HEADER OXIDOREDUCTASE 18-OCT-14 4V3F
TITLE CRYSTAL STRUCTURE OF BETAINE ALDEHYDE DEHYDROGENASE FROM SPINACH
TITLE 2 SHOWING A THIOHEMIACETAL WITH BETAINE ALDEHYDE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BETAINE ALDEHYDE DEHYDROGENASE, CHLOROPLASTIC;
COMPND 3 CHAIN: A, B, D;
COMPND 4 SYNONYM: BADH, BETAINE ALDEHYDE DEHYDROGENASE;
COMPND 5 EC: 1.2.1.8;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: BETAINE ALDEHYDE DEHYDROGENASE, CHLOROPLASTIC;
COMPND 9 CHAIN: C;
COMPND 10 SYNONYM: BADH, BETAINE ALDEHYDE DEHYDROGENASE;
COMPND 11 EC: 1.2.1.8;
COMPND 12 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SPINACIA OLERACEA;
SOURCE 3 ORGANISM_COMMON: SPINACH;
SOURCE 4 ORGANISM_TAXID: 3562;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR: PET28B;
SOURCE 10 MOL_ID: 2;
SOURCE 11 ORGANISM_SCIENTIFIC: SPINACIA OLERACEA;
SOURCE 12 ORGANISM_COMMON: SPINACH;
SOURCE 13 ORGANISM_TAXID: 3562;
SOURCE 14 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 15 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 16 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 17 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 18 EXPRESSION_SYSTEM_VECTOR: PET28B
KEYWDS OXIDOREDUCTASE, BETAINE ALDEHYDE DEHYDROGENASE, ALDH10.
EXPDTA X-RAY DIFFRACTION
AUTHOR A.ZARATE-ROMERO,R.A.MUNOZ-CLARES
REVDAT 6 10-JAN-24 4V3F 1 REMARK
REVDAT 5 30-OCT-19 4V3F 1 REMARK LINK
REVDAT 4 09-AUG-17 4V3F 1 REMARK
REVDAT 3 13-APR-16 4V3F 1 JRNL
REVDAT 2 03-FEB-16 4V3F 1 JRNL
REVDAT 1 20-JAN-16 4V3F 0
JRNL AUTH A.ZARATE-ROMERO,D.S.MURILLO-MELO,C.MUJICA-JIMENEZ,C.MONTIEL,
JRNL AUTH 2 R.A.MUNOZ-CLARES
JRNL TITL REVERSIBLE, PARTIAL INACTIVATION OF PLANT BETAINE ALDEHYDE
JRNL TITL 2 DEHYDROGENASE BY BETAINE ALDEHYDE: MECHANISM AND POSSIBLE
JRNL TITL 3 PHYSIOLOGICAL IMPLICATIONS.
JRNL REF BIOCHEM.J. V. 473 873 2016
JRNL REFN ISSN 0264-6021
JRNL PMID 26792760
JRNL DOI 10.1042/BJ20151084
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.8.4_1496)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 28.97
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.960
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.0
REMARK 3 NUMBER OF REFLECTIONS : 122084
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.197
REMARK 3 R VALUE (WORKING SET) : 0.196
REMARK 3 FREE R VALUE : 0.211
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT : 5965
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 28.9712 - 6.1890 0.96 3868 198 0.1604 0.1515
REMARK 3 2 6.1890 - 4.9202 0.99 3988 193 0.1621 0.1721
REMARK 3 3 4.9202 - 4.3005 0.99 3990 208 0.1345 0.1335
REMARK 3 4 4.3005 - 3.9084 0.99 3963 216 0.1517 0.1509
REMARK 3 5 3.9084 - 3.6288 0.99 3974 213 0.1609 0.1837
REMARK 3 6 3.6288 - 3.4152 0.99 3969 201 0.1749 0.1828
REMARK 3 7 3.4152 - 3.2444 0.98 3966 225 0.2002 0.2279
REMARK 3 8 3.2444 - 3.1033 0.98 3984 194 0.2084 0.2559
REMARK 3 9 3.1033 - 2.9840 0.98 3963 194 0.2141 0.2249
REMARK 3 10 2.9840 - 2.8811 0.98 3946 194 0.2175 0.2475
REMARK 3 11 2.8811 - 2.7911 0.98 3948 213 0.2228 0.2679
REMARK 3 12 2.7911 - 2.7114 0.98 3974 205 0.2162 0.2092
REMARK 3 13 2.7114 - 2.6401 0.98 3923 189 0.2183 0.2391
REMARK 3 14 2.6401 - 2.5757 0.98 3915 198 0.2201 0.2648
REMARK 3 15 2.5757 - 2.5172 0.97 3979 201 0.2180 0.2495
REMARK 3 16 2.5172 - 2.4636 0.97 3954 174 0.2263 0.2443
REMARK 3 17 2.4636 - 2.4144 0.97 3908 192 0.2289 0.2756
REMARK 3 18 2.4144 - 2.3688 0.97 3944 197 0.2392 0.2681
REMARK 3 19 2.3688 - 2.3265 0.97 3869 200 0.2348 0.2462
REMARK 3 20 2.3265 - 2.2871 0.97 3889 218 0.2315 0.2432
REMARK 3 21 2.2871 - 2.2502 0.97 3881 234 0.2354 0.2918
REMARK 3 22 2.2502 - 2.2156 0.97 3886 201 0.2364 0.2656
REMARK 3 23 2.2156 - 2.1831 0.96 3881 210 0.2422 0.2623
REMARK 3 24 2.1831 - 2.1523 0.95 3817 205 0.2397 0.2431
REMARK 3 25 2.1523 - 2.1232 0.95 3848 189 0.2461 0.2615
REMARK 3 26 2.1232 - 2.0957 0.94 3813 183 0.2629 0.2979
REMARK 3 27 2.0957 - 2.0695 0.93 3736 204 0.2746 0.2744
REMARK 3 28 2.0695 - 2.0446 0.91 3644 196 0.2758 0.3198
REMARK 3 29 2.0446 - 2.0208 0.90 3669 162 0.2885 0.3083
REMARK 3 30 2.0208 - 1.9981 0.75 3030 158 0.2822 0.2844
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.230
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 23.070
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.009 15951
REMARK 3 ANGLE : 1.259 21724
REMARK 3 CHIRALITY : 0.054 2434
REMARK 3 PLANARITY : 0.008 2795
REMARK 3 DIHEDRAL : 14.725 5824
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4V3F COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 18-OCT-14.
REMARK 100 THE DEPOSITION ID IS D_1290061999.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 13-MAR-14
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.2
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 19-BM
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9791
REMARK 200 MONOCHROMATOR : SI (1 1 1)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 122131
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 29.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.1
REMARK 200 DATA REDUNDANCY : 2.400
REMARK 200 R MERGE (I) : 0.04800
REMARK 200 R SYM (I) : 0.04800
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.11
REMARK 200 COMPLETENESS FOR SHELL (%) : 88.0
REMARK 200 DATA REDUNDANCY IN SHELL : 1.70
REMARK 200 R MERGE FOR SHELL (I) : 0.26800
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.300
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 4A0M
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 42.70
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.15
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: AMMONIUM IODIDE 0.2 M, POLY ETHYLENE
REMARK 280 GLYCOL 3350 20% (W/V), PH 6.2
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, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 10630 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 32310 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -28.8 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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 11050 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 32410 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -26.4 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D
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 1
REMARK 465 ALA A 2
REMARK 465 MET B 1
REMARK 465 ALA B 2
REMARK 465 PHE B 3
REMARK 465 MET C 1
REMARK 465 ALA C 2
REMARK 465 MET D 1
REMARK 465 ALA D 2
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 PRO A 497 CG CD
REMARK 470 PRO C 497 CG CD
REMARK 470 PRO D 497 CG CD
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 SER A 487 OD1 ASP A 488 1.54
REMARK 500 CD LYS B 336 CE1 TYR B 370 1.80
REMARK 500 OE2 GLU C 257 OD CSO C 291 1.96
REMARK 500 NE2 GLN D 121 O HOH D 2071 2.00
REMARK 500 OG SER C 403 O HOH C 2134 2.00
REMARK 500 OE2 GLU D 138 O HOH D 2076 2.01
REMARK 500 SG CYS B 291 O HOH B 2089 2.01
REMARK 500 OE2 GLU A 196 O HOH A 2010 2.02
REMARK 500 NH1 ARG B 146 O HOH B 2063 2.05
REMARK 500 NH2 ARG B 362 O GLY B 369 2.06
REMARK 500 O HOH B 2075 O HOH B 2131 2.07
REMARK 500 O LYS B 261 NH1 ARG B 296 2.09
REMARK 500 OE1 GLU C 268 OG SER C 302 2.10
REMARK 500 O ARG D 8 NH2 ARG D 24 2.11
REMARK 500 C ILE B 303 OE1 GLU B 306 2.11
REMARK 500 NE ARG C 24 OD2 ASP C 38 2.11
REMARK 500 NZ LYS C 81 O GLU C 200 2.13
REMARK 500 O ILE B 303 OE1 GLU B 306 2.14
REMARK 500 NZ LYS A 242 O HOH A 2115 2.15
REMARK 500 O SER C 496 O HOH C 2163 2.16
REMARK 500 O HOH B 2113 O HOH B 2118 2.18
REMARK 500 NH2 ARG C 362 O GLY C 369 2.18
REMARK 500 NH2 ARG A 296 O LEU A 410 2.18
REMARK 500 OD CSO C 450 O HOH C 2142 2.18
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 LEU C 256 CA - C - N ANGL. DEV. = 15.4 DEGREES
REMARK 500 LEU C 256 O - C - N ANGL. DEV. = -17.8 DEGREES
REMARK 500 PRO C 449 C - N - CA ANGL. DEV. = -9.1 DEGREES
REMARK 500 PRO C 497 N - CA - CB ANGL. DEV. = 8.9 DEGREES
REMARK 500 LEU D 250 O - C - N ANGL. DEV. = -11.2 DEGREES
REMARK 500 LEU D 396 O - C - N ANGL. DEV. = -17.2 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 TRP A 63 -72.10 -142.62
REMARK 500 ALA A 187 84.96 -167.64
REMARK 500 VAL A 251 50.02 35.84
REMARK 500 LEU A 330 117.77 -162.31
REMARK 500 SER A 424 143.40 -178.30
REMARK 500 GLN A 448 -7.06 96.97
REMARK 500 GLN A 448 -8.37 96.97
REMARK 500 LYS A 460 -135.68 56.20
REMARK 500 LEU A 468 179.54 71.66
REMARK 500 ASN B 61 45.29 -105.68
REMARK 500 ASN B 61 45.29 -108.22
REMARK 500 ASN B 62 16.98 -140.03
REMARK 500 TRP B 63 -71.03 -146.20
REMARK 500 ALA B 187 80.16 -158.91
REMARK 500 VAL B 251 47.71 34.79
REMARK 500 TRP B 285 157.16 -49.70
REMARK 500 GLN B 289 58.57 -91.52
REMARK 500 ALA B 304 -72.94 -71.62
REMARK 500 ASN B 317 50.69 -95.87
REMARK 500 LEU B 330 132.71 -174.11
REMARK 500 GLU B 352 1.05 -69.57
REMARK 500 SER B 402 -30.73 -137.32
REMARK 500 SER B 424 131.59 -175.87
REMARK 500 GLN B 448 -10.73 99.85
REMARK 500 GLN B 448 1.30 99.85
REMARK 500 LYS B 460 -137.04 59.09
REMARK 500 LYS B 460 -137.43 59.09
REMARK 500 LEU B 468 179.10 57.68
REMARK 500 PRO C 4 -152.23 -75.17
REMARK 500 ARG C 60 -175.44 -68.32
REMARK 500 TRP C 63 -57.20 -127.58
REMARK 500 ALA C 187 82.52 -162.82
REMARK 500 VAL C 251 52.19 31.09
REMARK 500 CYS C 283 -27.24 -141.74
REMARK 500 GLN C 289 52.83 -98.70
REMARK 500 LEU C 330 118.00 -167.83
REMARK 500 LEU C 418 -72.75 -74.70
REMARK 500 GLN C 448 -1.63 87.84
REMARK 500 LYS C 460 -132.88 52.81
REMARK 500 LEU C 468 177.79 64.58
REMARK 500 TRP D 63 -73.68 -141.78
REMARK 500 LYS D 85 31.38 -96.30
REMARK 500 PRO D 136 -74.77 -64.37
REMARK 500 ALA D 187 81.22 -153.38
REMARK 500 VAL D 251 51.39 27.01
REMARK 500 SER D 424 142.47 -170.64
REMARK 500 GLN D 448 -3.63 89.47
REMARK 500 LYS D 460 -136.07 51.28
REMARK 500 LEU D 468 177.82 62.27
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 THR A 166 -12.71
REMARK 500 LEU C 256 11.18
REMARK 500 LEU D 396 14.94
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH B2006 DISTANCE = 6.43 ANGSTROMS
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 PG4 A 1503
REMARK 610 PG4 C 1500
REMARK 610 PG4 D 1502
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD A 1499
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD A 1500
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD A 1501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CHT A 1502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PG4 A 1503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD B 1498
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD B 1499
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD B 1500
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CHT B 1501
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 1502
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD C 1498
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD C 1499
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PG4 C 1500
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ETX C 1501
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD D 1498
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD D 1500
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CHT D 1501
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PG4 D 1502
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL D 1503
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4V37 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF BETAINE ALDEHYDE DEHYDROGENASE FROM SPINACH
REMARK 900 SHOWING A THIOHEMIACETAL WITH 3- AMINOPROPIONALDEHYDE
DBREF 4V3F A 1 497 UNP P17202 BADH_SPIOL 1 497
DBREF 4V3F B 1 497 UNP P17202 BADH_SPIOL 1 497
DBREF 4V3F C 1 497 UNP P17202 BADH_SPIOL 1 497
DBREF 4V3F D 1 497 UNP P17202 BADH_SPIOL 1 497
SEQADV 4V3F CSO A 291 UNP P17202 CYS 291 MICROHETEROGENEITY
SEQADV 4V3F CSO B 291 UNP P17202 CYS 291 MICROHETEROGENEITY
SEQADV 4V3F CSO D 291 UNP P17202 CYS 291 MICROHETEROGENEITY
SEQRES 1 A 497 MET ALA PHE PRO ILE PRO ALA ARG GLN LEU PHE ILE ASP
SEQRES 2 A 497 GLY GLU TRP ARG GLU PRO ILE LYS LYS ASN ARG ILE PRO
SEQRES 3 A 497 VAL ILE ASN PRO SER THR GLU GLU ILE ILE GLY ASP ILE
SEQRES 4 A 497 PRO ALA ALA THR ALA GLU ASP VAL GLU VAL ALA VAL VAL
SEQRES 5 A 497 ALA ALA ARG ARG ALA PHE ARG ARG ASN ASN TRP SER ALA
SEQRES 6 A 497 THR SER GLY ALA HIS ARG ALA THR TYR LEU ARG ALA ILE
SEQRES 7 A 497 ALA ALA LYS ILE THR GLU LYS LYS ASP HIS PHE VAL LYS
SEQRES 8 A 497 LEU GLU THR ILE ASP SER GLY LYS PRO PHE ASP GLU ALA
SEQRES 9 A 497 VAL LEU ASP ILE ASP ASP VAL ALA SER CYS PHE GLU TYR
SEQRES 10 A 497 PHE ALA GLY GLN ALA GLU ALA LEU ASP GLY LYS GLN LYS
SEQRES 11 A 497 ALA PRO VAL THR LEU PRO MET GLU ARG PHE LYS SER HIS
SEQRES 12 A 497 VAL LEU ARG GLN PRO LEU GLY VAL VAL GLY LEU ILE SER
SEQRES 13 A 497 PRO TRP ASN TYR PRO LEU LEU MET ALA THR TRP LYS ILE
SEQRES 14 A 497 ALA PRO ALA LEU ALA ALA GLY CYS THR ALA VAL LEU LYS
SEQRES 15 A 497 PRO SER GLU LEU ALA SER VAL THR CYS LEU GLU PHE GLY
SEQRES 16 A 497 GLU VAL CYS ASN GLU VAL GLY LEU PRO PRO GLY VAL LEU
SEQRES 17 A 497 ASN ILE LEU THR GLY LEU GLY PRO ASP ALA GLY ALA PRO
SEQRES 18 A 497 LEU VAL SER HIS PRO ASP VAL ASP LYS ILE ALA PHE THR
SEQRES 19 A 497 GLY SER SER ALA THR GLY SER LYS VAL MET ALA SER ALA
SEQRES 20 A 497 ALA GLN LEU VAL LYS PRO VAL THR LEU GLU LEU GLY GLY
SEQRES 21 A 497 LYS SER PRO ILE VAL VAL PHE GLU ASP VAL ASP ILE ASP
SEQRES 22 A 497 LYS VAL VAL GLU TRP THR ILE PHE GLY CYS PHE TRP THR
SEQRES 23 A 497 ASN GLY GLN ILE CSO SER ALA THR SER ARG LEU LEU VAL
SEQRES 24 A 497 HIS GLU SER ILE ALA ALA GLU PHE VAL ASP LYS LEU VAL
SEQRES 25 A 497 LYS TRP THR LYS ASN ILE LYS ILE SER ASP PRO PHE GLU
SEQRES 26 A 497 GLU GLY CYS ARG LEU GLY PRO VAL ILE SER LYS GLY GLN
SEQRES 27 A 497 TYR ASP LYS ILE MET LYS PHE ILE SER THR ALA LYS SER
SEQRES 28 A 497 GLU GLY ALA THR ILE LEU TYR GLY GLY SER ARG PRO GLU
SEQRES 29 A 497 HIS LEU LYS LYS GLY TYR TYR ILE GLU PRO THR ILE VAL
SEQRES 30 A 497 THR ASP ILE SER THR SER MET GLN ILE TRP LYS GLU GLU
SEQRES 31 A 497 VAL PHE GLY PRO VAL LEU CYS VAL LYS THR PHE SER SER
SEQRES 32 A 497 GLU ASP GLU ALA ILE ALA LEU ALA ASN ASP THR GLU TYR
SEQRES 33 A 497 GLY LEU ALA ALA ALA VAL PHE SER ASN ASP LEU GLU ARG
SEQRES 34 A 497 CYS GLU ARG ILE THR LYS ALA LEU GLU VAL GLY ALA VAL
SEQRES 35 A 497 TRP VAL ASN CYS SER GLN PRO CYS PHE VAL GLN ALA PRO
SEQRES 36 A 497 TRP GLY GLY ILE LYS ARG SER GLY PHE GLY ARG GLU LEU
SEQRES 37 A 497 GLY GLU TRP GLY ILE GLN ASN TYR LEU ASN ILE LYS GLN
SEQRES 38 A 497 VAL THR GLN ASP ILE SER ASP GLU PRO TRP GLY TRP TYR
SEQRES 39 A 497 LYS SER PRO
SEQRES 1 B 497 MET ALA PHE PRO ILE PRO ALA ARG GLN LEU PHE ILE ASP
SEQRES 2 B 497 GLY GLU TRP ARG GLU PRO ILE LYS LYS ASN ARG ILE PRO
SEQRES 3 B 497 VAL ILE ASN PRO SER THR GLU GLU ILE ILE GLY ASP ILE
SEQRES 4 B 497 PRO ALA ALA THR ALA GLU ASP VAL GLU VAL ALA VAL VAL
SEQRES 5 B 497 ALA ALA ARG ARG ALA PHE ARG ARG ASN ASN TRP SER ALA
SEQRES 6 B 497 THR SER GLY ALA HIS ARG ALA THR TYR LEU ARG ALA ILE
SEQRES 7 B 497 ALA ALA LYS ILE THR GLU LYS LYS ASP HIS PHE VAL LYS
SEQRES 8 B 497 LEU GLU THR ILE ASP SER GLY LYS PRO PHE ASP GLU ALA
SEQRES 9 B 497 VAL LEU ASP ILE ASP ASP VAL ALA SER CYS PHE GLU TYR
SEQRES 10 B 497 PHE ALA GLY GLN ALA GLU ALA LEU ASP GLY LYS GLN LYS
SEQRES 11 B 497 ALA PRO VAL THR LEU PRO MET GLU ARG PHE LYS SER HIS
SEQRES 12 B 497 VAL LEU ARG GLN PRO LEU GLY VAL VAL GLY LEU ILE SER
SEQRES 13 B 497 PRO TRP ASN TYR PRO LEU LEU MET ALA THR TRP LYS ILE
SEQRES 14 B 497 ALA PRO ALA LEU ALA ALA GLY CYS THR ALA VAL LEU LYS
SEQRES 15 B 497 PRO SER GLU LEU ALA SER VAL THR CYS LEU GLU PHE GLY
SEQRES 16 B 497 GLU VAL CYS ASN GLU VAL GLY LEU PRO PRO GLY VAL LEU
SEQRES 17 B 497 ASN ILE LEU THR GLY LEU GLY PRO ASP ALA GLY ALA PRO
SEQRES 18 B 497 LEU VAL SER HIS PRO ASP VAL ASP LYS ILE ALA PHE THR
SEQRES 19 B 497 GLY SER SER ALA THR GLY SER LYS VAL MET ALA SER ALA
SEQRES 20 B 497 ALA GLN LEU VAL LYS PRO VAL THR LEU GLU LEU GLY GLY
SEQRES 21 B 497 LYS SER PRO ILE VAL VAL PHE GLU ASP VAL ASP ILE ASP
SEQRES 22 B 497 LYS VAL VAL GLU TRP THR ILE PHE GLY CYS PHE TRP THR
SEQRES 23 B 497 ASN GLY GLN ILE CSO SER ALA THR SER ARG LEU LEU VAL
SEQRES 24 B 497 HIS GLU SER ILE ALA ALA GLU PHE VAL ASP LYS LEU VAL
SEQRES 25 B 497 LYS TRP THR LYS ASN ILE LYS ILE SER ASP PRO PHE GLU
SEQRES 26 B 497 GLU GLY CYS ARG LEU GLY PRO VAL ILE SER LYS GLY GLN
SEQRES 27 B 497 TYR ASP LYS ILE MET LYS PHE ILE SER THR ALA LYS SER
SEQRES 28 B 497 GLU GLY ALA THR ILE LEU TYR GLY GLY SER ARG PRO GLU
SEQRES 29 B 497 HIS LEU LYS LYS GLY TYR TYR ILE GLU PRO THR ILE VAL
SEQRES 30 B 497 THR ASP ILE SER THR SER MET GLN ILE TRP LYS GLU GLU
SEQRES 31 B 497 VAL PHE GLY PRO VAL LEU CYS VAL LYS THR PHE SER SER
SEQRES 32 B 497 GLU ASP GLU ALA ILE ALA LEU ALA ASN ASP THR GLU TYR
SEQRES 33 B 497 GLY LEU ALA ALA ALA VAL PHE SER ASN ASP LEU GLU ARG
SEQRES 34 B 497 CYS GLU ARG ILE THR LYS ALA LEU GLU VAL GLY ALA VAL
SEQRES 35 B 497 TRP VAL ASN CYS SER GLN PRO CYS PHE VAL GLN ALA PRO
SEQRES 36 B 497 TRP GLY GLY ILE LYS ARG SER GLY PHE GLY ARG GLU LEU
SEQRES 37 B 497 GLY GLU TRP GLY ILE GLN ASN TYR LEU ASN ILE LYS GLN
SEQRES 38 B 497 VAL THR GLN ASP ILE SER ASP GLU PRO TRP GLY TRP TYR
SEQRES 39 B 497 LYS SER PRO
SEQRES 1 C 497 MET ALA PHE PRO ILE PRO ALA ARG GLN LEU PHE ILE ASP
SEQRES 2 C 497 GLY GLU TRP ARG GLU PRO ILE LYS LYS ASN ARG ILE PRO
SEQRES 3 C 497 VAL ILE ASN PRO SER THR GLU GLU ILE ILE GLY ASP ILE
SEQRES 4 C 497 PRO ALA ALA THR ALA GLU ASP VAL GLU VAL ALA VAL VAL
SEQRES 5 C 497 ALA ALA ARG ARG ALA PHE ARG ARG ASN ASN TRP SER ALA
SEQRES 6 C 497 THR SER GLY ALA HIS ARG ALA THR TYR LEU ARG ALA ILE
SEQRES 7 C 497 ALA ALA LYS ILE THR GLU LYS LYS ASP HIS PHE VAL LYS
SEQRES 8 C 497 LEU GLU THR ILE ASP SER GLY LYS PRO PHE ASP GLU ALA
SEQRES 9 C 497 VAL LEU ASP ILE ASP ASP VAL ALA SER CYS PHE GLU TYR
SEQRES 10 C 497 PHE ALA GLY GLN ALA GLU ALA LEU ASP GLY LYS GLN LYS
SEQRES 11 C 497 ALA PRO VAL THR LEU PRO MET GLU ARG PHE LYS SER HIS
SEQRES 12 C 497 VAL LEU ARG GLN PRO LEU GLY VAL VAL GLY LEU ILE SER
SEQRES 13 C 497 PRO TRP ASN TYR PRO LEU LEU MET ALA THR TRP LYS ILE
SEQRES 14 C 497 ALA PRO ALA LEU ALA ALA GLY CYS THR ALA VAL LEU LYS
SEQRES 15 C 497 PRO SER GLU LEU ALA SER VAL THR CYS LEU GLU PHE GLY
SEQRES 16 C 497 GLU VAL CYS ASN GLU VAL GLY LEU PRO PRO GLY VAL LEU
SEQRES 17 C 497 ASN ILE LEU THR GLY LEU GLY PRO ASP ALA GLY ALA PRO
SEQRES 18 C 497 LEU VAL SER HIS PRO ASP VAL ASP LYS ILE ALA PHE THR
SEQRES 19 C 497 GLY SER SER ALA THR GLY SER LYS VAL MET ALA SER ALA
SEQRES 20 C 497 ALA GLN LEU VAL LYS PRO VAL THR LEU GLU LEU GLY GLY
SEQRES 21 C 497 LYS SER PRO ILE VAL VAL PHE GLU ASP VAL ASP ILE ASP
SEQRES 22 C 497 LYS VAL VAL GLU TRP THR ILE PHE GLY CYS PHE TRP THR
SEQRES 23 C 497 ASN GLY GLN ILE CSO SER ALA THR SER ARG LEU LEU VAL
SEQRES 24 C 497 HIS GLU SER ILE ALA ALA GLU PHE VAL ASP LYS LEU VAL
SEQRES 25 C 497 LYS TRP THR LYS ASN ILE LYS ILE SER ASP PRO PHE GLU
SEQRES 26 C 497 GLU GLY CYS ARG LEU GLY PRO VAL ILE SER LYS GLY GLN
SEQRES 27 C 497 TYR ASP LYS ILE MET LYS PHE ILE SER THR ALA LYS SER
SEQRES 28 C 497 GLU GLY ALA THR ILE LEU TYR GLY GLY SER ARG PRO GLU
SEQRES 29 C 497 HIS LEU LYS LYS GLY TYR TYR ILE GLU PRO THR ILE VAL
SEQRES 30 C 497 THR ASP ILE SER THR SER MET GLN ILE TRP LYS GLU GLU
SEQRES 31 C 497 VAL PHE GLY PRO VAL LEU CYS VAL LYS THR PHE SER SER
SEQRES 32 C 497 GLU ASP GLU ALA ILE ALA LEU ALA ASN ASP THR GLU TYR
SEQRES 33 C 497 GLY LEU ALA ALA ALA VAL PHE SER ASN ASP LEU GLU ARG
SEQRES 34 C 497 CYS GLU ARG ILE THR LYS ALA LEU GLU VAL GLY ALA VAL
SEQRES 35 C 497 TRP VAL ASN CYS SER GLN PRO CSO PHE VAL GLN ALA PRO
SEQRES 36 C 497 TRP GLY GLY ILE LYS ARG SER GLY PHE GLY ARG GLU LEU
SEQRES 37 C 497 GLY GLU TRP GLY ILE GLN ASN TYR LEU ASN ILE LYS GLN
SEQRES 38 C 497 VAL THR GLN ASP ILE SER ASP GLU PRO TRP GLY TRP TYR
SEQRES 39 C 497 LYS SER PRO
SEQRES 1 D 497 MET ALA PHE PRO ILE PRO ALA ARG GLN LEU PHE ILE ASP
SEQRES 2 D 497 GLY GLU TRP ARG GLU PRO ILE LYS LYS ASN ARG ILE PRO
SEQRES 3 D 497 VAL ILE ASN PRO SER THR GLU GLU ILE ILE GLY ASP ILE
SEQRES 4 D 497 PRO ALA ALA THR ALA GLU ASP VAL GLU VAL ALA VAL VAL
SEQRES 5 D 497 ALA ALA ARG ARG ALA PHE ARG ARG ASN ASN TRP SER ALA
SEQRES 6 D 497 THR SER GLY ALA HIS ARG ALA THR TYR LEU ARG ALA ILE
SEQRES 7 D 497 ALA ALA LYS ILE THR GLU LYS LYS ASP HIS PHE VAL LYS
SEQRES 8 D 497 LEU GLU THR ILE ASP SER GLY LYS PRO PHE ASP GLU ALA
SEQRES 9 D 497 VAL LEU ASP ILE ASP ASP VAL ALA SER CYS PHE GLU TYR
SEQRES 10 D 497 PHE ALA GLY GLN ALA GLU ALA LEU ASP GLY LYS GLN LYS
SEQRES 11 D 497 ALA PRO VAL THR LEU PRO MET GLU ARG PHE LYS SER HIS
SEQRES 12 D 497 VAL LEU ARG GLN PRO LEU GLY VAL VAL GLY LEU ILE SER
SEQRES 13 D 497 PRO TRP ASN TYR PRO LEU LEU MET ALA THR TRP LYS ILE
SEQRES 14 D 497 ALA PRO ALA LEU ALA ALA GLY CYS THR ALA VAL LEU LYS
SEQRES 15 D 497 PRO SER GLU LEU ALA SER VAL THR CYS LEU GLU PHE GLY
SEQRES 16 D 497 GLU VAL CYS ASN GLU VAL GLY LEU PRO PRO GLY VAL LEU
SEQRES 17 D 497 ASN ILE LEU THR GLY LEU GLY PRO ASP ALA GLY ALA PRO
SEQRES 18 D 497 LEU VAL SER HIS PRO ASP VAL ASP LYS ILE ALA PHE THR
SEQRES 19 D 497 GLY SER SER ALA THR GLY SER LYS VAL MET ALA SER ALA
SEQRES 20 D 497 ALA GLN LEU VAL LYS PRO VAL THR LEU GLU LEU GLY GLY
SEQRES 21 D 497 LYS SER PRO ILE VAL VAL PHE GLU ASP VAL ASP ILE ASP
SEQRES 22 D 497 LYS VAL VAL GLU TRP THR ILE PHE GLY CYS PHE TRP THR
SEQRES 23 D 497 ASN GLY GLN ILE CSO SER ALA THR SER ARG LEU LEU VAL
SEQRES 24 D 497 HIS GLU SER ILE ALA ALA GLU PHE VAL ASP LYS LEU VAL
SEQRES 25 D 497 LYS TRP THR LYS ASN ILE LYS ILE SER ASP PRO PHE GLU
SEQRES 26 D 497 GLU GLY CYS ARG LEU GLY PRO VAL ILE SER LYS GLY GLN
SEQRES 27 D 497 TYR ASP LYS ILE MET LYS PHE ILE SER THR ALA LYS SER
SEQRES 28 D 497 GLU GLY ALA THR ILE LEU TYR GLY GLY SER ARG PRO GLU
SEQRES 29 D 497 HIS LEU LYS LYS GLY TYR TYR ILE GLU PRO THR ILE VAL
SEQRES 30 D 497 THR ASP ILE SER THR SER MET GLN ILE TRP LYS GLU GLU
SEQRES 31 D 497 VAL PHE GLY PRO VAL LEU CYS VAL LYS THR PHE SER SER
SEQRES 32 D 497 GLU ASP GLU ALA ILE ALA LEU ALA ASN ASP THR GLU TYR
SEQRES 33 D 497 GLY LEU ALA ALA ALA VAL PHE SER ASN ASP LEU GLU ARG
SEQRES 34 D 497 CYS GLU ARG ILE THR LYS ALA LEU GLU VAL GLY ALA VAL
SEQRES 35 D 497 TRP VAL ASN CYS SER GLN PRO CYS PHE VAL GLN ALA PRO
SEQRES 36 D 497 TRP GLY GLY ILE LYS ARG SER GLY PHE GLY ARG GLU LEU
SEQRES 37 D 497 GLY GLU TRP GLY ILE GLN ASN TYR LEU ASN ILE LYS GLN
SEQRES 38 D 497 VAL THR GLN ASP ILE SER ASP GLU PRO TRP GLY TRP TYR
SEQRES 39 D 497 LYS SER PRO
MODRES 4V3F CSO A 291 CYS S-HYDROXYCYSTEINE
MODRES 4V3F CSO B 291 CYS S-HYDROXYCYSTEINE
MODRES 4V3F CSO C 291 CYS S-HYDROXYCYSTEINE
MODRES 4V3F CSO C 450 CYS S-HYDROXYCYSTEINE
MODRES 4V3F CSO D 291 CYS S-HYDROXYCYSTEINE
HET CSO A 291 7
HET CSO B 291 14
HET CSO C 291 7
HET CSO C 450 7
HET CSO D 291 7
HET IOD A 501 1
HET IOD A1498 1
HET IOD A1499 1
HET IOD A1500 1
HET IOD A1501 1
HET CHT A1502 7
HET PG4 A1503 12
HET IOD B 502 1
HET IOD B1498 1
HET IOD B1499 1
HET IOD B1500 1
HET CHT B1501 7
HET GOL B1502 6
HET IOD C 503 1
HET IOD C1498 1
HET IOD C1499 1
HET PG4 C1500 12
HET ETX C1501 6
HET IOD D1498 1
HET IOD D1499 1
HET IOD D1500 1
HET CHT D1501 7
HET PG4 D1502 12
HET GOL D1503 6
HETNAM CSO S-HYDROXYCYSTEINE
HETNAM IOD IODIDE ION
HETNAM CHT CHOLINE ION
HETNAM PG4 TETRAETHYLENE GLYCOL
HETNAM GOL GLYCEROL
HETNAM ETX 2-ETHOXYETHANOL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 1 CSO 5(C3 H7 N O3 S)
FORMUL 5 IOD 15(I 1-)
FORMUL 10 CHT 3(C5 H14 N O 1+)
FORMUL 11 PG4 3(C8 H18 O5)
FORMUL 17 GOL 2(C3 H8 O3)
FORMUL 22 ETX C4 H10 O2
FORMUL 29 HOH *661(H2 O)
HELIX 1 1 THR A 43 ARG A 60 1 18
HELIX 2 2 SER A 67 LYS A 85 1 19
HELIX 3 3 LYS A 85 GLY A 98 1 14
HELIX 4 4 PRO A 100 GLY A 127 1 28
HELIX 5 5 TYR A 160 GLY A 176 1 17
HELIX 6 6 SER A 188 VAL A 201 1 14
HELIX 7 7 LEU A 214 HIS A 225 1 12
HELIX 8 8 SER A 236 ALA A 248 1 13
HELIX 9 9 GLN A 249 VAL A 251 5 3
HELIX 10 10 ASP A 271 GLY A 282 1 12
HELIX 11 11 PHE A 284 GLN A 289 5 6
HELIX 12 12 ILE A 303 ASN A 317 1 15
HELIX 13 13 SER A 335 GLU A 352 1 18
HELIX 14 14 MET A 384 GLU A 389 1 6
HELIX 15 15 SER A 403 ASN A 412 1 10
HELIX 16 16 ASP A 426 LEU A 437 1 12
HELIX 17 17 ILE A 459 ARG A 461 5 3
HELIX 18 18 LEU A 468 GLY A 472 5 5
HELIX 19 19 GLY A 472 ASN A 475 5 4
HELIX 20 20 THR B 43 ARG B 60 1 18
HELIX 21 21 SER B 67 LYS B 85 1 19
HELIX 22 22 LYS B 85 SER B 97 1 13
HELIX 23 23 PRO B 100 GLY B 127 1 28
HELIX 24 24 TYR B 160 GLY B 176 1 17
HELIX 25 25 SER B 188 GLY B 202 1 15
HELIX 26 26 LEU B 214 HIS B 225 1 12
HELIX 27 27 SER B 236 GLN B 249 1 14
HELIX 28 28 ASP B 271 TRP B 285 1 15
HELIX 29 29 THR B 286 GLN B 289 5 4
HELIX 30 30 ILE B 303 ASN B 317 1 15
HELIX 31 31 SER B 335 GLU B 352 1 18
HELIX 32 32 MET B 384 GLU B 389 1 6
HELIX 33 33 SER B 403 ASP B 413 1 11
HELIX 34 34 ASP B 426 LEU B 437 1 12
HELIX 35 35 ILE B 459 ARG B 461 5 3
HELIX 36 36 LEU B 468 GLY B 472 5 5
HELIX 37 37 GLY B 472 ASN B 475 5 4
HELIX 38 38 THR C 43 ARG C 59 1 17
HELIX 39 39 SER C 67 LYS C 85 1 19
HELIX 40 40 LYS C 85 GLY C 98 1 14
HELIX 41 41 PRO C 100 GLY C 127 1 28
HELIX 42 42 TYR C 160 GLY C 176 1 17
HELIX 43 43 SER C 188 VAL C 201 1 14
HELIX 44 44 LEU C 214 HIS C 225 1 12
HELIX 45 45 SER C 236 GLN C 249 1 14
HELIX 46 46 ASP C 271 GLY C 282 1 12
HELIX 47 47 PHE C 284 GLN C 289 5 6
HELIX 48 48 GLU C 301 ASN C 317 1 17
HELIX 49 49 SER C 335 GLU C 352 1 18
HELIX 50 50 MET C 384 GLU C 389 1 6
HELIX 51 51 SER C 403 ASP C 413 1 11
HELIX 52 52 ASP C 426 LEU C 437 1 12
HELIX 53 53 ILE C 459 ARG C 461 5 3
HELIX 54 54 LEU C 468 GLY C 472 5 5
HELIX 55 55 GLY C 472 ASN C 475 5 4
HELIX 56 56 THR D 43 ARG D 60 1 18
HELIX 57 57 SER D 67 LYS D 85 1 19
HELIX 58 58 LYS D 85 GLY D 98 1 14
HELIX 59 59 PRO D 100 ASP D 126 1 27
HELIX 60 60 TYR D 160 ALA D 175 1 16
HELIX 61 61 SER D 188 VAL D 201 1 14
HELIX 62 62 ALA D 218 HIS D 225 1 8
HELIX 63 63 SER D 236 LEU D 250 1 15
HELIX 64 64 ASP D 271 TRP D 285 1 15
HELIX 65 65 THR D 286 GLN D 289 5 4
HELIX 66 66 ILE D 303 ASN D 317 1 15
HELIX 67 67 SER D 335 GLU D 352 1 18
HELIX 68 68 MET D 384 GLU D 389 1 6
HELIX 69 69 SER D 403 ASP D 413 1 11
HELIX 70 70 ASP D 426 LEU D 437 1 12
HELIX 71 71 ILE D 459 ARG D 461 5 3
HELIX 72 72 LEU D 468 GLY D 472 5 5
HELIX 73 73 GLY D 472 ASN D 475 5 4
SHEET 1 AA 2 LEU A 10 ILE A 12 0
SHEET 2 AA 2 GLU A 15 ARG A 17 -1 O GLU A 15 N ILE A 12
SHEET 1 AB 2 ARG A 24 ILE A 28 0
SHEET 2 AB 2 ILE A 35 PRO A 40 -1 N ILE A 36 O VAL A 27
SHEET 1 AC10 ALA A 131 VAL A 133 0
SHEET 2 AC10 PHE A 140 PRO A 148 -1 O SER A 142 N VAL A 133
SHEET 3 AC10 LEU A 477 ASP A 485 -1 O ASN A 478 N GLN A 147
SHEET 4 AC10 ALA B 441 VAL B 444 1 O VAL B 442 N THR A 483
SHEET 5 AC10 ALA B 419 PHE B 423 1 O ALA B 420 N TRP B 443
SHEET 6 AC10 SER B 262 VAL B 266 1 O PRO B 263 N ALA B 421
SHEET 7 AC10 THR B 294 HIS B 300 1 O ARG B 296 N ILE B 264
SHEET 8 AC10 VAL B 395 PHE B 401 1 O CYS B 397 N LEU B 297
SHEET 9 AC10 THR B 375 THR B 378 1 O THR B 375 N LEU B 396
SHEET 10 AC10 THR B 355 TYR B 358 -1 O THR B 355 N THR B 378
SHEET 1 AD 6 LEU A 208 ILE A 210 0
SHEET 2 AD 6 THR A 178 PRO A 183 1 O ALA A 179 N ASN A 209
SHEET 3 AD 6 VAL A 151 SER A 156 1 O VAL A 152 N VAL A 180
SHEET 4 AD 6 LYS A 230 THR A 234 1 O LYS A 230 N GLY A 153
SHEET 5 AD 6 VAL A 254 GLU A 257 1 O THR A 255 N PHE A 233
SHEET 6 AD 6 GLY A 463 PHE A 464 -1 O PHE A 464 N LEU A 256
SHEET 1 AE10 THR A 355 TYR A 358 0
SHEET 2 AE10 THR A 375 THR A 378 -1 O ILE A 376 N TYR A 358
SHEET 3 AE10 VAL A 395 PHE A 401 1 O LEU A 396 N VAL A 377
SHEET 4 AE10 THR A 294 HIS A 300 1 O SER A 295 N CYS A 397
SHEET 5 AE10 SER A 262 VAL A 266 1 O SER A 262 N ARG A 296
SHEET 6 AE10 ALA A 419 PHE A 423 1 O ALA A 421 N VAL A 265
SHEET 7 AE10 ALA A 441 VAL A 444 1 O ALA A 441 N ALA A 420
SHEET 8 AE10 LEU B 477 ASP B 485 1 O GLN B 481 N VAL A 442
SHEET 9 AE10 PHE B 140 PRO B 148 -1 O LYS B 141 N GLN B 484
SHEET 10 AE10 ALA B 131 VAL B 133 -1 O ALA B 131 N VAL B 144
SHEET 1 BA 2 LEU B 10 ILE B 12 0
SHEET 2 BA 2 GLU B 15 ARG B 17 -1 O GLU B 15 N ILE B 12
SHEET 1 BB 2 ARG B 24 ILE B 28 0
SHEET 2 BB 2 ILE B 35 PRO B 40 -1 N ILE B 36 O VAL B 27
SHEET 1 BC 6 LEU B 208 ILE B 210 0
SHEET 2 BC 6 THR B 178 PRO B 183 1 O ALA B 179 N ASN B 209
SHEET 3 BC 6 VAL B 151 SER B 156 1 O VAL B 152 N VAL B 180
SHEET 4 BC 6 LYS B 230 THR B 234 1 O LYS B 230 N GLY B 153
SHEET 5 BC 6 VAL B 254 GLU B 257 1 O THR B 255 N PHE B 233
SHEET 6 BC 6 GLY B 463 PHE B 464 -1 O PHE B 464 N LEU B 256
SHEET 1 CA 2 LEU C 10 ILE C 12 0
SHEET 2 CA 2 GLU C 15 ARG C 17 -1 O GLU C 15 N ILE C 12
SHEET 1 CB 2 ARG C 24 ILE C 28 0
SHEET 2 CB 2 ILE C 35 PRO C 40 -1 N ILE C 36 O VAL C 27
SHEET 1 CC10 ALA C 131 VAL C 133 0
SHEET 2 CC10 PHE C 140 PRO C 148 -1 O SER C 142 N VAL C 133
SHEET 3 CC10 LEU C 477 ASP C 485 -1 O ASN C 478 N GLN C 147
SHEET 4 CC10 ALA D 441 VAL D 444 1 O VAL D 442 N THR C 483
SHEET 5 CC10 ALA D 419 PHE D 423 1 O ALA D 420 N TRP D 443
SHEET 6 CC10 SER D 262 VAL D 266 1 O PRO D 263 N ALA D 421
SHEET 7 CC10 THR D 294 HIS D 300 1 O ARG D 296 N ILE D 264
SHEET 8 CC10 VAL D 395 PHE D 401 1 O CYS D 397 N LEU D 297
SHEET 9 CC10 THR D 375 THR D 378 1 O THR D 375 N LEU D 396
SHEET 10 CC10 THR D 355 TYR D 358 -1 O THR D 355 N THR D 378
SHEET 1 CD 6 LEU C 208 ILE C 210 0
SHEET 2 CD 6 THR C 178 LYS C 182 1 O ALA C 179 N ASN C 209
SHEET 3 CD 6 VAL C 151 ILE C 155 1 O VAL C 152 N VAL C 180
SHEET 4 CD 6 LYS C 230 THR C 234 1 O LYS C 230 N GLY C 153
SHEET 5 CD 6 VAL C 254 GLU C 257 1 O THR C 255 N PHE C 233
SHEET 6 CD 6 GLY C 463 PHE C 464 -1 O PHE C 464 N LEU C 256
SHEET 1 CE10 THR C 355 TYR C 358 0
SHEET 2 CE10 THR C 375 THR C 378 -1 O ILE C 376 N LEU C 357
SHEET 3 CE10 VAL C 395 PHE C 401 1 O LEU C 396 N VAL C 377
SHEET 4 CE10 ARG C 296 HIS C 300 1 O LEU C 297 N LYS C 399
SHEET 5 CE10 PRO C 263 VAL C 266 1 O ILE C 264 N LEU C 298
SHEET 6 CE10 ALA C 419 PHE C 423 1 O ALA C 421 N VAL C 265
SHEET 7 CE10 ALA C 441 VAL C 444 1 O ALA C 441 N ALA C 420
SHEET 8 CE10 LEU D 477 ASP D 485 1 O GLN D 481 N VAL C 442
SHEET 9 CE10 PHE D 140 PRO D 148 -1 O LYS D 141 N GLN D 484
SHEET 10 CE10 ALA D 131 VAL D 133 -1 O ALA D 131 N VAL D 144
SHEET 1 DA 2 LEU D 10 ILE D 12 0
SHEET 2 DA 2 GLU D 15 ARG D 17 -1 O GLU D 15 N ILE D 12
SHEET 1 DB 2 ARG D 24 ILE D 28 0
SHEET 2 DB 2 ILE D 35 PRO D 40 -1 N ILE D 36 O VAL D 27
SHEET 1 DC 6 LEU D 208 ILE D 210 0
SHEET 2 DC 6 THR D 178 PRO D 183 1 O ALA D 179 N ASN D 209
SHEET 3 DC 6 VAL D 151 SER D 156 1 O VAL D 152 N VAL D 180
SHEET 4 DC 6 LYS D 230 THR D 234 1 O LYS D 230 N GLY D 153
SHEET 5 DC 6 VAL D 254 GLU D 257 1 O THR D 255 N PHE D 233
SHEET 6 DC 6 GLY D 463 PHE D 464 -1 O PHE D 464 N LEU D 256
LINK C ILE A 290 N ACSO A 291 1555 1555 1.33
LINK C ACSO A 291 N SER A 292 1555 1555 1.33
LINK SG ACYS A 450 C4 CHT A1502 1555 1555 1.69
LINK C ILE B 290 N ACSO B 291 1555 1555 1.33
LINK C ILE B 290 N BCSO B 291 1555 1555 1.33
LINK C ACSO B 291 N SER B 292 1555 1555 1.33
LINK C BCSO B 291 N SER B 292 1555 1555 1.33
LINK SG ACYS B 450 C4 CHT B1501 1555 1555 1.77
LINK C ILE C 290 N CSO C 291 1555 1555 1.33
LINK C CSO C 291 N SER C 292 1555 1555 1.34
LINK C PRO C 449 N CSO C 450 1555 1555 1.34
LINK C CSO C 450 N PHE C 451 1555 1555 1.33
LINK C ILE D 290 N ACSO D 291 1555 1555 1.33
LINK C ACSO D 291 N SER D 292 1555 1555 1.33
LINK SG CYS D 450 C4 CHT D1501 1555 1555 1.68
SITE 1 AC1 2 HIS A 143 THR B 434
SITE 1 AC2 2 LYS A 21 ASN A 23
SITE 1 AC3 1 GLN A 474
SITE 1 AC4 6 TYR A 160 TRP A 167 ILE A 290 SER A 292
SITE 2 AC4 6 GLN A 448 CYS A 450
SITE 1 AC5 4 TRP A 471 GLN A 474 GLU B 470 TRP B 471
SITE 1 AC6 2 GLU A 431 HIS B 143
SITE 1 AC7 1 LYS B 128
SITE 1 AC8 2 HOH A2186 GLY B 465
SITE 1 AC9 5 TYR B 160 TRP B 167 CSO B 291 GLN B 448
SITE 2 AC9 5 CYS B 450
SITE 1 BC1 3 CYS B 450 PHE B 451 HOH B2121
SITE 1 BC2 1 HIS C 143
SITE 1 BC3 1 GLN C 474
SITE 1 BC4 3 TRP C 471 GLU D 470 TRP D 471
SITE 1 BC5 5 THR C 378 ASP C 379 ILE C 380 VAL C 398
SITE 2 BC5 5 HOH C2128
SITE 1 BC6 3 THR C 434 LYS D 130 HIS D 143
SITE 1 BC7 1 ARG D 146
SITE 1 BC8 5 TYR D 160 ILE D 290 CSO D 291 GLN D 448
SITE 2 BC8 5 CYS D 450
SITE 1 BC9 12 LEU C 149 VAL C 251 PRO C 253 LEU C 477
SITE 2 BC9 12 ILE C 479 GLY D 458 ILE D 459 LYS D 460
SITE 3 BC9 12 GLY D 463 PHE D 464 ARG D 466 HOH D2170
SITE 1 CC1 6 PHE D 281 TRP D 285 GLN D 448 PRO D 449
SITE 2 CC1 6 CYS D 450 HOH D2177
CRYST1 69.440 82.256 88.516 79.44 84.89 77.32 P 1 3
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 0.014401 -0.003240 -0.000753 0.00000
SCALE2 0.000000 0.012461 -0.002130 0.00000
SCALE3 0.000000 0.000000 0.011507 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
