR F 475 1 28
HELIX 127 127 ASP F 480 GLU F 499 1 20
SHEET 1 A10 ASP A 167 ALA A 170 0
SHEET 2 A10 CYS A 93 ARG A 98 1 N CYS A 93 O VAL A 168
SHEET 3 A10 GLY A 127 GLY A 132 1 O GLY A 127 N LYS A 94
SHEET 4 A10 TRP A 76 GLN A 85 -1 N ALA A 84 O LYS A 130
SHEET 5 A10 HIS A 61 ARG A 70 -1 N LEU A 65 O GLY A 81
SHEET 6 A10 HIS E 61 LEU E 65 -1 O VAL E 62 N SER A 64
SHEET 7 A10 GLY E 81 GLN E 85 -1 O GLN E 85 N HIS E 61
SHEET 8 A10 GLY E 127 VAL E 133 -1 O LYS E 130 N ALA E 84
SHEET 9 A10 CYS E 93 TYR E 99 1 N ARG E 98 O ALA E 131
SHEET 10 A10 ASP E 167 ALA E 170 1 O VAL E 168 N CYS E 93
SHEET 1 B 5 LYS A 273 VAL A 277 0
SHEET 2 B 5 THR A 250 VAL A 253 1 N PHE A 251 O LYS A 273
SHEET 3 B 5 ILE A 325 ILE A 327 1 O ILE A 327 N VAL A 252
SHEET 4 B 5 ILE A 347 ALA A 349 1 O ILE A 347 N LEU A 326
SHEET 5 B 5 MET A 370 ILE A 372 1 O MET A 370 N ILE A 348
SHEET 1 C10 ASP D 167 ALA D 170 0
SHEET 2 C10 CYS D 93 ARG D 98 1 N CYS D 93 O VAL D 168
SHEET 3 C10 ALA D 129 GLY D 132 1 O ALA D 131 N ARG D 98
SHEET 4 C10 TRP D 76 GLN D 85 -1 N ALA D 84 O LYS D 130
SHEET 5 C10 HIS D 61 ARG D 70 -1 N PHE D 67 O ILE D 79
SHEET 6 C10 HIS B 61 ARG B 70 -1 N SER B 64 O VAL D 62
SHEET 7 C10 TRP B 76 GLN B 85 -1 O ILE B 79 N PHE B 67
SHEET 8 C10 GLY B 127 VAL B 133 -1 O LYS B 130 N ALA B 84
SHEET 9 C10 CYS B 93 LYS B 94 1 N LYS B 94 O GLY B 127
SHEET 10 C10 ASP B 167 VAL B 168 1 O VAL B 168 N CYS B 93
SHEET 1 D 9 ASP D 167 ALA D 170 0
SHEET 2 D 9 CYS D 93 ARG D 98 1 N CYS D 93 O VAL D 168
SHEET 3 D 9 ALA D 129 GLY D 132 1 O ALA D 131 N ARG D 98
SHEET 4 D 9 TRP D 76 GLN D 85 -1 N ALA D 84 O LYS D 130
SHEET 5 D 9 HIS D 61 ARG D 70 -1 N PHE D 67 O ILE D 79
SHEET 6 D 9 HIS B 61 ARG B 70 -1 N SER B 64 O VAL D 62
SHEET 7 D 9 TRP B 76 GLN B 85 -1 O ILE B 79 N PHE B 67
SHEET 8 D 9 GLY B 127 VAL B 133 -1 O LYS B 130 N ALA B 84
SHEET 9 D 9 ILE B 97 ARG B 98 1 N ARG B 98 O ALA B 131
SHEET 1 E 5 LYS B 273 GLY B 278 0
SHEET 2 E 5 THR B 250 GLN B 254 1 N PHE B 251 O LYS B 273
SHEET 3 E 5 ILE B 325 PRO B 328 1 O ILE B 327 N VAL B 252
SHEET 4 E 5 ILE B 347 ALA B 349 1 O ILE B 347 N LEU B 326
SHEET 5 E 5 MET B 370 ILE B 372 1 O ILE B 372 N ILE B 348
SHEET 1 F10 ASP C 167 ALA C 170 0
SHEET 2 F10 CYS C 93 ARG C 98 1 N CYS C 93 O VAL C 168
SHEET 3 F10 GLY C 127 VAL C 133 1 O ALA C 131 N ARG C 98
SHEET 4 F10 TRP C 76 GLN C 85 -1 N ALA C 84 O LYS C 130
SHEET 5 F10 HIS C 61 ARG C 70 -1 N LEU C 65 O GLY C 81
SHEET 6 F10 HIS F 61 ARG F 70 -1 O SER F 64 N VAL C 62
SHEET 7 F10 TRP F 76 GLN F 85 -1 O ILE F 79 N PHE F 67
SHEET 8 F10 GLY F 127 LYS F 134 -1 O LYS F 130 N ALA F 84
SHEET 9 F10 CYS F 93 LYS F 94 1 N LYS F 94 O GLY F 127
SHEET 10 F10 ASP F 167 VAL F 168 1 O VAL F 168 N CYS F 93
SHEET 1 G 9 ASP C 167 ALA C 170 0
SHEET 2 G 9 CYS C 93 ARG C 98 1 N CYS C 93 O VAL C 168
SHEET 3 G 9 GLY C 127 VAL C 133 1 O ALA C 131 N ARG C 98
SHEET 4 G 9 TRP C 76 GLN C 85 -1 N ALA C 84 O LYS C 130
SHEET 5 G 9 HIS C 61 ARG C 70 -1 N LEU C 65 O GLY C 81
SHEET 6 G 9 HIS F 61 ARG F 70 -1 O SER F 64 N VAL C 62
SHEET 7 G 9 TRP F 76 GLN F 85 -1 O ILE F 79 N PHE F 67
SHEET 8 G 9 GLY F 127 LYS F 134 -1 O LYS F 130 N ALA F 84
SHEET 9 G 9 ILE F 97 SER F 100 1 N ARG F 98 O ALA F 131
SHEET 1 H 5 LYS C 273 GLY C 278 0
SHEET 2 H 5 THR C 250 GLN C 254 1 N PHE C 251 O LYS C 273
SHEET 3 H 5 ILE C 325 PRO C 328 1 O ILE C 327 N VAL C 252
SHEET 4 H 5 ILE C 347 ALA C 349 1 O ALA C 349 N LEU C 326
SHEET 5 H 5 MET C 370 ILE C 372 1 O MET C 370 N ILE C 348
SHEET 1 I 5 LYS D 273 VAL D 277 0
SHEET 2 I 5 THR D 250 GLN D 254 1 N PHE D 251 O LYS D 273
SHEET 3 I 5 ILE D 325 PRO D 328 1 O ILE D 327 N VAL D 252
SHEET 4 I 5 ILE D 347 ALA D 349 1 O ILE D 347 N LEU D 326
SHEET 5 I 5 MET D 370 ILE D 372 1 O ILE D 372 N ILE D 348
SHEET 1 J 2 PHE E 67 ILE E 69 0
SHEET 2 J 2 GLU E 77 ILE E 79 -1 O ILE E 79 N PHE E 67
SHEET 1 K 5 LYS E 273 GLY E 278 0
SHEET 2 K 5 THR E 250 GLN E 254 1 N PHE E 251 O ILE E 275
SHEET 3 K 5 ILE E 325 PRO E 328 1 O ILE E 325 N VAL E 252
SHEET 4 K 5 ILE E 347 ALA E 349 1 O ALA E 349 N LEU E 326
SHEET 5 K 5 MET E 370 ILE E 372 1 O MET E 370 N ILE E 348
SHEET 1 L 5 LYS F 273 GLY F 278 0
SHEET 2 L 5 THR F 250 GLN F 254 1 N PHE F 251 O LYS F 273
SHEET 3 L 5 ILE F 325 PRO F 328 1 O ILE F 327 N VAL F 252
SHEET 4 L 5 ILE F 347 ALA F 349 1 O ILE F 347 N LEU F 326
SHEET 5 L 5 MET F 370 ILE F 372 1 O ILE F 372 N ILE F 348
CRYST1 96.920 98.640 124.260 86.48 69.69 60.87 P 1 6
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 0.010318 -0.005750 -0.004614 0.00000
SCALE2 0.000000 0.011606 0.001537 0.00000
SCALE3 0.000000 0.000000 0.008656 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
