HEADER OXIDOREDUCTASE 04-APR-16 5J5Z
TITLE CRYSTAL STRUCTURE OF THE D444V DISEASE-CAUSING MUTANT OF THE HUMAN
TITLE 2 DIHYDROLIPOAMIDE DEHYDROGENASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DIHYDROLIPOYL DEHYDROGENASE, MITOCHONDRIAL;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: DIHYDROLIPOAMIDE DEHYDROGENASE,GLYCINE CLEAVAGE SYSTEM L
COMPND 5 PROTEIN;
COMPND 6 EC: 1.8.1.4;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: DLD, GCSL, LAD, PHE3;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET52B+
KEYWDS DIHYDROLIPOAMIDE DEHYDROGENASE, E3 SUBUNIT, DISEASE-CAUSING MUTANT,
KEYWDS 2 E3 DEFICIENCY, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR E.SZABO,R.MIZSEI,Z.ZAMBO,B.TOROCSIK,M.S.WEISS,V.ADAM-VIZI,A.AMBRUS
REVDAT 5 10-JAN-24 5J5Z 1 JRNL
REVDAT 4 11-JUL-18 5J5Z 1 JRNL
REVDAT 3 04-JUL-18 5J5Z 1 JRNL
REVDAT 2 28-MAR-18 5J5Z 1 SOURCE
REVDAT 1 15-NOV-17 5J5Z 0
JRNL AUTH E.SZABO,R.MIZSEI,P.WILK,Z.ZAMBO,B.TOROCSIK,M.S.WEISS,
JRNL AUTH 2 V.ADAM-VIZI,A.AMBRUS
JRNL TITL CRYSTAL STRUCTURES OF THE DISEASE-CAUSING D444V MUTANT AND
JRNL TITL 2 THE RELEVANT WILD TYPE HUMAN DIHYDROLIPOAMIDE DEHYDROGENASE.
JRNL REF FREE RADIC. BIOL. MED. V. 124 214 2018
JRNL REFN ESSN 1873-4596
JRNL PMID 29908278
JRNL DOI 10.1016/J.FREERADBIOMED.2018.06.008
REMARK 2
REMARK 2 RESOLUTION. 1.84 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0131
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.84
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 48.38
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.1
REMARK 3 NUMBER OF REFLECTIONS : 103058
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 + TEST SET) : 0.182
REMARK 3 R VALUE (WORKING SET) : 0.181
REMARK 3 FREE R VALUE : 0.226
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 2.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2101
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) : 1.84
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.89
REMARK 3 REFLECTION IN BIN (WORKING SET) : 7390
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 96.49
REMARK 3 BIN R VALUE (WORKING SET) : 0.4010
REMARK 3 BIN FREE R VALUE SET COUNT : 151
REMARK 3 BIN FREE R VALUE : 0.3950
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 7123
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 134
REMARK 3 SOLVENT ATOMS : 495
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 36.45
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 39.36
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.71000
REMARK 3 B22 (A**2) : -0.42000
REMARK 3 B33 (A**2) : 1.12000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.112
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.116
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.126
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 9.562
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.973
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.952
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 7483 ; 0.027 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 7295 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 10139 ; 2.427 ; 1.981
REMARK 3 BOND ANGLES OTHERS (DEGREES): 16840 ; 1.184 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 980 ; 6.661 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 281 ;40.234 ;25.160
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1288 ;15.353 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 27 ;14.945 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1165 ; 0.154 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 8447 ; 0.013 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 1570 ; 0.002 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 3878 ; 1.728 ; 1.972
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 3877 ; 1.722 ; 1.972
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 4857 ; 2.643 ; 2.947
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 2
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A -6 A 500
REMARK 3 ORIGIN FOR THE GROUP (A): 36.6333 4.0401 12.6204
REMARK 3 T TENSOR
REMARK 3 T11: 0.2888 T22: 0.0137
REMARK 3 T33: 0.2374 T12: 0.0004
REMARK 3 T13: 0.0360 T23: 0.0164
REMARK 3 L TENSOR
REMARK 3 L11: 0.3420 L22: 0.5379
REMARK 3 L33: 0.0554 L12: 0.1022
REMARK 3 L13: 0.1003 L23: -0.0680
REMARK 3 S TENSOR
REMARK 3 S11: -0.0048 S12: 0.0349 S13: 0.0327
REMARK 3 S21: -0.0131 S22: 0.0494 S23: 0.0883
REMARK 3 S31: 0.0000 S32: 0.0031 S33: -0.0446
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B -7 B 500
REMARK 3 ORIGIN FOR THE GROUP (A): 32.8678 -29.9974 24.9236
REMARK 3 T TENSOR
REMARK 3 T11: 0.2973 T22: 0.0096
REMARK 3 T33: 0.2665 T12: -0.0127
REMARK 3 T13: -0.0003 T23: 0.0125
REMARK 3 L TENSOR
REMARK 3 L11: 0.2821 L22: 0.5778
REMARK 3 L33: 0.0477 L12: 0.1298
REMARK 3 L13: -0.0083 L23: -0.1034
REMARK 3 S TENSOR
REMARK 3 S11: 0.0473 S12: 0.0044 S13: -0.0765
REMARK 3 S21: 0.1369 S22: 0.0425 S23: 0.0663
REMARK 3 S31: -0.0170 S32: -0.0054 S33: -0.0898
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS U VALUES : WITH TLS ADDED
REMARK 4
REMARK 4 5J5Z COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 05-APR-16.
REMARK 100 THE DEPOSITION ID IS D_1000218821.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 06-MAY-15
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.1
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : BESSY
REMARK 200 BEAMLINE : 14.1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.91841
REMARK 200 MONOCHROMATOR : SI-111 CRYSTAL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 105160
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.840
REMARK 200 RESOLUTION RANGE LOW (A) : 48.380
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.1
REMARK 200 DATA REDUNDANCY : 4.540
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 10.7800
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.84
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.95
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.4
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 : 0.870
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: 1ZMD
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 57.75
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.91
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: RESERVOIR SOLUTION: 1.6 M
REMARK 280 NAH2PO4/K2HPO4 BUFFER, PH 8.1 (K2HPO4 WAS TITRATED WITH NAH2PO4
REMARK 280 TO PH 8.1), VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293.15K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -X+1/2,Y+1/2,-Z
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 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 59.01750
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 84.46950
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 59.01750
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 84.46950
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 11700 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 36030 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -67.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 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 -21
REMARK 465 ALA A -20
REMARK 465 SER A -19
REMARK 465 TRP A -18
REMARK 465 SER A -17
REMARK 465 HIS A -16
REMARK 465 PRO A -15
REMARK 465 GLN A -14
REMARK 465 PHE A -13
REMARK 465 GLU A -12
REMARK 465 LYS A -11
REMARK 465 GLY A -10
REMARK 465 ALA A -9
REMARK 465 LEU A -8
REMARK 465 GLU A -7
REMARK 465 GLN A -3
REMARK 465 GLY A -2
REMARK 465 PRO A -1
REMARK 465 GLY A 0
REMARK 465 MET B -21
REMARK 465 ALA B -20
REMARK 465 SER B -19
REMARK 465 TRP B -18
REMARK 465 SER B -17
REMARK 465 HIS B -16
REMARK 465 PRO B -15
REMARK 465 GLN B -14
REMARK 465 PHE B -13
REMARK 465 GLU B -12
REMARK 465 LYS B -11
REMARK 465 GLY B -10
REMARK 465 ALA B -9
REMARK 465 LEU B -8
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 OE2 GLU B 334 OH TYR B 351 2.15
REMARK 500 O2 GOL A 505 O HOH A 601 2.16
REMARK 500 OE1 GLU A 437 O HOH A 602 2.16
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 VAL A 191 CB VAL A 191 CG1 -0.139
REMARK 500 GLU A 291 CD GLU A 291 OE1 0.114
REMARK 500 GLU A 291 CD GLU A 291 OE2 0.071
REMARK 500 PHE A 388 CG PHE A 388 CD2 0.097
REMARK 500 GLU A 437 CD GLU A 437 OE1 0.109
REMARK 500 SER A 456 CB SER A 456 OG 0.107
REMARK 500 GLU B 427 CD GLU B 427 OE2 0.073
REMARK 500 SER B 456 CB SER B 456 OG 0.129
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 ASP A 251 CB - CG - OD1 ANGL. DEV. = 7.9 DEGREES
REMARK 500 ARG A 299 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 ARG A 299 NE - CZ - NH2 ANGL. DEV. = -4.5 DEGREES
REMARK 500 ASP A 320 CB - CG - OD2 ANGL. DEV. = -6.2 DEGREES
REMARK 500 ARG A 460 NE - CZ - NH2 ANGL. DEV. = -3.6 DEGREES
REMARK 500 ARG B 199 NE - CZ - NH2 ANGL. DEV. = -4.1 DEGREES
REMARK 500 ASP B 255 CB - CG - OD1 ANGL. DEV. = 5.7 DEGREES
REMARK 500 ASP B 401 CB - CG - OD2 ANGL. DEV. = -7.1 DEGREES
REMARK 500 MET B 403 CG - SD - CE ANGL. DEV. = 10.9 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 ASP A 163 -75.89 -126.36
REMARK 500 ASP A 251 6.89 -67.19
REMARK 500 TYR A 359 31.10 -90.16
REMARK 500 ALA B 147 49.33 -143.32
REMARK 500 ASP B 163 -81.94 -118.89
REMARK 500 ALA B 186 44.35 -109.89
REMARK 500 LYS B 265 40.28 74.58
REMARK 500 TYR B 359 35.18 -89.89
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 FAD A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 A 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 505
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue FAD B 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 B 502
DBREF 5J5Z A 1 474 UNP P09622 DLDH_HUMAN 36 509
DBREF 5J5Z B 1 474 UNP P09622 DLDH_HUMAN 36 509
SEQADV 5J5Z MET A -21 UNP P09622 INITIATING METHIONINE
SEQADV 5J5Z ALA A -20 UNP P09622 EXPRESSION TAG
SEQADV 5J5Z SER A -19 UNP P09622 EXPRESSION TAG
SEQADV 5J5Z TRP A -18 UNP P09622 EXPRESSION TAG
SEQADV 5J5Z SER A -17 UNP P09622 EXPRESSION TAG
SEQADV 5J5Z HIS A -16 UNP P09622 EXPRESSION TAG
SEQADV 5J5Z PRO A -15 UNP P09622 EXPRESSION TAG
SEQADV 5J5Z GLN A -14 UNP P09622 EXPRESSION TAG
SEQADV 5J5Z PHE A -13 UNP P09622 EXPRESSION TAG
SEQADV 5J5Z GLU A -12 UNP P09622 EXPRESSION TAG
SEQADV 5J5Z LYS A -11 UNP P09622 EXPRESSION TAG
SEQADV 5J5Z GLY A -10 UNP P09622 EXPRESSION TAG
SEQADV 5J5Z ALA A -9 UNP P09622 EXPRESSION TAG
SEQADV 5J5Z LEU A -8 UNP P09622 EXPRESSION TAG
SEQADV 5J5Z GLU A -7 UNP P09622 EXPRESSION TAG
SEQADV 5J5Z VAL A -6 UNP P09622 EXPRESSION TAG
SEQADV 5J5Z LEU A -5 UNP P09622 EXPRESSION TAG
SEQADV 5J5Z PHE A -4 UNP P09622 EXPRESSION TAG
SEQADV 5J5Z GLN A -3 UNP P09622 EXPRESSION TAG
SEQADV 5J5Z GLY A -2 UNP P09622 EXPRESSION TAG
SEQADV 5J5Z PRO A -1 UNP P09622 EXPRESSION TAG
SEQADV 5J5Z GLY A 0 UNP P09622 EXPRESSION TAG
SEQADV 5J5Z VAL A 444 UNP P09622 ASP 479 ENGINEERED MUTATION
SEQADV 5J5Z MET B -21 UNP P09622 INITIATING METHIONINE
SEQADV 5J5Z ALA B -20 UNP P09622 EXPRESSION TAG
SEQADV 5J5Z SER B -19 UNP P09622 EXPRESSION TAG
SEQADV 5J5Z TRP B -18 UNP P09622 EXPRESSION TAG
SEQADV 5J5Z SER B -17 UNP P09622 EXPRESSION TAG
SEQADV 5J5Z HIS B -16 UNP P09622 EXPRESSION TAG
SEQADV 5J5Z PRO B -15 UNP P09622 EXPRESSION TAG
SEQADV 5J5Z GLN B -14 UNP P09622 EXPRESSION TAG
SEQADV 5J5Z PHE B -13 UNP P09622 EXPRESSION TAG
SEQADV 5J5Z GLU B -12 UNP P09622 EXPRESSION TAG
SEQADV 5J5Z LYS B -11 UNP P09622 EXPRESSION TAG
SEQADV 5J5Z GLY B -10 UNP P09622 EXPRESSION TAG
SEQADV 5J5Z ALA B -9 UNP P09622 EXPRESSION TAG
SEQADV 5J5Z LEU B -8 UNP P09622 EXPRESSION TAG
SEQADV 5J5Z GLU B -7 UNP P09622 EXPRESSION TAG
SEQADV 5J5Z VAL B -6 UNP P09622 EXPRESSION TAG
SEQADV 5J5Z LEU B -5 UNP P09622 EXPRESSION TAG
SEQADV 5J5Z PHE B -4 UNP P09622 EXPRESSION TAG
SEQADV 5J5Z GLN B -3 UNP P09622 EXPRESSION TAG
SEQADV 5J5Z GLY B -2 UNP P09622 EXPRESSION TAG
SEQADV 5J5Z PRO B -1 UNP P09622 EXPRESSION TAG
SEQADV 5J5Z GLY B 0 UNP P09622 EXPRESSION TAG
SEQADV 5J5Z VAL B 444 UNP P09622 ASP 479 ENGINEERED MUTATION
SEQRES 1 A 496 MET ALA SER TRP SER HIS PRO GLN PHE GLU LYS GLY ALA
SEQRES 2 A 496 LEU GLU VAL LEU PHE GLN GLY PRO GLY ALA ASP GLN PRO
SEQRES 3 A 496 ILE ASP ALA ASP VAL THR VAL ILE GLY SER GLY PRO GLY
SEQRES 4 A 496 GLY TYR VAL ALA ALA ILE LYS ALA ALA GLN LEU GLY PHE
SEQRES 5 A 496 LYS THR VAL CYS ILE GLU LYS ASN GLU THR LEU GLY GLY
SEQRES 6 A 496 THR CYS LEU ASN VAL GLY CYS ILE PRO SER LYS ALA LEU
SEQRES 7 A 496 LEU ASN ASN SER HIS TYR TYR HIS MET ALA HIS GLY LYS
SEQRES 8 A 496 ASP PHE ALA SER ARG GLY ILE GLU MET SER GLU VAL ARG
SEQRES 9 A 496 LEU ASN LEU ASP LYS MET MET GLU GLN LYS SER THR ALA
SEQRES 10 A 496 VAL LYS ALA LEU THR GLY GLY ILE ALA HIS LEU PHE LYS
SEQRES 11 A 496 GLN ASN LYS VAL VAL HIS VAL ASN GLY TYR GLY LYS ILE
SEQRES 12 A 496 THR GLY LYS ASN GLN VAL THR ALA THR LYS ALA ASP GLY
SEQRES 13 A 496 GLY THR GLN VAL ILE ASP THR LYS ASN ILE LEU ILE ALA
SEQRES 14 A 496 THR GLY SER GLU VAL THR PRO PHE PRO GLY ILE THR ILE
SEQRES 15 A 496 ASP GLU ASP THR ILE VAL SER SER THR GLY ALA LEU SER
SEQRES 16 A 496 LEU LYS LYS VAL PRO GLU LYS MET VAL VAL ILE GLY ALA
SEQRES 17 A 496 GLY VAL ILE GLY VAL GLU LEU GLY SER VAL TRP GLN ARG
SEQRES 18 A 496 LEU GLY ALA ASP VAL THR ALA VAL GLU PHE LEU GLY HIS
SEQRES 19 A 496 VAL GLY GLY VAL GLY ILE ASP MET GLU ILE SER LYS ASN
SEQRES 20 A 496 PHE GLN ARG ILE LEU GLN LYS GLN GLY PHE LYS PHE LYS
SEQRES 21 A 496 LEU ASN THR LYS VAL THR GLY ALA THR LYS LYS SER ASP
SEQRES 22 A 496 GLY LYS ILE ASP VAL SER ILE GLU ALA ALA SER GLY GLY
SEQRES 23 A 496 LYS ALA GLU VAL ILE THR CYS ASP VAL LEU LEU VAL CYS
SEQRES 24 A 496 ILE GLY ARG ARG PRO PHE THR LYS ASN LEU GLY LEU GLU
SEQRES 25 A 496 GLU LEU GLY ILE GLU LEU ASP PRO ARG GLY ARG ILE PRO
SEQRES 26 A 496 VAL ASN THR ARG PHE GLN THR LYS ILE PRO ASN ILE TYR
SEQRES 27 A 496 ALA ILE GLY ASP VAL VAL ALA GLY PRO MET LEU ALA HIS
SEQRES 28 A 496 LYS ALA GLU ASP GLU GLY ILE ILE CYS VAL GLU GLY MET
SEQRES 29 A 496 ALA GLY GLY ALA VAL HIS ILE ASP TYR ASN CYS VAL PRO
SEQRES 30 A 496 SER VAL ILE TYR THR HIS PRO GLU VAL ALA TRP VAL GLY
SEQRES 31 A 496 LYS SER GLU GLU GLN LEU LYS GLU GLU GLY ILE GLU TYR
SEQRES 32 A 496 LYS VAL GLY LYS PHE PRO PHE ALA ALA ASN SER ARG ALA
SEQRES 33 A 496 LYS THR ASN ALA ASP THR ASP GLY MET VAL LYS ILE LEU
SEQRES 34 A 496 GLY GLN LYS SER THR ASP ARG VAL LEU GLY ALA HIS ILE
SEQRES 35 A 496 LEU GLY PRO GLY ALA GLY GLU MET VAL ASN GLU ALA ALA
SEQRES 36 A 496 LEU ALA LEU GLU TYR GLY ALA SER CYS GLU VAL ILE ALA
SEQRES 37 A 496 ARG VAL CYS HIS ALA HIS PRO THR LEU SER GLU ALA PHE
SEQRES 38 A 496 ARG GLU ALA ASN LEU ALA ALA SER PHE GLY LYS SER ILE
SEQRES 39 A 496 ASN PHE
SEQRES 1 B 496 MET ALA SER TRP SER HIS PRO GLN PHE GLU LYS GLY ALA
SEQRES 2 B 496 LEU GLU VAL LEU PHE GLN GLY PRO GLY ALA ASP GLN PRO
SEQRES 3 B 496 ILE ASP ALA ASP VAL THR VAL ILE GLY SER GLY PRO GLY
SEQRES 4 B 496 GLY TYR VAL ALA ALA ILE LYS ALA ALA GLN LEU GLY PHE
SEQRES 5 B 496 LYS THR VAL CYS ILE GLU LYS ASN GLU THR LEU GLY GLY
SEQRES 6 B 496 THR CYS LEU ASN VAL GLY CYS ILE PRO SER LYS ALA LEU
SEQRES 7 B 496 LEU ASN ASN SER HIS TYR TYR HIS MET ALA HIS GLY LYS
SEQRES 8 B 496 ASP PHE ALA SER ARG GLY ILE GLU MET SER GLU VAL ARG
SEQRES 9 B 496 LEU ASN LEU ASP LYS MET MET GLU GLN LYS SER THR ALA
SEQRES 10 B 496 VAL LYS ALA LEU THR GLY GLY ILE ALA HIS LEU PHE LYS
SEQRES 11 B 496 GLN ASN LYS VAL VAL HIS VAL ASN GLY TYR GLY LYS ILE
SEQRES 12 B 496 THR GLY LYS ASN GLN VAL THR ALA THR LYS ALA ASP GLY
SEQRES 13 B 496 GLY THR GLN VAL ILE ASP THR LYS ASN ILE LEU ILE ALA
SEQRES 14 B 496 THR GLY SER GLU VAL THR PRO PHE PRO GLY ILE THR ILE
SEQRES 15 B 496 ASP GLU ASP THR ILE VAL SER SER THR GLY ALA LEU SER
SEQRES 16 B 496 LEU LYS LYS VAL PRO GLU LYS MET VAL VAL ILE GLY ALA
SEQRES 17 B 496 GLY VAL ILE GLY VAL GLU LEU GLY SER VAL TRP GLN ARG
SEQRES 18 B 496 LEU GLY ALA ASP VAL THR ALA VAL GLU PHE LEU GLY HIS
SEQRES 19 B 496 VAL GLY GLY VAL GLY ILE ASP MET GLU ILE SER LYS ASN
SEQRES 20 B 496 PHE GLN ARG ILE LEU GLN LYS GLN GLY PHE LYS PHE LYS
SEQRES 21 B 496 LEU ASN THR LYS VAL THR GLY ALA THR LYS LYS SER ASP
SEQRES 22 B 496 GLY LYS ILE ASP VAL SER ILE GLU ALA ALA SER GLY GLY
SEQRES 23 B 496 LYS ALA GLU VAL ILE THR CYS ASP VAL LEU LEU VAL CYS
SEQRES 24 B 496 ILE GLY ARG ARG PRO PHE THR LYS ASN LEU GLY LEU GLU
SEQRES 25 B 496 GLU LEU GLY ILE GLU LEU ASP PRO ARG GLY ARG ILE PRO
SEQRES 26 B 496 VAL ASN THR ARG PHE GLN THR LYS ILE PRO ASN ILE TYR
SEQRES 27 B 496 ALA ILE GLY ASP VAL VAL ALA GLY PRO MET LEU ALA HIS
SEQRES 28 B 496 LYS ALA GLU ASP GLU GLY ILE ILE CYS VAL GLU GLY MET
SEQRES 29 B 496 ALA GLY GLY ALA VAL HIS ILE ASP TYR ASN CYS VAL PRO
SEQRES 30 B 496 SER VAL ILE TYR THR HIS PRO GLU VAL ALA TRP VAL GLY
SEQRES 31 B 496 LYS SER GLU GLU GLN LEU LYS GLU GLU GLY ILE GLU TYR
SEQRES 32 B 496 LYS VAL GLY LYS PHE PRO PHE ALA ALA ASN SER ARG ALA
SEQRES 33 B 496 LYS THR ASN ALA ASP THR ASP GLY MET VAL LYS ILE LEU
SEQRES 34 B 496 GLY GLN LYS SER THR ASP ARG VAL LEU GLY ALA HIS ILE
SEQRES 35 B 496 LEU GLY PRO GLY ALA GLY GLU MET VAL ASN GLU ALA ALA
SEQRES 36 B 496 LEU ALA LEU GLU TYR GLY ALA SER CYS GLU VAL ILE ALA
SEQRES 37 B 496 ARG VAL CYS HIS ALA HIS PRO THR LEU SER GLU ALA PHE
SEQRES 38 B 496 ARG GLU ALA ASN LEU ALA ALA SER PHE GLY LYS SER ILE
SEQRES 39 B 496 ASN PHE
HET FAD A 501 53
HET PO4 A 502 5
HET GOL A 503 12
HET GOL A 504 6
HET GOL A 505 6
HET FAD B 501 53
HET PO4 B 502 5
HETNAM FAD FLAVIN-ADENINE DINUCLEOTIDE
HETNAM PO4 PHOSPHATE ION
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 3 FAD 2(C27 H33 N9 O15 P2)
FORMUL 4 PO4 2(O4 P 3-)
FORMUL 5 GOL 3(C3 H8 O3)
FORMUL 10 HOH *495(H2 O)
HELIX 1 AA1 GLY A 15 LEU A 28 1 14
HELIX 2 AA2 GLY A 42 GLY A 49 1 8
HELIX 3 AA3 GLY A 49 GLY A 68 1 20
HELIX 4 AA4 LYS A 69 ARG A 74 1 6
HELIX 5 AA5 ASN A 84 LYS A 111 1 28
HELIX 6 AA6 SER A 167 LEU A 172 1 6
HELIX 7 AA7 GLY A 187 GLY A 201 1 15
HELIX 8 AA8 ASP A 219 GLY A 234 1 16
HELIX 9 AA9 GLY A 288 GLY A 293 1 6
HELIX 10 AB1 GLY A 319 VAL A 322 5 4
HELIX 11 AB2 LEU A 327 ALA A 343 1 17
HELIX 12 AB3 ASP A 350 VAL A 354 5 5
HELIX 13 AB4 SER A 370 GLU A 377 1 8
HELIX 14 AB5 ASN A 391 ALA A 398 1 8
HELIX 15 AB6 GLY A 424 GLY A 439 1 16
HELIX 16 AB7 SER A 441 VAL A 448 1 8
HELIX 17 AB8 LEU A 455 GLY A 469 1 15
HELIX 18 AB9 GLY B 15 LEU B 28 1 14
HELIX 19 AC1 GLY B 42 GLY B 49 1 8
HELIX 20 AC2 GLY B 49 GLY B 68 1 20
HELIX 21 AC3 LYS B 69 ARG B 74 1 6
HELIX 22 AC4 ASN B 84 ASN B 110 1 27
HELIX 23 AC5 SER B 167 LEU B 172 1 6
HELIX 24 AC6 GLY B 187 LEU B 200 1 14
HELIX 25 AC7 ASP B 219 GLN B 233 1 15
HELIX 26 AC8 GLY B 288 GLY B 293 1 6
HELIX 27 AC9 GLY B 319 VAL B 322 5 4
HELIX 28 AD1 LEU B 327 ALA B 343 1 17
HELIX 29 AD2 ASP B 350 VAL B 354 5 5
HELIX 30 AD3 SER B 370 GLU B 377 1 8
HELIX 31 AD4 ASN B 391 ALA B 398 1 8
HELIX 32 AD5 GLY B 424 TYR B 438 1 15
HELIX 33 AD6 SER B 441 ARG B 447 1 7
HELIX 34 AD7 LEU B 455 GLY B 469 1 15
SHEET 1 AA1 6 VAL A 113 ASN A 116 0
SHEET 2 AA1 6 THR A 32 GLU A 36 1 N CYS A 34 O VAL A 113
SHEET 3 AA1 6 ILE A 5 ILE A 12 1 N VAL A 11 O VAL A 33
SHEET 4 AA1 6 THR A 136 ILE A 146 1 O LEU A 145 N THR A 10
SHEET 5 AA1 6 GLN A 126 THR A 130 -1 N ALA A 129 O GLN A 137
SHEET 6 AA1 6 TYR A 118 GLY A 123 -1 N TYR A 118 O THR A 130
SHEET 1 AA2 5 VAL A 113 ASN A 116 0
SHEET 2 AA2 5 THR A 32 GLU A 36 1 N CYS A 34 O VAL A 113
SHEET 3 AA2 5 ILE A 5 ILE A 12 1 N VAL A 11 O VAL A 33
SHEET 4 AA2 5 THR A 136 ILE A 146 1 O LEU A 145 N THR A 10
SHEET 5 AA2 5 ILE A 315 ALA A 317 1 O TYR A 316 N ILE A 146
SHEET 1 AA3 2 ILE A 76 MET A 78 0
SHEET 2 AA3 2 VAL B 81 LEU B 83 -1 O ARG B 82 N GLU A 77
SHEET 1 AA4 2 VAL A 81 LEU A 83 0
SHEET 2 AA4 2 ILE B 76 MET B 78 -1 O GLU B 77 N ARG A 82
SHEET 1 AA5 2 SER A 150 VAL A 152 0
SHEET 2 AA5 2 ARG A 280 PRO A 282 -1 O ARG A 281 N GLU A 151
SHEET 1 AA6 5 ILE A 165 VAL A 166 0
SHEET 2 AA6 5 VAL A 273 VAL A 276 1 O LEU A 274 N VAL A 166
SHEET 3 AA6 5 LYS A 180 ILE A 184 1 N ILE A 184 O LEU A 275
SHEET 4 AA6 5 ASP A 203 VAL A 207 1 O VAL A 207 N VAL A 183
SHEET 5 AA6 5 LYS A 236 LYS A 238 1 O LYS A 238 N ALA A 206
SHEET 1 AA7 3 THR A 241 LYS A 248 0
SHEET 2 AA7 3 ILE A 254 ALA A 260 -1 O SER A 257 N GLY A 245
SHEET 3 AA7 3 GLU A 267 CYS A 271 -1 O GLU A 267 N ILE A 258
SHEET 1 AA8 5 SER A 356 ILE A 358 0
SHEET 2 AA8 5 GLU A 363 GLY A 368 -1 O VAL A 364 N ILE A 358
SHEET 3 AA8 5 VAL A 415 GLY A 422 -1 O ILE A 420 N ALA A 365
SHEET 4 AA8 5 MET A 403 GLN A 409 -1 N LYS A 405 O HIS A 419
SHEET 5 AA8 5 TYR A 381 PRO A 387 -1 N GLY A 384 O ILE A 406
SHEET 1 AA9 7 PHE B -4 GLN B -3 0
SHEET 2 AA9 7 VAL B 113 ASN B 116 1 O HIS B 114 N GLN B -3
SHEET 3 AA9 7 THR B 32 GLU B 36 1 N CYS B 34 O VAL B 113
SHEET 4 AA9 7 ILE B 5 ILE B 12 1 N VAL B 11 O VAL B 33
SHEET 5 AA9 7 THR B 136 ILE B 146 1 O LEU B 145 N THR B 10
SHEET 6 AA9 7 GLN B 126 THR B 130 -1 N ALA B 129 O GLN B 137
SHEET 7 AA9 7 TYR B 118 GLY B 123 -1 N LYS B 120 O THR B 128
SHEET 1 AB1 6 PHE B -4 GLN B -3 0
SHEET 2 AB1 6 VAL B 113 ASN B 116 1 O HIS B 114 N GLN B -3
SHEET 3 AB1 6 THR B 32 GLU B 36 1 N CYS B 34 O VAL B 113
SHEET 4 AB1 6 ILE B 5 ILE B 12 1 N VAL B 11 O VAL B 33
SHEET 5 AB1 6 THR B 136 ILE B 146 1 O LEU B 145 N THR B 10
SHEET 6 AB1 6 ILE B 315 ALA B 317 1 O TYR B 316 N ILE B 144
SHEET 1 AB2 2 SER B 150 VAL B 152 0
SHEET 2 AB2 2 ARG B 280 PRO B 282 -1 O ARG B 281 N GLU B 151
SHEET 1 AB3 5 ILE B 165 VAL B 166 0
SHEET 2 AB3 5 VAL B 273 VAL B 276 1 O VAL B 276 N VAL B 166
SHEET 3 AB3 5 LYS B 180 ILE B 184 1 N VAL B 182 O LEU B 275
SHEET 4 AB3 5 ASP B 203 VAL B 207 1 O ASP B 203 N MET B 181
SHEET 5 AB3 5 LYS B 236 LYS B 238 1 O LYS B 238 N ALA B 206
SHEET 1 AB4 3 THR B 241 LYS B 248 0
SHEET 2 AB4 3 ILE B 254 ALA B 260 -1 O SER B 257 N GLY B 245
SHEET 3 AB4 3 GLU B 267 CYS B 271 -1 O ILE B 269 N VAL B 256
SHEET 1 AB5 5 SER B 356 ILE B 358 0
SHEET 2 AB5 5 GLU B 363 GLY B 368 -1 O VAL B 364 N ILE B 358
SHEET 3 AB5 5 VAL B 415 GLY B 422 -1 O ILE B 420 N ALA B 365
SHEET 4 AB5 5 MET B 403 GLN B 409 -1 N LEU B 407 O LEU B 416
SHEET 5 AB5 5 TYR B 381 PRO B 387 -1 N GLY B 384 O ILE B 406
SSBOND 1 CYS A 45 CYS A 50 1555 1555 2.29
SSBOND 2 CYS B 45 CYS B 50 1555 1555 2.29
CISPEP 1 HIS A 361 PRO A 362 0 -0.93
CISPEP 2 HIS A 452 PRO A 453 0 2.23
CISPEP 3 HIS B 361 PRO B 362 0 -4.62
CISPEP 4 HIS B 452 PRO B 453 0 -0.71
SITE 1 AC1 38 ILE A 12 GLY A 13 GLY A 15 PRO A 16
SITE 2 AC1 38 GLY A 17 GLU A 36 LYS A 37 ASN A 38
SITE 3 AC1 38 GLY A 43 THR A 44 CYS A 45 VAL A 48
SITE 4 AC1 38 GLY A 49 CYS A 50 LYS A 54 GLY A 117
SITE 5 AC1 38 TYR A 118 GLY A 119 ALA A 147 THR A 148
SITE 6 AC1 38 GLY A 149 SER A 150 ILE A 189 ARG A 280
SITE 7 AC1 38 PHE A 283 GLY A 319 ASP A 320 MET A 326
SITE 8 AC1 38 LEU A 327 ALA A 328 HIS A 329 TYR A 359
SITE 9 AC1 38 HOH A 649 HOH A 667 HOH A 668 HOH A 696
SITE 10 AC1 38 HOH A 788 HIS B 452
SITE 1 AC2 6 ARG A 299 ARG A 301 GLY A 324 GOL A 504
SITE 2 AC2 6 HOH A 622 HOH A 797
SITE 1 AC3 10 THR A 284 ASN A 286 LEU A 287 GLY A 288
SITE 2 AC3 10 LEU A 289 GLU A 290 GLU A 291 HOH A 616
SITE 3 AC3 10 HOH A 642 HOH A 769
SITE 1 AC4 8 ARG A 301 GLN A 409 SER A 411 PO4 A 502
SITE 2 AC4 8 HOH A 644 HOH A 658 HOH A 676 HOH A 845
SITE 1 AC5 9 ASP A 333 HIS A 348 ASP A 350 CYS A 353
SITE 2 AC5 9 GLU A 437 HOH A 601 HOH A 621 HOH A 624
SITE 3 AC5 9 ARG B 447
SITE 1 AC6 39 HIS A 452 ILE B 12 GLY B 13 GLY B 15
SITE 2 AC6 39 PRO B 16 GLY B 17 ILE B 35 GLU B 36
SITE 3 AC6 39 LYS B 37 ASN B 38 GLY B 43 THR B 44
SITE 4 AC6 39 CYS B 45 VAL B 48 GLY B 49 CYS B 50
SITE 5 AC6 39 LYS B 54 GLY B 117 TYR B 118 GLY B 119
SITE 6 AC6 39 ALA B 147 THR B 148 GLY B 149 SER B 150
SITE 7 AC6 39 ILE B 189 ARG B 280 PHE B 283 GLY B 319
SITE 8 AC6 39 ASP B 320 MET B 326 LEU B 327 ALA B 328
SITE 9 AC6 39 HIS B 329 TYR B 359 HOH B 605 HOH B 628
SITE 10 AC6 39 HOH B 655 HOH B 656 HOH B 721
SITE 1 AC7 4 ARG B 299 ARG B 301 ALA B 323 GLY B 324
CRYST1 118.035 168.939 61.279 90.00 90.00 90.00 P 21 21 2 8
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 0.008472 0.000000 0.000000 0.00000
SCALE2 0.000000 0.005919 0.000000 0.00000
SCALE3 0.000000 0.000000 0.016319 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
