HEADER OXIDOREDUCTASE/ELECTRON TRANSPORT 21-APR-11 3RMZ
TITLE CRYSTAL STRUCTURE OF THE W199F-MAUG/PRE-METHYLAMINE DEHYDROGENASE
TITLE 2 COMPLEX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: METHYLAMINE UTILIZATION PROTEIN MAUG;
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 1.-.-.-;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: METHYLAMINE DEHYDROGENASE LIGHT CHAIN;
COMPND 9 CHAIN: C, E;
COMPND 10 EC: 1.4.99.3;
COMPND 11 ENGINEERED: YES;
COMPND 12 MOL_ID: 3;
COMPND 13 MOLECULE: METHYLAMINE DEHYDROGENASE HEAVY CHAIN;
COMPND 14 CHAIN: D, F;
COMPND 15 EC: 1.4.99.3;
COMPND 16 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PARACOCCUS DENITRIFICANS;
SOURCE 3 ORGANISM_TAXID: 318586;
SOURCE 4 STRAIN: PD 1222;
SOURCE 5 GENE: MAUG, PDEN_4736;
SOURCE 6 EXPRESSION_SYSTEM: PARACOCCUS DENITRIFICANS;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 266;
SOURCE 8 MOL_ID: 2;
SOURCE 9 ORGANISM_SCIENTIFIC: PARACOCCUS DENITRIFICANS;
SOURCE 10 ORGANISM_TAXID: 318586;
SOURCE 11 STRAIN: PD 1222;
SOURCE 12 GENE: PDEN_4733;
SOURCE 13 EXPRESSION_SYSTEM: RHODOBACTER SPHAEROIDES;
SOURCE 14 EXPRESSION_SYSTEM_TAXID: 1063;
SOURCE 15 MOL_ID: 3;
SOURCE 16 ORGANISM_SCIENTIFIC: PARACOCCUS DENITRIFICANS;
SOURCE 17 ORGANISM_TAXID: 318586;
SOURCE 18 STRAIN: PD 1222;
SOURCE 19 GENE: PDEN_4730;
SOURCE 20 EXPRESSION_SYSTEM: RHODOBACTER SPHAEROIDES;
SOURCE 21 EXPRESSION_SYSTEM_TAXID: 1063
KEYWDS MAUG, METHYLAMINE DEHYDROGENASE, C-HEME, QUINONE COFACTOR, ELECTRON
KEYWDS 2 TRANSPORT, OXIDOREDUCTASE-ELECTRON TRANSPORT COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR L.M.R.JENSEN,C.M.WILMOT
REVDAT 5 06-DEC-23 3RMZ 1 REMARK
REVDAT 4 13-SEP-23 3RMZ 1 REMARK SEQADV LINK
REVDAT 3 26-OCT-11 3RMZ 1 JRNL
REVDAT 2 19-OCT-11 3RMZ 1 JRNL
REVDAT 1 05-OCT-11 3RMZ 0
JRNL AUTH N.A.TARBOUSH,L.M.JENSEN,E.T.YUKL,J.GENG,A.LIU,C.M.WILMOT,
JRNL AUTH 2 V.L.DAVIDSON
JRNL TITL MUTAGENESIS OF TRYPTOPHAN199 SUGGESTS THAT HOPPING IS
JRNL TITL 2 REQUIRED FOR MAUG-DEPENDENT TRYPTOPHAN TRYPTOPHYLQUINONE
JRNL TITL 3 BIOSYNTHESIS.
JRNL REF PROC.NATL.ACAD.SCI.USA V. 108 16956 2011
JRNL REFN ISSN 0027-8424
JRNL PMID 21969534
JRNL DOI 10.1073/PNAS.1109423108
REMARK 2
REMARK 2 RESOLUTION. 1.72 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0109
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.72
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 39.58
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 94.8
REMARK 3 NUMBER OF REFLECTIONS : 165090
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) : 0.141
REMARK 3 R VALUE (WORKING SET) : 0.138
REMARK 3 FREE R VALUE : 0.181
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 8789
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.72
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.77
REMARK 3 REFLECTION IN BIN (WORKING SET) : 8282
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 64.19
REMARK 3 BIN R VALUE (WORKING SET) : 0.2320
REMARK 3 BIN FREE R VALUE SET COUNT : 423
REMARK 3 BIN FREE R VALUE : 0.2920
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 13280
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 241
REMARK 3 SOLVENT ATOMS : 1876
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 20.26
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.06000
REMARK 3 B22 (A**2) : 0.08000
REMARK 3 B33 (A**2) : 0.01000
REMARK 3 B12 (A**2) : -0.01000
REMARK 3 B13 (A**2) : -0.01000
REMARK 3 B23 (A**2) : 0.05000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.099
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.061
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.133
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.974
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.958
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 14115 ; 0.027 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 19307 ; 2.308 ; 1.973
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1780 ; 6.656 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 687 ;34.879 ;23.755
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 2098 ;13.033 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 109 ;16.296 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 2024 ; 0.215 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 11217 ; 0.014 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
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): 8666 ; 1.316 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 13936 ; 2.092 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 5449 ; 3.322 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 5339 ; 5.030 ; 4.500
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 : 6
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 600
REMARK 3 ORIGIN FOR THE GROUP (A): 21.8860 27.1270 -75.7700
REMARK 3 T TENSOR
REMARK 3 T11: 0.0577 T22: 0.0315
REMARK 3 T33: 0.0566 T12: 0.0285
REMARK 3 T13: -0.0018 T23: -0.0307
REMARK 3 L TENSOR
REMARK 3 L11: 0.3294 L22: 0.3447
REMARK 3 L33: 1.0465 L12: 0.1051
REMARK 3 L13: -0.1643 L23: -0.0924
REMARK 3 S TENSOR
REMARK 3 S11: -0.0360 S12: 0.0130 S13: -0.0177
REMARK 3 S21: -0.0170 S22: 0.0087 S23: -0.0269
REMARK 3 S31: 0.0103 S32: -0.0045 S33: 0.0273
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 6 B 600
REMARK 3 ORIGIN FOR THE GROUP (A): 24.3160 29.9440 22.7960
REMARK 3 T TENSOR
REMARK 3 T11: 0.0369 T22: 0.0287
REMARK 3 T33: 0.0313 T12: -0.0047
REMARK 3 T13: 0.0169 T23: -0.0239
REMARK 3 L TENSOR
REMARK 3 L11: 0.5879 L22: 0.5870
REMARK 3 L33: 0.9959 L12: 0.0710
REMARK 3 L13: -0.0470 L23: -0.5014
REMARK 3 S TENSOR
REMARK 3 S11: 0.0345 S12: -0.0825 S13: 0.0446
REMARK 3 S21: 0.0669 S22: -0.0318 S23: 0.0265
REMARK 3 S31: -0.0343 S32: 0.0170 S33: -0.0027
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 7 C 137
REMARK 3 ORIGIN FOR THE GROUP (A): 0.1060 28.1810 -48.1310
REMARK 3 T TENSOR
REMARK 3 T11: 0.0452 T22: 0.0422
REMARK 3 T33: 0.0238 T12: 0.0111
REMARK 3 T13: -0.0239 T23: -0.0136
REMARK 3 L TENSOR
REMARK 3 L11: 0.3178 L22: 0.4748
REMARK 3 L33: 0.4388 L12: 0.0828
REMARK 3 L13: 0.0979 L23: -0.0445
REMARK 3 S TENSOR
REMARK 3 S11: 0.0171 S12: 0.0501 S13: -0.0239
REMARK 3 S21: -0.0803 S22: 0.0082 S23: 0.0694
REMARK 3 S31: 0.0313 S32: -0.0736 S33: -0.0253
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 11 D 386
REMARK 3 ORIGIN FOR THE GROUP (A): 2.8660 9.6630 -29.3810
REMARK 3 T TENSOR
REMARK 3 T11: 0.0971 T22: 0.0128
REMARK 3 T33: 0.0656 T12: -0.0175
REMARK 3 T13: -0.0175 T23: 0.0056
REMARK 3 L TENSOR
REMARK 3 L11: 0.2577 L22: 0.2249
REMARK 3 L33: 0.5717 L12: -0.1124
REMARK 3 L13: 0.0054 L23: 0.1481
REMARK 3 S TENSOR
REMARK 3 S11: 0.0345 S12: 0.0135 S13: -0.0872
REMARK 3 S21: -0.0033 S22: -0.0198 S23: 0.0653
REMARK 3 S31: 0.1981 S32: -0.0692 S33: -0.0147
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : E 7 E 130
REMARK 3 ORIGIN FOR THE GROUP (A): 1.8960 34.3740 -4.3730
REMARK 3 T TENSOR
REMARK 3 T11: 0.0137 T22: 0.0387
REMARK 3 T33: 0.0372 T12: 0.0031
REMARK 3 T13: 0.0147 T23: 0.0097
REMARK 3 L TENSOR
REMARK 3 L11: 0.2287 L22: 0.2121
REMARK 3 L33: 0.3478 L12: -0.0603
REMARK 3 L13: -0.0079 L23: -0.0843
REMARK 3 S TENSOR
REMARK 3 S11: 0.0013 S12: -0.0441 S13: -0.0043
REMARK 3 S21: 0.0180 S22: 0.0310 S23: 0.0358
REMARK 3 S31: 0.0298 S32: -0.0115 S33: -0.0323
REMARK 3
REMARK 3 TLS GROUP : 6
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : F 11 F 386
REMARK 3 ORIGIN FOR THE GROUP (A): 7.6930 52.7220 -22.1920
REMARK 3 T TENSOR
REMARK 3 T11: 0.0258 T22: 0.0084
REMARK 3 T33: 0.0302 T12: -0.0018
REMARK 3 T13: 0.0168 T23: 0.0037
REMARK 3 L TENSOR
REMARK 3 L11: 0.3062 L22: 0.2861
REMARK 3 L33: 0.4283 L12: -0.0413
REMARK 3 L13: -0.0247 L23: 0.1494
REMARK 3 S TENSOR
REMARK 3 S11: 0.0303 S12: -0.0127 S13: 0.0426
REMARK 3 S21: -0.0458 S22: -0.0137 S23: -0.0016
REMARK 3 S31: -0.0707 S32: 0.0222 S33: -0.0166
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3RMZ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-APR-11.
REMARK 100 THE DEPOSITION ID IS D_1000065131.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 08-MAR-10
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 23-ID-D
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.03315
REMARK 200 MONOCHROMATOR : SI(111) DOUBLE CRYSTAL
REMARK 200 MONOCHROMATOR
REMARK 200 OPTICS : BIOMORPH MIRRORS (KIRKPATRICK
REMARK 200 -BAEZ CONFIGURATION)
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 300 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 173890
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.720
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.4
REMARK 200 DATA REDUNDANCY : 3.800
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.06400
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 18.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.72
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.77
REMARK 200 COMPLETENESS FOR SHELL (%) : 82.7
REMARK 200 DATA REDUNDANCY IN SHELL : 2.80
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.35500
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.800
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: REFMAC 5.5.0109
REMARK 200 STARTING MODEL: PDB ENTRY 3L4M
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 45.89
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.27
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: DROPS CONTAINED 1UL PROTEIN WITH 3UL
REMARK 280 RESERVOIR SOLUTION. PROTEIN SOLUTION: 100UM W199F-MAUG AND 50UM
REMARK 280 PREMADH IN 10MM POTASSIUM PHOSPHATE, PH 7.5. RESERVOIR SOLUTION
REMARK 280 CONTAINED: 22% W/V PEG 8000, 0.1M SODIUM ACETATE, 0.1M MES PH
REMARK 280 6.4, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: HEXAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 26030 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 59750 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -204.0 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 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 GLU A 1
REMARK 465 GLN A 2
REMARK 465 ALA A 3
REMARK 465 ARG A 4
REMARK 465 PRO A 5
REMARK 465 GLU A 360
REMARK 465 SER A 361
REMARK 465 ARG A 362
REMARK 465 ALA A 363
REMARK 465 ALA A 364
REMARK 465 GLN A 365
REMARK 465 LYS A 366
REMARK 465 ASP A 367
REMARK 465 HIS A 368
REMARK 465 HIS A 369
REMARK 465 HIS A 370
REMARK 465 HIS A 371
REMARK 465 HIS A 372
REMARK 465 HIS A 373
REMARK 465 GLU B 1
REMARK 465 GLN B 2
REMARK 465 ALA B 3
REMARK 465 ARG B 4
REMARK 465 PRO B 5
REMARK 465 SER B 361
REMARK 465 ARG B 362
REMARK 465 ALA B 363
REMARK 465 ALA B 364
REMARK 465 GLN B 365
REMARK 465 LYS B 366
REMARK 465 ASP B 367
REMARK 465 HIS B 368
REMARK 465 HIS B 369
REMARK 465 HIS B 370
REMARK 465 HIS B 371
REMARK 465 HIS B 372
REMARK 465 HIS B 373
REMARK 465 ALA C 1
REMARK 465 ASP C 2
REMARK 465 ALA C 3
REMARK 465 PRO C 4
REMARK 465 ALA C 5
REMARK 465 GLY C 6
REMARK 465 GLN D 1
REMARK 465 ASP D 2
REMARK 465 ALA D 3
REMARK 465 PRO D 4
REMARK 465 GLU D 5
REMARK 465 ALA D 6
REMARK 465 GLU D 7
REMARK 465 THR D 8
REMARK 465 GLN D 9
REMARK 465 ALA D 10
REMARK 465 ALA E 1
REMARK 465 ASP E 2
REMARK 465 ALA E 3
REMARK 465 PRO E 4
REMARK 465 ALA E 5
REMARK 465 GLY E 6
REMARK 465 SER E 131
REMARK 465 HIS E 132
REMARK 465 HIS E 133
REMARK 465 HIS E 134
REMARK 465 HIS E 135
REMARK 465 HIS E 136
REMARK 465 HIS E 137
REMARK 465 GLN F 1
REMARK 465 ASP F 2
REMARK 465 ALA F 3
REMARK 465 PRO F 4
REMARK 465 GLU F 5
REMARK 465 ALA F 6
REMARK 465 GLU F 7
REMARK 465 THR F 8
REMARK 465 GLN F 9
REMARK 465 ALA F 10
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 SG CYS A 201 CAB HEC A 600 1.74
REMARK 500 SG CYS B 201 CAB HEC B 600 1.78
REMARK 500 SG CYS B 31 CAB HEC B 500 1.80
REMARK 500 SG CYS A 31 CAB HEC A 500 1.86
REMARK 500 SG CYS A 204 CAC HEC A 600 1.88
REMARK 500 SG CYS A 34 CAC HEC A 500 1.89
REMARK 500 SG CYS B 204 CAC HEC B 600 1.92
REMARK 500 SG CYS B 34 CAC HEC B 500 1.93
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 TYR A 162 CE2 TYR A 162 CD2 0.096
REMARK 500 PHE B 199 CE2 PHE B 199 CD2 0.124
REMARK 500 GLU B 360 CB GLU B 360 CG 0.120
REMARK 500 GLU B 360 CG GLU B 360 CD 0.093
REMARK 500 CYS C 36 CB CYS C 36 SG -0.174
REMARK 500 CYS D 181 CB CYS D 181 SG -0.125
REMARK 500 CYS E 36 CB CYS E 36 SG -0.214
REMARK 500 CYS F 181 CB CYS F 181 SG -0.114
REMARK 500 GLU F 213 CD GLU F 213 OE1 0.089
REMARK 500 PHE F 220 CE2 PHE F 220 CD2 0.123
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ARG A 25 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES
REMARK 500 ASP A 82 CB - CG - OD2 ANGL. DEV. = 5.5 DEGREES
REMARK 500 ASP A 99 CB - CG - OD2 ANGL. DEV. = 6.2 DEGREES
REMARK 500 ASP A 118 CB - CG - OD1 ANGL. DEV. = 7.0 DEGREES
REMARK 500 ARG A 127 NE - CZ - NH1 ANGL. DEV. = -3.5 DEGREES
REMARK 500 ARG A 127 NE - CZ - NH2 ANGL. DEV. = 4.1 DEGREES
REMARK 500 LYS A 142 CD - CE - NZ ANGL. DEV. = 13.9 DEGREES
REMARK 500 ARG A 180 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 ARG A 202 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES
REMARK 500 MET A 206 CG - SD - CE ANGL. DEV. = -15.1 DEGREES
REMARK 500 ARG A 252 NE - CZ - NH2 ANGL. DEV. = -3.6 DEGREES
REMARK 500 ASP A 257 CB - CG - OD1 ANGL. DEV. = 5.7 DEGREES
REMARK 500 ASP A 257 CB - CG - OD2 ANGL. DEV. = -5.7 DEGREES
REMARK 500 MET B 206 CG - SD - CE ANGL. DEV. = -24.6 DEGREES
REMARK 500 ARG B 208 NE - CZ - NH1 ANGL. DEV. = -4.3 DEGREES
REMARK 500 ARG B 252 NE - CZ - NH2 ANGL. DEV. = -3.5 DEGREES
REMARK 500 ARG B 321 NE - CZ - NH1 ANGL. DEV. = -3.4 DEGREES
REMARK 500 ASP C 19 CB - CG - OD1 ANGL. DEV. = 5.6 DEGREES
REMARK 500 ARG D 70 NE - CZ - NH1 ANGL. DEV. = 4.7 DEGREES
REMARK 500 ARG D 101 NE - CZ - NH2 ANGL. DEV. = -3.9 DEGREES
REMARK 500 ARG D 132 NE - CZ - NH2 ANGL. DEV. = -4.1 DEGREES
REMARK 500 ASP D 253 CB - CG - OD1 ANGL. DEV. = 5.5 DEGREES
REMARK 500 LYS D 354 CD - CE - NZ ANGL. DEV. = -16.1 DEGREES
REMARK 500 GLN F 14 CA - CB - CG ANGL. DEV. = 13.9 DEGREES
REMARK 500 ARG F 104 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES
REMARK 500 ARG F 174 NE - CZ - NH2 ANGL. DEV. = -3.6 DEGREES
REMARK 500 ARG F 197 NE - CZ - NH1 ANGL. DEV. = -4.4 DEGREES
REMARK 500 LYS F 236 CD - CE - NZ ANGL. DEV. = 14.0 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 GLN A 60 -40.21 -133.27
REMARK 500 PHE A 92 154.69 79.56
REMARK 500 GLU A 113 -114.31 -121.22
REMARK 500 HIS A 205 41.92 -99.55
REMARK 500 MET A 279 171.15 77.91
REMARK 500 THR A 298 -39.14 -133.06
REMARK 500 PRO A 313 152.10 -48.38
REMARK 500 ALA A 320 49.50 -96.43
REMARK 500 HIS B 35 78.82 -107.74
REMARK 500 PHE B 92 156.85 79.53
REMARK 500 GLU B 113 -109.68 -117.42
REMARK 500 HIS B 205 42.99 -101.53
REMARK 500 PHE B 221 14.99 59.76
REMARK 500 MET B 279 171.44 73.54
REMARK 500 THR B 298 -32.42 -131.91
REMARK 500 ALA B 320 41.25 -97.59
REMARK 500 ASP C 19 108.24 -160.15
REMARK 500 THR C 91 39.20 -142.43
REMARK 500 ALA C 130 172.74 153.28
REMARK 500 HIS C 135 92.28 -162.40
REMARK 500 ILE D 102 -73.94 62.92
REMARK 500 ILE D 102 -82.04 71.56
REMARK 500 LEU D 119 15.08 59.21
REMARK 500 LYS D 173 -64.55 -102.58
REMARK 500 PRO D 179 -166.77 -76.22
REMARK 500 HIS D 183 158.93 67.33
REMARK 500 GLU D 209 149.62 76.91
REMARK 500 TRP D 282 -87.88 -116.68
REMARK 500 ARG D 305 42.20 -106.10
REMARK 500 ASN D 371 -169.47 -103.20
REMARK 500 TRP E 13 123.94 -36.28
REMARK 500 HIS E 28 30.08 -94.92
REMARK 500 THR E 91 36.75 -142.60
REMARK 500 LEU F 80 64.99 37.71
REMARK 500 ILE F 102 -76.91 62.22
REMARK 500 LYS F 173 -63.36 -100.63
REMARK 500 PRO F 179 -163.51 -73.87
REMARK 500 HIS F 183 165.70 65.83
REMARK 500 TRP F 282 -85.09 -122.28
REMARK 500 ARG F 305 42.04 -108.30
REMARK 500 LYS F 354 49.69 38.62
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEC A 500 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 35 NE2
REMARK 620 2 HEC A 500 NA 88.7
REMARK 620 3 HEC A 500 NB 88.7 89.0
REMARK 620 4 HEC A 500 NC 94.2 177.1 90.7
REMARK 620 5 HEC A 500 ND 94.0 90.7 177.3 89.4
REMARK 620 6 HOH A1962 O 170.8 94.8 99.9 82.5 77.4
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 400 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN A 66 OD1
REMARK 620 2 THR A 275 O 145.6
REMARK 620 3 PRO A 277 O 94.0 86.5
REMARK 620 4 HOH A 378 O 75.0 70.7 86.1
REMARK 620 5 HOH A 380 O 74.1 140.1 86.1 147.5
REMARK 620 6 HOH A 387 O 142.2 70.1 102.4 139.2 73.3
REMARK 620 7 HOH A 396 O 85.5 88.3 170.1 84.2 103.3 83.7
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEC A 600 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 205 NE2
REMARK 620 2 HEC A 600 NA 89.8
REMARK 620 3 HEC A 600 NB 89.1 90.1
REMARK 620 4 HEC A 600 NC 90.4 179.5 89.5
REMARK 620 5 HEC A 600 ND 89.9 89.8 179.0 90.6
REMARK 620 6 TYR A 294 OH 176.7 90.6 94.2 89.3 86.9
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA A 401 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN A 231 OD1
REMARK 620 2 THR A 233 OG1 88.1
REMARK 620 3 HOH A 382 O 91.0 78.3
REMARK 620 4 HOH A 492 O 94.0 171.5 93.5
REMARK 620 5 HOH A 854 O 79.4 92.5 167.0 96.0
REMARK 620 6 HOH A 934 O 174.9 93.0 94.1 85.6 95.6
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA A 402 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 LEU A 250 O
REMARK 620 2 ARG A 252 O 91.7
REMARK 620 3 ILE A 255 O 94.7 96.2
REMARK 620 4 HOH A 777 O 177.4 90.7 86.0
REMARK 620 5 HOH A 947 O 97.6 84.4 167.6 81.6
REMARK 620 6 HOH A1611 O 89.7 177.8 85.5 87.9 93.6
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEC B 500 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 35 NE2
REMARK 620 2 HEC B 500 NA 91.1
REMARK 620 3 HEC B 500 NB 89.4 90.2
REMARK 620 4 HEC B 500 NC 91.9 177.0 89.8
REMARK 620 5 HEC B 500 ND 93.8 90.0 176.9 89.9
REMARK 620 6 HOH B1931 O 178.4 90.5 90.5 86.5 86.3
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 400 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN B 66 OD1
REMARK 620 2 THR B 275 O 147.2
REMARK 620 3 PRO B 277 O 92.2 86.6
REMARK 620 4 HOH B 383 O 84.6 91.2 170.3
REMARK 620 5 HOH B 399 O 70.8 141.5 85.6 101.9
REMARK 620 6 HOH B 417 O 138.1 73.4 103.6 84.8 72.1
REMARK 620 7 HOH B 443 O 77.0 70.3 85.4 85.0 146.1 141.9
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEC B 600 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 205 NE2
REMARK 620 2 HEC B 600 NA 88.6
REMARK 620 3 HEC B 600 NB 89.6 89.2
REMARK 620 4 HEC B 600 NC 91.3 179.6 90.4
REMARK 620 5 HEC B 600 ND 89.9 90.2 179.2 90.2
REMARK 620 6 TYR B 294 OH 177.2 91.9 93.2 88.2 87.3
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA B 401 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN B 231 OD1
REMARK 620 2 THR B 233 OG1 85.2
REMARK 620 3 HOH B 411 O 93.1 80.1
REMARK 620 4 HOH B 999 O 172.5 93.9 94.2
REMARK 620 5 HOH B1109 O 78.7 91.0 168.4 93.8
REMARK 620 6 HOH B1146 O 95.1 172.8 92.7 86.7 96.1
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA B 402 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 LEU B 250 O
REMARK 620 2 ARG B 252 O 95.0
REMARK 620 3 ILE B 255 O 93.9 94.5
REMARK 620 4 HOH B 517 O 172.6 92.4 85.2
REMARK 620 5 HOH B 818 O 87.1 177.2 83.4 85.6
REMARK 620 6 HOH B1261 O 100.9 85.2 165.2 80.0 96.3
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 400
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEC A 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEC A 600
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 400
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA B 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEC B 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEC B 600
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PG4 F 387
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE P6G F 388
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 374
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 374
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG D 387
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MES F 389
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT D 388
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3L4M RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE WT-MAUG/PRE-METHYLAMINE DEHYDROGENASE
REMARK 900 COMPLEX
REMARK 900 RELATED ID: 3L4O RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE WT-MAUG/PRE-METHYLAMINE DEHYDROGENASE
REMARK 900 COMPLEX AFTER TREATMENT WITH HYDROGEN PEROXIDE
REMARK 900 RELATED ID: 3ORV RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE Y294H-MAUG/PRE-METHYLAMINE DEHYDROGENASE
REMARK 900 COMPLEX
REMARK 900 RELATED ID: 3RLM RELATED DB: PDB
REMARK 900 RELATED ID: 3RN0 RELATED DB: PDB
REMARK 900 RELATED ID: 3RN1 RELATED DB: PDB
DBREF 3RMZ A 1 367 UNP Q51658 MAUG_PARDP 21 387
DBREF 3RMZ B 1 367 UNP Q51658 MAUG_PARDP 21 387
DBREF 3RMZ C 1 131 UNP A1BBA0 A1BBA0_PARDP 58 188
DBREF 3RMZ D 1 386 UNP A1BB97 A1BB97_PARDP 32 417
DBREF 3RMZ E 1 131 UNP A1BBA0 A1BBA0_PARDP 58 188
DBREF 3RMZ F 1 386 UNP A1BB97 A1BB97_PARDP 32 417
SEQADV 3RMZ PHE A 199 UNP Q51658 TRP 219 ENGINEERED MUTATION
SEQADV 3RMZ HIS A 368 UNP Q51658 EXPRESSION TAG
SEQADV 3RMZ HIS A 369 UNP Q51658 EXPRESSION TAG
SEQADV 3RMZ HIS A 370 UNP Q51658 EXPRESSION TAG
SEQADV 3RMZ HIS A 371 UNP Q51658 EXPRESSION TAG
SEQADV 3RMZ HIS A 372 UNP Q51658 EXPRESSION TAG
SEQADV 3RMZ HIS A 373 UNP Q51658 EXPRESSION TAG
SEQADV 3RMZ PHE B 199 UNP Q51658 TRP 219 ENGINEERED MUTATION
SEQADV 3RMZ HIS B 368 UNP Q51658 EXPRESSION TAG
SEQADV 3RMZ HIS B 369 UNP Q51658 EXPRESSION TAG
SEQADV 3RMZ HIS B 370 UNP Q51658 EXPRESSION TAG
SEQADV 3RMZ HIS B 371 UNP Q51658 EXPRESSION TAG
SEQADV 3RMZ HIS B 372 UNP Q51658 EXPRESSION TAG
SEQADV 3RMZ HIS B 373 UNP Q51658 EXPRESSION TAG
SEQADV 3RMZ HIS C 132 UNP A1BBA0 EXPRESSION TAG
SEQADV 3RMZ HIS C 133 UNP A1BBA0 EXPRESSION TAG
SEQADV 3RMZ HIS C 134 UNP A1BBA0 EXPRESSION TAG
SEQADV 3RMZ HIS C 135 UNP A1BBA0 EXPRESSION TAG
SEQADV 3RMZ HIS C 136 UNP A1BBA0 EXPRESSION TAG
SEQADV 3RMZ HIS C 137 UNP A1BBA0 EXPRESSION TAG
SEQADV 3RMZ HIS E 132 UNP A1BBA0 EXPRESSION TAG
SEQADV 3RMZ HIS E 133 UNP A1BBA0 EXPRESSION TAG
SEQADV 3RMZ HIS E 134 UNP A1BBA0 EXPRESSION TAG
SEQADV 3RMZ HIS E 135 UNP A1BBA0 EXPRESSION TAG
SEQADV 3RMZ HIS E 136 UNP A1BBA0 EXPRESSION TAG
SEQADV 3RMZ HIS E 137 UNP A1BBA0 EXPRESSION TAG
SEQRES 1 A 373 GLU GLN ALA ARG PRO ALA ASP ASP ALA LEU ALA ALA LEU
SEQRES 2 A 373 GLY ALA GLN LEU PHE VAL ASP PRO ALA LEU SER ARG ASN
SEQRES 3 A 373 ALA THR GLN SER CYS ALA THR CYS HIS ASP PRO ALA ARG
SEQRES 4 A 373 ALA PHE THR ASP PRO ARG GLU GLY LYS ALA GLY LEU ALA
SEQRES 5 A 373 VAL SER VAL GLY ASP ASP GLY GLN SER HIS GLY ASP ARG
SEQRES 6 A 373 ASN THR PRO THR LEU GLY TYR ALA ALA LEU VAL PRO ALA
SEQRES 7 A 373 PHE HIS ARG ASP ALA ASN GLY LYS TYR LYS GLY GLY GLN
SEQRES 8 A 373 PHE TRP ASP GLY ARG ALA ASP ASP LEU LYS GLN GLN ALA
SEQRES 9 A 373 GLY GLN PRO MET LEU ASN PRO VAL GLU MET ALA MET PRO
SEQRES 10 A 373 ASP ARG ALA ALA VAL ALA ALA ARG LEU ARG ASP ASP PRO
SEQRES 11 A 373 ALA TYR ARG THR GLY PHE GLU ALA LEU PHE GLY LYS GLY
SEQRES 12 A 373 VAL LEU ASP ASP PRO GLU ARG ALA PHE ASP ALA ALA ALA
SEQRES 13 A 373 GLU ALA LEU ALA ALA TYR GLN ALA THR GLY GLU PHE SER
SEQRES 14 A 373 PRO PHE ASP SER LYS TYR ASP ARG VAL MET ARG GLY GLU
SEQRES 15 A 373 GLU LYS PHE THR PRO LEU GLU GLU PHE GLY TYR THR VAL
SEQRES 16 A 373 PHE ILE THR PHE ASN CYS ARG LEU CYS HIS MET GLN ARG
SEQRES 17 A 373 LYS GLN GLY VAL ALA GLU ARG GLU THR PHE THR ASN PHE
SEQRES 18 A 373 GLU TYR HIS ASN ILE GLY LEU PRO VAL ASN GLU THR ALA
SEQRES 19 A 373 ARG GLU ALA SER GLY LEU GLY ALA ASP HIS VAL ASP HIS
SEQRES 20 A 373 GLY LEU LEU ALA ARG PRO GLY ILE GLU ASP PRO ALA GLN
SEQRES 21 A 373 SER GLY ARG PHE LYS VAL PRO SER LEU ARG ASN VAL ALA
SEQRES 22 A 373 VAL THR GLY PRO TYR MET HIS ASN GLY VAL PHE THR ASP
SEQRES 23 A 373 LEU ARG THR ALA ILE LEU PHE TYR ASN LYS TYR THR SER
SEQRES 24 A 373 ARG ARG PRO GLU ALA LYS ILE ASN PRO GLU THR GLY ALA
SEQRES 25 A 373 PRO TRP GLY GLU PRO GLU VAL ALA ARG ASN LEU SER LEU
SEQRES 26 A 373 ALA GLU LEU GLN SER GLY LEU MET LEU ASP ASP GLY ARG
SEQRES 27 A 373 VAL ASP ALA LEU VAL ALA PHE LEU GLU THR LEU THR ASP
SEQRES 28 A 373 ARG ARG TYR GLU PRO LEU LEU GLU GLU SER ARG ALA ALA
SEQRES 29 A 373 GLN LYS ASP HIS HIS HIS HIS HIS HIS
SEQRES 1 B 373 GLU GLN ALA ARG PRO ALA ASP ASP ALA LEU ALA ALA LEU
SEQRES 2 B 373 GLY ALA GLN LEU PHE VAL ASP PRO ALA LEU SER ARG ASN
SEQRES 3 B 373 ALA THR GLN SER CYS ALA THR CYS HIS ASP PRO ALA ARG
SEQRES 4 B 373 ALA PHE THR ASP PRO ARG GLU GLY LYS ALA GLY LEU ALA
SEQRES 5 B 373 VAL SER VAL GLY ASP ASP GLY GLN SER HIS GLY ASP ARG
SEQRES 6 B 373 ASN THR PRO THR LEU GLY TYR ALA ALA LEU VAL PRO ALA
SEQRES 7 B 373 PHE HIS ARG ASP ALA ASN GLY LYS TYR LYS GLY GLY GLN
SEQRES 8 B 373 PHE TRP ASP GLY ARG ALA ASP ASP LEU LYS GLN GLN ALA
SEQRES 9 B 373 GLY GLN PRO MET LEU ASN PRO VAL GLU MET ALA MET PRO
SEQRES 10 B 373 ASP ARG ALA ALA VAL ALA ALA ARG LEU ARG ASP ASP PRO
SEQRES 11 B 373 ALA TYR ARG THR GLY PHE GLU ALA LEU PHE GLY LYS GLY
SEQRES 12 B 373 VAL LEU ASP ASP PRO GLU ARG ALA PHE ASP ALA ALA ALA
SEQRES 13 B 373 GLU ALA LEU ALA ALA TYR GLN ALA THR GLY GLU PHE SER
SEQRES 14 B 373 PRO PHE ASP SER LYS TYR ASP ARG VAL MET ARG GLY GLU
SEQRES 15 B 373 GLU LYS PHE THR PRO LEU GLU GLU PHE GLY TYR THR VAL
SEQRES 16 B 373 PHE ILE THR PHE ASN CYS ARG LEU CYS HIS MET GLN ARG
SEQRES 17 B 373 LYS GLN GLY VAL ALA GLU ARG GLU THR PHE THR ASN PHE
SEQRES 18 B 373 GLU TYR HIS ASN ILE GLY LEU PRO VAL ASN GLU THR ALA
SEQRES 19 B 373 ARG GLU ALA SER GLY LEU GLY ALA ASP HIS VAL ASP HIS
SEQRES 20 B 373 GLY LEU LEU ALA ARG PRO GLY ILE GLU ASP PRO ALA GLN
SEQRES 21 B 373 SER GLY ARG PHE LYS VAL PRO SER LEU ARG ASN VAL ALA
SEQRES 22 B 373 VAL THR GLY PRO TYR MET HIS ASN GLY VAL PHE THR ASP
SEQRES 23 B 373 LEU ARG THR ALA ILE LEU PHE TYR ASN LYS TYR THR SER
SEQRES 24 B 373 ARG ARG PRO GLU ALA LYS ILE ASN PRO GLU THR GLY ALA
SEQRES 25 B 373 PRO TRP GLY GLU PRO GLU VAL ALA ARG ASN LEU SER LEU
SEQRES 26 B 373 ALA GLU LEU GLN SER GLY LEU MET LEU ASP ASP GLY ARG
SEQRES 27 B 373 VAL ASP ALA LEU VAL ALA PHE LEU GLU THR LEU THR ASP
SEQRES 28 B 373 ARG ARG TYR GLU PRO LEU LEU GLU GLU SER ARG ALA ALA
SEQRES 29 B 373 GLN LYS ASP HIS HIS HIS HIS HIS HIS
SEQRES 1 C 137 ALA ASP ALA PRO ALA GLY THR ASP PRO ARG ALA LYS TRP
SEQRES 2 C 137 VAL PRO GLN ASP ASN ASP ILE GLN ALA CYS ASP TYR TRP
SEQRES 3 C 137 ARG HIS CYS SER ILE ASP GLY ASN ILE CYS ASP CYS SER
SEQRES 4 C 137 GLY GLY SER LEU THR ASN CYS PRO PRO GLY THR LYS LEU
SEQRES 5 C 137 ALA THR ALA SER 0AF VAL ALA SER CYS TYR ASN PRO THR
SEQRES 6 C 137 ASP GLY GLN SER TYR LEU ILE ALA TYR ARG ASP CYS CYS
SEQRES 7 C 137 GLY TYR ASN VAL SER GLY ARG CYS PRO CYS LEU ASN THR
SEQRES 8 C 137 GLU GLY GLU LEU PRO VAL TYR ARG PRO GLU PHE ALA ASN
SEQRES 9 C 137 ASP ILE ILE TRP CYS PHE GLY ALA GLU ASP ASP ALA MET
SEQRES 10 C 137 THR TYR HIS CYS THR ILE SER PRO ILE VAL GLY LYS ALA
SEQRES 11 C 137 SER HIS HIS HIS HIS HIS HIS
SEQRES 1 D 386 GLN ASP ALA PRO GLU ALA GLU THR GLN ALA GLN GLU THR
SEQRES 2 D 386 GLN GLY GLN ALA ALA ALA ARG ALA ALA ALA ALA ASP LEU
SEQRES 3 D 386 ALA ALA GLY GLN ASP ASP GLU PRO ARG ILE LEU GLU ALA
SEQRES 4 D 386 PRO ALA PRO ASP ALA ARG ARG VAL TYR VAL ASN ASP PRO
SEQRES 5 D 386 ALA HIS PHE ALA ALA VAL THR GLN GLN PHE VAL ILE ASP
SEQRES 6 D 386 GLY GLU ALA GLY ARG VAL ILE GLY MET ILE ASP GLY GLY
SEQRES 7 D 386 PHE LEU PRO ASN PRO VAL VAL ALA ASP ASP GLY SER PHE
SEQRES 8 D 386 ILE ALA HIS ALA SER THR VAL PHE SER ARG ILE ALA ARG
SEQRES 9 D 386 GLY GLU ARG THR ASP TYR VAL GLU VAL PHE ASP PRO VAL
SEQRES 10 D 386 THR LEU LEU PRO THR ALA ASP ILE GLU LEU PRO ASP ALA
SEQRES 11 D 386 PRO ARG PHE LEU VAL GLY THR TYR PRO TRP MET THR SER
SEQRES 12 D 386 LEU THR PRO ASP GLY LYS THR LEU LEU PHE TYR GLN PHE
SEQRES 13 D 386 SER PRO ALA PRO ALA VAL GLY VAL VAL ASP LEU GLU GLY
SEQRES 14 D 386 LYS ALA PHE LYS ARG MET LEU ASP VAL PRO ASP CYS TYR
SEQRES 15 D 386 HIS ILE PHE PRO THR ALA PRO ASP THR PHE PHE MET HIS
SEQRES 16 D 386 CYS ARG ASP GLY SER LEU ALA LYS VAL ALA PHE GLY THR
SEQRES 17 D 386 GLU GLY THR PRO GLU ILE THR HIS THR GLU VAL PHE HIS
SEQRES 18 D 386 PRO GLU ASP GLU PHE LEU ILE ASN HIS PRO ALA TYR SER
SEQRES 19 D 386 GLN LYS ALA GLY ARG LEU VAL TRP PRO THR TYR THR GLY
SEQRES 20 D 386 LYS ILE HIS GLN ILE ASP LEU SER SER GLY ASP ALA LYS
SEQRES 21 D 386 PHE LEU PRO ALA VAL GLU ALA LEU THR GLU ALA GLU ARG
SEQRES 22 D 386 ALA ASP GLY TRP ARG PRO GLY GLY TRP GLN GLN VAL ALA
SEQRES 23 D 386 TYR HIS ARG ALA LEU ASP ARG ILE TYR LEU LEU VAL ASP
SEQRES 24 D 386 GLN ARG ASP GLU TRP ARG HIS LYS THR ALA SER ARG PHE
SEQRES 25 D 386 VAL VAL VAL LEU ASP ALA LYS THR GLY GLU ARG LEU ALA
SEQRES 26 D 386 LYS PHE GLU MET GLY HIS GLU ILE ASP SER ILE ASN VAL
SEQRES 27 D 386 SER GLN ASP GLU LYS PRO LEU LEU TYR ALA LEU SER THR
SEQRES 28 D 386 GLY ASP LYS THR LEU TYR ILE HIS ASP ALA GLU SER GLY
SEQRES 29 D 386 GLU GLU LEU ARG SER VAL ASN GLN LEU GLY HIS GLY PRO
SEQRES 30 D 386 GLN VAL ILE THR THR ALA ASP MET GLY
SEQRES 1 E 137 ALA ASP ALA PRO ALA GLY THR ASP PRO ARG ALA LYS TRP
SEQRES 2 E 137 VAL PRO GLN ASP ASN ASP ILE GLN ALA CYS ASP TYR TRP
SEQRES 3 E 137 ARG HIS CYS SER ILE ASP GLY ASN ILE CYS ASP CYS SER
SEQRES 4 E 137 GLY GLY SER LEU THR ASN CYS PRO PRO GLY THR LYS LEU
SEQRES 5 E 137 ALA THR ALA SER 0AF VAL ALA SER CYS TYR ASN PRO THR
SEQRES 6 E 137 ASP GLY GLN SER TYR LEU ILE ALA TYR ARG ASP CYS CYS
SEQRES 7 E 137 GLY TYR ASN VAL SER GLY ARG CYS PRO CYS LEU ASN THR
SEQRES 8 E 137 GLU GLY GLU LEU PRO VAL TYR ARG PRO GLU PHE ALA ASN
SEQRES 9 E 137 ASP ILE ILE TRP CYS PHE GLY ALA GLU ASP ASP ALA MET
SEQRES 10 E 137 THR TYR HIS CYS THR ILE SER PRO ILE VAL GLY LYS ALA
SEQRES 11 E 137 SER HIS HIS HIS HIS HIS HIS
SEQRES 1 F 386 GLN ASP ALA PRO GLU ALA GLU THR GLN ALA GLN GLU THR
SEQRES 2 F 386 GLN GLY GLN ALA ALA ALA ARG ALA ALA ALA ALA ASP LEU
SEQRES 3 F 386 ALA ALA GLY GLN ASP ASP GLU PRO ARG ILE LEU GLU ALA
SEQRES 4 F 386 PRO ALA PRO ASP ALA ARG ARG VAL TYR VAL ASN ASP PRO
SEQRES 5 F 386 ALA HIS PHE ALA ALA VAL THR GLN GLN PHE VAL ILE ASP
SEQRES 6 F 386 GLY GLU ALA GLY ARG VAL ILE GLY MET ILE ASP GLY GLY
SEQRES 7 F 386 PHE LEU PRO ASN PRO VAL VAL ALA ASP ASP GLY SER PHE
SEQRES 8 F 386 ILE ALA HIS ALA SER THR VAL PHE SER ARG ILE ALA ARG
SEQRES 9 F 386 GLY GLU ARG THR ASP TYR VAL GLU VAL PHE ASP PRO VAL
SEQRES 10 F 386 THR LEU LEU PRO THR ALA ASP ILE GLU LEU PRO ASP ALA
SEQRES 11 F 386 PRO ARG PHE LEU VAL GLY THR TYR PRO TRP MET THR SER
SEQRES 12 F 386 LEU THR PRO ASP GLY LYS THR LEU LEU PHE TYR GLN PHE
SEQRES 13 F 386 SER PRO ALA PRO ALA VAL GLY VAL VAL ASP LEU GLU GLY
SEQRES 14 F 386 LYS ALA PHE LYS ARG MET LEU ASP VAL PRO ASP CYS TYR
SEQRES 15 F 386 HIS ILE PHE PRO THR ALA PRO ASP THR PHE PHE MET HIS
SEQRES 16 F 386 CYS ARG ASP GLY SER LEU ALA LYS VAL ALA PHE GLY THR
SEQRES 17 F 386 GLU GLY THR PRO GLU ILE THR HIS THR GLU VAL PHE HIS
SEQRES 18 F 386 PRO GLU ASP GLU PHE LEU ILE ASN HIS PRO ALA TYR SER
SEQRES 19 F 386 GLN LYS ALA GLY ARG LEU VAL TRP PRO THR TYR THR GLY
SEQRES 20 F 386 LYS ILE HIS GLN ILE ASP LEU SER SER GLY ASP ALA LYS
SEQRES 21 F 386 PHE LEU PRO ALA VAL GLU ALA LEU THR GLU ALA GLU ARG
SEQRES 22 F 386 ALA ASP GLY TRP ARG PRO GLY GLY TRP GLN GLN VAL ALA
SEQRES 23 F 386 TYR HIS ARG ALA LEU ASP ARG ILE TYR LEU LEU VAL ASP
SEQRES 24 F 386 GLN ARG ASP GLU TRP ARG HIS LYS THR ALA SER ARG PHE
SEQRES 25 F 386 VAL VAL VAL LEU ASP ALA LYS THR GLY GLU ARG LEU ALA
SEQRES 26 F 386 LYS PHE GLU MET GLY HIS GLU ILE ASP SER ILE ASN VAL
SEQRES 27 F 386 SER GLN ASP GLU LYS PRO LEU LEU TYR ALA LEU SER THR
SEQRES 28 F 386 GLY ASP LYS THR LEU TYR ILE HIS ASP ALA GLU SER GLY
SEQRES 29 F 386 GLU GLU LEU ARG SER VAL ASN GLN LEU GLY HIS GLY PRO
SEQRES 30 F 386 GLN VAL ILE THR THR ALA ASP MET GLY
MODRES 3RMZ 0AF C 57 TRP 7-HYDROXY-L-TRYPTOPHAN
MODRES 3RMZ 0AF E 57 TRP 7-HYDROXY-L-TRYPTOPHAN
HET 0AF C 57 15
HET 0AF E 57 15
HET CA A 400 1
HET NA A 401 1
HET NA A 402 1
HET HEC A 500 43
HET HEC A 600 43
HET EDO A 374 4
HET CA B 400 1
HET NA B 401 1
HET NA B 402 1
HET HEC B 500 43
HET HEC B 600 43
HET EDO B 374 4
HET PEG D 387 7
HET ACT D 388 4
HET PG4 F 387 13
HET P6G F 388 19
HET MES F 389 12
HETNAM 0AF 7-HYDROXY-L-TRYPTOPHAN
HETNAM CA CALCIUM ION
HETNAM NA SODIUM ION
HETNAM HEC HEME C
HETNAM EDO 1,2-ETHANEDIOL
HETNAM PEG DI(HYDROXYETHYL)ETHER
HETNAM ACT ACETATE ION
HETNAM PG4 TETRAETHYLENE GLYCOL
HETNAM P6G HEXAETHYLENE GLYCOL
HETNAM MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID
HETSYN EDO ETHYLENE GLYCOL
HETSYN P6G POLYETHYLENE GLYCOL PEG400
FORMUL 3 0AF 2(C11 H12 N2 O3)
FORMUL 7 CA 2(CA 2+)
FORMUL 8 NA 4(NA 1+)
FORMUL 10 HEC 4(C34 H34 FE N4 O4)
FORMUL 12 EDO 2(C2 H6 O2)
FORMUL 19 PEG C4 H10 O3
FORMUL 20 ACT C2 H3 O2 1-
FORMUL 21 PG4 C8 H18 O5
FORMUL 22 P6G C12 H26 O7
FORMUL 23 MES C6 H13 N O4 S
FORMUL 24 HOH *1876(H2 O)
HELIX 1 1 ALA A 6 VAL A 19 1 14
HELIX 2 2 ASP A 20 SER A 24 5 5
HELIX 3 3 SER A 30 HIS A 35 1 6
HELIX 4 4 ASP A 36 ALA A 40 5 5
HELIX 5 5 TYR A 72 VAL A 76 5 5
HELIX 6 6 ASP A 99 ASN A 110 1 12
HELIX 7 7 ASP A 118 ASP A 128 1 11
HELIX 8 8 ASP A 129 GLY A 141 1 13
HELIX 9 9 GLY A 143 ASP A 146 5 4
HELIX 10 10 ASP A 147 ALA A 164 1 18
HELIX 11 11 SER A 173 ARG A 180 1 8
HELIX 12 12 THR A 186 PHE A 199 1 14
HELIX 13 13 ASN A 200 CYS A 204 5 5
HELIX 14 14 ASN A 231 GLY A 239 1 9
HELIX 15 15 HIS A 247 ARG A 252 5 6
HELIX 16 16 ASP A 257 SER A 261 5 5
HELIX 17 17 ASN A 271 THR A 275 5 5
HELIX 18 18 ASP A 286 ASN A 295 1 10
HELIX 19 19 LYS A 296 THR A 298 5 3
HELIX 20 20 ARG A 301 ILE A 306 5 6
HELIX 21 21 SER A 324 GLN A 329 1 6
HELIX 22 22 ASP A 335 THR A 348 1 14
HELIX 23 23 LEU A 349 THR A 350 5 2
HELIX 24 24 ASP A 351 ARG A 353 5 3
HELIX 25 25 TYR A 354 GLU A 359 1 6
HELIX 26 26 ALA B 6 VAL B 19 1 14
HELIX 27 27 ASP B 20 SER B 24 5 5
HELIX 28 28 SER B 30 HIS B 35 1 6
HELIX 29 29 ASP B 36 ALA B 40 5 5
HELIX 30 30 TYR B 72 VAL B 76 5 5
HELIX 31 31 ASP B 99 GLY B 105 1 7
HELIX 32 32 GLY B 105 ASN B 110 1 6
HELIX 33 33 ASP B 118 ASP B 129 1 12
HELIX 34 34 ASP B 129 GLY B 141 1 13
HELIX 35 35 GLY B 143 ASP B 146 5 4
HELIX 36 36 ASP B 147 ALA B 164 1 18
HELIX 37 37 SER B 173 ARG B 180 1 8
HELIX 38 38 THR B 186 PHE B 199 1 14
HELIX 39 39 ASN B 200 CYS B 204 5 5
HELIX 40 40 ASN B 231 GLY B 239 1 9
HELIX 41 41 HIS B 247 ARG B 252 5 6
HELIX 42 42 ASP B 257 SER B 261 5 5
HELIX 43 43 ASN B 271 THR B 275 5 5
HELIX 44 44 ASP B 286 ASN B 295 1 10
HELIX 45 45 LYS B 296 THR B 298 5 3
HELIX 46 46 ARG B 301 ILE B 306 5 6
HELIX 47 47 SER B 324 GLN B 329 1 6
HELIX 48 48 ASP B 335 THR B 348 1 14
HELIX 49 49 LEU B 349 THR B 350 5 2
HELIX 50 50 ASP B 351 GLU B 359 5 9
HELIX 51 51 TYR C 25 CYS C 29 5 5
HELIX 52 52 CYS C 36 GLY C 40 5 5
HELIX 53 53 ARG C 99 ALA C 103 5 5
HELIX 54 54 ALA C 112 ALA C 116 5 5
HELIX 55 55 THR D 13 GLY D 29 1 17
HELIX 56 56 PRO D 52 ALA D 56 5 5
HELIX 57 57 TYR D 138 TRP D 140 5 3
HELIX 58 58 THR D 269 ASP D 275 1 7
HELIX 59 59 TYR E 25 CYS E 29 5 5
HELIX 60 60 CYS E 36 GLY E 40 5 5
HELIX 61 61 ARG E 99 ALA E 103 5 5
HELIX 62 62 ALA E 112 ALA E 116 5 5
HELIX 63 63 THR F 13 GLY F 29 1 17
HELIX 64 64 PRO F 52 ALA F 56 5 5
HELIX 65 65 TYR F 138 TRP F 140 5 3
HELIX 66 66 THR F 269 ASP F 275 1 7
SHEET 1 A 2 HIS A 80 ARG A 81 0
SHEET 2 A 2 TYR A 87 LYS A 88 -1 O LYS A 88 N HIS A 80
SHEET 1 B 2 TYR A 223 HIS A 224 0
SHEET 2 B 2 PHE A 264 LYS A 265 -1 O PHE A 264 N HIS A 224
SHEET 1 C 2 HIS B 80 ARG B 81 0
SHEET 2 C 2 TYR B 87 LYS B 88 -1 O LYS B 88 N HIS B 80
SHEET 1 D 2 TYR B 223 HIS B 224 0
SHEET 2 D 2 PHE B 264 LYS B 265 -1 O PHE B 264 N HIS B 224
SHEET 1 E 2 ASP C 32 ASN C 34 0
SHEET 2 E 2 PRO C 87 LEU C 89 -1 O CYS C 88 N GLY C 33
SHEET 1 F 3 LYS C 51 LEU C 52 0
SHEET 2 F 3 GLN C 68 CYS C 78 -1 O CYS C 78 N LYS C 51
SHEET 3 F 3 TYR C 119 ILE C 123 -1 O CYS C 121 N CYS C 77
SHEET 1 G 3 0AF C 57 ASN C 63 0
SHEET 2 G 3 GLN C 68 CYS C 78 -1 O TYR C 70 N CYS C 61
SHEET 3 G 3 ILE C 126 GLY C 128 -1 O VAL C 127 N LEU C 71
SHEET 1 H 4 ARG D 70 GLY D 77 0
SHEET 2 H 4 THR D 59 ASP D 65 -1 N VAL D 63 O GLY D 73
SHEET 3 H 4 ARG D 46 ASP D 51 -1 N VAL D 49 O PHE D 62
SHEET 4 H 4 VAL D 379 THR D 381 -1 O VAL D 379 N ASN D 50
SHEET 1 I 4 ASN D 82 VAL D 85 0
SHEET 2 I 4 ILE D 92 ARG D 101 -1 O ALA D 93 N VAL D 84
SHEET 3 I 4 ARG D 104 PHE D 114 -1 O PHE D 114 N ILE D 92
SHEET 4 I 4 PRO D 121 LEU D 127 -1 O ILE D 125 N VAL D 111
SHEET 1 J 4 THR D 142 LEU D 144 0
SHEET 2 J 4 THR D 150 GLN D 155 -1 O LEU D 152 N SER D 143
SHEET 3 J 4 ALA D 161 ASP D 166 -1 O GLY D 163 N PHE D 153
SHEET 4 J 4 ALA D 171 ASP D 177 -1 O LEU D 176 N VAL D 162
SHEET 1 K 4 CYS D 181 ALA D 188 0
SHEET 2 K 4 THR D 191 CYS D 196 -1 O THR D 191 N THR D 187
SHEET 3 K 4 LEU D 201 ALA D 205 -1 O VAL D 204 N PHE D 192
SHEET 4 K 4 GLU D 213 HIS D 216 -1 O THR D 215 N LYS D 203
SHEET 1 L 4 ALA D 232 SER D 234 0
SHEET 2 L 4 ARG D 239 PRO D 243 -1 O VAL D 241 N ALA D 232
SHEET 3 L 4 LYS D 248 ASP D 253 -1 O HIS D 250 N TRP D 242
SHEET 4 L 4 LYS D 260 PHE D 261 -1 O LYS D 260 N ASP D 253
SHEET 1 M 4 ALA D 232 SER D 234 0
SHEET 2 M 4 ARG D 239 PRO D 243 -1 O VAL D 241 N ALA D 232
SHEET 3 M 4 LYS D 248 ASP D 253 -1 O HIS D 250 N TRP D 242
SHEET 4 M 4 VAL D 265 GLU D 266 -1 O VAL D 265 N ILE D 249
SHEET 1 N 3 TRP D 277 PRO D 279 0
SHEET 2 N 3 ARG D 293 GLN D 300 -1 O ASP D 299 N ARG D 278
SHEET 3 N 3 VAL D 285 HIS D 288 -1 N HIS D 288 O ARG D 293
SHEET 1 O 4 TRP D 277 PRO D 279 0
SHEET 2 O 4 ARG D 293 GLN D 300 -1 O ASP D 299 N ARG D 278
SHEET 3 O 4 SER D 310 ASP D 317 -1 O VAL D 314 N LEU D 296
SHEET 4 O 4 ARG D 323 ILE D 333 -1 O ILE D 333 N SER D 310
SHEET 1 P 4 SER D 335 VAL D 338 0
SHEET 2 P 4 LEU D 345 SER D 350 -1 O LEU D 349 N SER D 335
SHEET 3 P 4 THR D 355 ASP D 360 -1 O HIS D 359 N LEU D 346
SHEET 4 P 4 GLU D 366 VAL D 370 -1 O LEU D 367 N ILE D 358
SHEET 1 Q 2 ASP E 32 ASN E 34 0
SHEET 2 Q 2 PRO E 87 LEU E 89 -1 O CYS E 88 N GLY E 33
SHEET 1 R 3 LYS E 51 LEU E 52 0
SHEET 2 R 3 SER E 69 CYS E 78 -1 O CYS E 78 N LYS E 51
SHEET 3 R 3 TYR E 119 ILE E 123 -1 O CYS E 121 N CYS E 77
SHEET 1 S 3 0AF E 57 TYR E 62 0
SHEET 2 S 3 SER E 69 CYS E 78 -1 O TYR E 70 N CYS E 61
SHEET 3 S 3 ILE E 126 LYS E 129 -1 O VAL E 127 N LEU E 71
SHEET 1 T 4 ARG F 70 GLY F 77 0
SHEET 2 T 4 THR F 59 ASP F 65 -1 N VAL F 63 O GLY F 73
SHEET 3 T 4 ARG F 46 ASP F 51 -1 N VAL F 47 O ILE F 64
SHEET 4 T 4 VAL F 379 THR F 381 -1 O VAL F 379 N ASN F 50
SHEET 1 U 4 ASN F 82 VAL F 85 0
SHEET 2 U 4 ILE F 92 ARG F 101 -1 O ALA F 93 N VAL F 84
SHEET 3 U 4 ARG F 104 PHE F 114 -1 O TYR F 110 N SER F 96
SHEET 4 U 4 PRO F 121 LEU F 127 -1 O THR F 122 N VAL F 113
SHEET 1 V 4 THR F 142 LEU F 144 0
SHEET 2 V 4 THR F 150 GLN F 155 -1 O LEU F 152 N SER F 143
SHEET 3 V 4 ALA F 161 ASP F 166 -1 O GLY F 163 N PHE F 153
SHEET 4 V 4 ALA F 171 ASP F 177 -1 O ARG F 174 N VAL F 164
SHEET 1 W 4 CYS F 181 ALA F 188 0
SHEET 2 W 4 THR F 191 CYS F 196 -1 O HIS F 195 N TYR F 182
SHEET 3 W 4 LEU F 201 ALA F 205 -1 O VAL F 204 N PHE F 192
SHEET 4 W 4 GLU F 213 HIS F 216 -1 O THR F 215 N LYS F 203
SHEET 1 X 4 ALA F 232 SER F 234 0
SHEET 2 X 4 ARG F 239 PRO F 243 -1 O VAL F 241 N ALA F 232
SHEET 3 X 4 LYS F 248 ASP F 253 -1 O HIS F 250 N TRP F 242
SHEET 4 X 4 LYS F 260 PHE F 261 -1 O LYS F 260 N ASP F 253
SHEET 1 Y 4 ALA F 232 SER F 234 0
SHEET 2 Y 4 ARG F 239 PRO F 243 -1 O VAL F 241 N ALA F 232
SHEET 3 Y 4 LYS F 248 ASP F 253 -1 O HIS F 250 N TRP F 242
SHEET 4 Y 4 VAL F 265 GLU F 266 -1 O VAL F 265 N ILE F 249
SHEET 1 Z 3 TRP F 277 PRO F 279 0
SHEET 2 Z 3 ARG F 293 GLN F 300 -1 O ASP F 299 N ARG F 278
SHEET 3 Z 3 VAL F 285 HIS F 288 -1 N HIS F 288 O ARG F 293
SHEET 1 AA 4 TRP F 277 PRO F 279 0
SHEET 2 AA 4 ARG F 293 GLN F 300 -1 O ASP F 299 N ARG F 278
SHEET 3 AA 4 SER F 310 ASP F 317 -1 O LEU F 316 N ILE F 294
SHEET 4 AA 4 ARG F 323 ILE F 333 -1 O LEU F 324 N VAL F 315
SHEET 1 AB 4 SER F 335 VAL F 338 0
SHEET 2 AB 4 LEU F 345 SER F 350 -1 O LEU F 349 N SER F 335
SHEET 3 AB 4 THR F 355 ASP F 360 -1 O TYR F 357 N ALA F 348
SHEET 4 AB 4 GLU F 366 VAL F 370 -1 O VAL F 370 N LEU F 356
SSBOND 1 CYS C 23 CYS C 88 1555 1555 2.11
SSBOND 2 CYS C 29 CYS C 61 1555 1555 2.14
SSBOND 3 CYS C 36 CYS C 121 1555 1555 2.08
SSBOND 4 CYS C 38 CYS C 86 1555 1555 2.13
SSBOND 5 CYS C 46 CYS C 77 1555 1555 1.99
SSBOND 6 CYS C 78 CYS C 109 1555 1555 2.05
SSBOND 7 CYS D 181 CYS D 196 1555 1555 2.22
SSBOND 8 CYS E 23 CYS E 88 1555 1555 2.09
SSBOND 9 CYS E 29 CYS E 61 1555 1555 2.16
SSBOND 10 CYS E 36 CYS E 121 1555 1555 2.08
SSBOND 11 CYS E 38 CYS E 86 1555 1555 2.09
SSBOND 12 CYS E 46 CYS E 77 1555 1555 1.96
SSBOND 13 CYS E 78 CYS E 109 1555 1555 2.06
SSBOND 14 CYS F 181 CYS F 196 1555 1555 2.25
LINK C 0AF C 57 N VAL C 58 1555 1555 1.34
LINK C 0AF E 57 N VAL E 58 1555 1555 1.34
LINK NE2 HIS A 35 FE HEC A 500 1555 1555 2.14
LINK OD1 ASN A 66 CA CA A 400 1555 1555 2.33
LINK NE2 HIS A 205 FE HEC A 600 1555 1555 2.06
LINK OD1 ASN A 231 NA NA A 401 1555 1555 2.36
LINK OG1 THR A 233 NA NA A 401 1555 1555 2.43
LINK O LEU A 250 NA NA A 402 1555 1555 2.32
LINK O ARG A 252 NA NA A 402 1555 1555 2.63
LINK O ILE A 255 NA NA A 402 1555 1555 2.40
LINK O THR A 275 CA CA A 400 1555 1555 2.44
LINK O PRO A 277 CA CA A 400 1555 1555 2.31
LINK OH TYR A 294 FE HEC A 600 1555 1555 1.95
LINK O HOH A 378 CA CA A 400 1555 1555 2.52
LINK O HOH A 380 CA CA A 400 1555 1555 2.39
LINK O HOH A 382 NA NA A 401 1555 1555 2.45
LINK O HOH A 387 CA CA A 400 1555 1555 2.37
LINK O HOH A 396 CA CA A 400 1555 1555 2.29
LINK NA NA A 401 O HOH A 492 1555 1555 2.45
LINK NA NA A 401 O HOH A 854 1555 1555 2.37
LINK NA NA A 401 O HOH A 934 1555 1555 2.29
LINK NA NA A 402 O HOH A 777 1555 1555 2.72
LINK NA NA A 402 O HOH A 947 1555 1555 2.50
LINK NA NA A 402 O HOH A1611 1555 1555 2.37
LINK FE HEC A 500 O HOH A1962 1555 1555 2.48
LINK NE2 HIS B 35 FE HEC B 500 1555 1555 2.13
LINK OD1 ASN B 66 CA CA B 400 1555 1555 2.37
LINK NE2 HIS B 205 FE HEC B 600 1555 1555 2.00
LINK OD1 ASN B 231 NA NA B 401 1555 1555 2.36
LINK OG1 THR B 233 NA NA B 401 1555 1555 2.42
LINK O LEU B 250 NA NA B 402 1555 1555 2.37
LINK O ARG B 252 NA NA B 402 1555 1555 2.58
LINK O ILE B 255 NA NA B 402 1555 1555 2.37
LINK O THR B 275 CA CA B 400 1555 1555 2.41
LINK O PRO B 277 CA CA B 400 1555 1555 2.26
LINK OH TYR B 294 FE HEC B 600 1555 1555 1.91
LINK O HOH B 383 CA CA B 400 1555 1555 2.26
LINK O HOH B 399 CA CA B 400 1555 1555 2.45
LINK CA CA B 400 O HOH B 417 1555 1555 2.35
LINK CA CA B 400 O HOH B 443 1555 1555 2.50
LINK NA NA B 401 O HOH B 411 1555 1555 2.44
LINK NA NA B 401 O HOH B 999 1555 1555 2.42
LINK NA NA B 401 O HOH B1109 1555 1555 2.35
LINK NA NA B 401 O HOH B1146 1555 1555 2.43
LINK NA NA B 402 O HOH B 517 1555 1555 2.48
LINK NA NA B 402 O HOH B 818 1555 1555 2.41
LINK NA NA B 402 O HOH B1261 1555 1555 2.40
LINK FE HEC B 500 O HOH B1931 1555 1555 2.21
CISPEP 1 GLY A 276 PRO A 277 0 -1.89
CISPEP 2 GLY B 276 PRO B 277 0 -9.21
CISPEP 3 SER D 157 PRO D 158 0 1.44
CISPEP 4 SER F 157 PRO F 158 0 4.36
SITE 1 AC1 7 ASN A 66 THR A 275 PRO A 277 HOH A 378
SITE 2 AC1 7 HOH A 380 HOH A 387 HOH A 396
SITE 1 AC2 6 ASN A 231 THR A 233 HOH A 382 HOH A 492
SITE 2 AC2 6 HOH A 854 HOH A 934
SITE 1 AC3 6 LEU A 250 ARG A 252 ILE A 255 HOH A 777
SITE 2 AC3 6 HOH A 947 HOH A1611
SITE 1 AC4 28 GLN A 29 SER A 30 CYS A 31 CYS A 34
SITE 2 AC4 28 HIS A 35 VAL A 55 ARG A 65 THR A 67
SITE 3 AC4 28 PRO A 68 LEU A 70 GLN A 91 PHE A 92
SITE 4 AC4 28 TRP A 93 ARG A 96 LEU A 100 GLN A 103
SITE 5 AC4 28 ALA A 104 PRO A 107 GLU A 113 MET A 114
SITE 6 AC4 28 GLN A 163 LYS A 265 HOH A 444 HOH A 530
SITE 7 AC4 28 HOH A1195 HOH A1350 HOH A1962 HOH A1966
SITE 1 AC5 22 TRP A 93 ASN A 200 CYS A 201 CYS A 204
SITE 2 AC5 22 HIS A 205 HIS A 224 LEU A 228 PHE A 264
SITE 3 AC5 22 PRO A 267 LEU A 269 TYR A 278 MET A 279
SITE 4 AC5 22 HIS A 280 LEU A 287 TYR A 294 SER A 324
SITE 5 AC5 22 GLU A 327 HOH A 380 HOH A 387 HOH A 426
SITE 6 AC5 22 HOH A 442 HOH A 456
SITE 1 AC6 7 ASN B 66 THR B 275 PRO B 277 HOH B 383
SITE 2 AC6 7 HOH B 399 HOH B 417 HOH B 443
SITE 1 AC7 6 ASN B 231 THR B 233 HOH B 411 HOH B 999
SITE 2 AC7 6 HOH B1109 HOH B1146
SITE 1 AC8 6 LEU B 250 ARG B 252 ILE B 255 HOH B 517
SITE 2 AC8 6 HOH B 818 HOH B1261
SITE 1 AC9 25 GLN B 29 SER B 30 CYS B 31 CYS B 34
SITE 2 AC9 25 HIS B 35 ARG B 65 THR B 67 PRO B 68
SITE 3 AC9 25 LEU B 70 GLN B 91 PHE B 92 TRP B 93
SITE 4 AC9 25 ARG B 96 LEU B 100 GLN B 103 ALA B 104
SITE 5 AC9 25 PRO B 107 MET B 114 GLN B 163 LYS B 265
SITE 6 AC9 25 HOH B 549 HOH B 605 HOH B 770 HOH B 901
SITE 7 AC9 25 HOH B1931
SITE 1 BC1 22 TRP B 93 ASN B 200 CYS B 201 CYS B 204
SITE 2 BC1 22 HIS B 205 HIS B 224 LEU B 228 PHE B 264
SITE 3 BC1 22 PRO B 267 LEU B 269 TYR B 278 MET B 279
SITE 4 BC1 22 HIS B 280 LEU B 287 TYR B 294 SER B 324
SITE 5 BC1 22 GLU B 327 HOH B 375 HOH B 399 HOH B 417
SITE 6 BC1 22 HOH B 423 HOH B 430
SITE 1 BC2 8 THR F 187 LYS F 236 LEU F 254 SER F 255
SITE 2 BC2 8 SER F 256 GLY F 257 HOH F 851 HOH F 990
SITE 1 BC3 8 ARG A 25 ARG A 125 ASP A 128 GLU F 218
SITE 2 BC3 8 VAL F 219 PHE F 261 HOH F 903 HOH F1748
SITE 1 BC4 2 ALA A 164 ARG A 215
SITE 1 BC5 2 ALA B 164 ARG B 215
SITE 1 BC6 8 THR D 187 GLN D 235 LYS D 236 ALA D 237
SITE 2 BC6 8 GLY D 238 LEU D 254 SER D 255 HOH D1956
SITE 1 BC7 10 GLU B 137 ALA B 138 LEU B 139 PHE B 140
SITE 2 BC7 10 GLY B 141 ARG F 35 LEU F 37 GLU F 38
SITE 3 BC7 10 HOH F 502 HOH F1843
SITE 1 BC8 5 ARG D 35 LEU D 37 GLU D 38 HOH D 477
SITE 2 BC8 5 HOH D1158
CRYST1 55.527 83.524 107.782 109.94 91.54 105.78 P 1 2
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 0.018009 0.005088 0.002497 0.00000
SCALE2 0.000000 0.012441 0.004834 0.00000
SCALE3 0.000000 0.000000 0.009957 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
