HEADER FAD-BINDING PROTEIN 24-DEC-08 2ZXH
TITLE STRUCTURE OF AQUIFEX AEOLICUS GIDA IN THE FORM I CRYSTAL
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TRNA URIDINE 5-CARBOXYMETHYLAMINOMETHYL MODIFICATION ENZYME
COMPND 3 MNMG;
COMPND 4 CHAIN: A, B;
COMPND 5 SYNONYM: GIDA, GLUCOSE-INHIBITED DIVISION PROTEIN A;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: AQUIFEX AEOLICUS;
SOURCE 3 ORGANISM_TAXID: 63363;
SOURCE 4 GENE: AQ_761;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21-CODONPLUS (DE3)-RIL;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET28B
KEYWDS 5-CARBOXYMETHYLAMINOMETHYLURIDINE, MODIFICATION, TRNA, WOBBLE
KEYWDS 2 URIDINE, FAD, FAD-BINDING PROTEIN, TRNA MODIFICATION ENZYME
EXPDTA X-RAY DIFFRACTION
AUTHOR T.NUMATA,T.OSAWA
REVDAT 3 13-MAR-24 2ZXH 1 REMARK SEQADV
REVDAT 2 04-APR-12 2ZXH 1 JRNL VERSN
REVDAT 1 19-MAY-09 2ZXH 0
JRNL AUTH T.OSAWA,K.ITO,H.INANAGA,O.NUREKI,K.TOMITA,T.NUMATA
JRNL TITL CONSERVED CYSTEINE RESIDUES OF GIDA ARE ESSENTIAL FOR
JRNL TITL 2 BIOGENESIS OF 5-CARBOXYMETHYLAMINOMETHYLURIDINE AT TRNA
JRNL TITL 3 ANTICODON
JRNL REF STRUCTURE V. 17 713 2009
JRNL REFN ISSN 0969-2126
JRNL PMID 19446527
JRNL DOI 10.1016/J.STR.2009.03.013
REMARK 2
REMARK 2 RESOLUTION. 3.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.2
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.97
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 46244.260
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 98.0
REMARK 3 NUMBER OF REFLECTIONS : 78176
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.242
REMARK 3 FREE R VALUE : 0.271
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT : 3800
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.004
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 3.20
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.40
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 92.70
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 11795
REMARK 3 BIN R VALUE (WORKING SET) : 0.4290
REMARK 3 BIN FREE R VALUE : 0.4180
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.60
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 574
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.017
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 9593
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 121
REMARK 3 SOLVENT ATOMS : 0
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 71.10
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 24.26000
REMARK 3 B22 (A**2) : 0.56000
REMARK 3 B33 (A**2) : -24.83000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.47
REMARK 3 ESD FROM SIGMAA (A) : 1.15
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.51
REMARK 3 ESD FROM C-V SIGMAA (A) : 1.10
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.009
REMARK 3 BOND ANGLES (DEGREES) : 1.400
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 22.90
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.910
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 4.050 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 6.440 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 5.970 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 8.750 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.25
REMARK 3 BSOL : -1.81
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : FAD.PARAM
REMARK 3 PARAMETER FILE 2 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 3 : ION.PARAM
REMARK 3 PARAMETER FILE 4 : NULL
REMARK 3 TOPOLOGY FILE 1 : FAD.TOP
REMARK 3 TOPOLOGY FILE 2 : PROTEIN_REP.TOP
REMARK 3 TOPOLOGY FILE 3 : ION.TOP
REMARK 3 TOPOLOGY FILE 4 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: BULK SOLVENT MODEL USED, THE FILE
REMARK 3 CONTAINS FRIEDEL PAIRS.
REMARK 4
REMARK 4 2ZXH COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 25-DEC-08.
REMARK 100 THE DEPOSITION ID IS D_1000028548.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 21-MAY-08
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.9
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PHOTON FACTORY
REMARK 200 BEAMLINE : AR-NW12A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97928
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 78176
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.200
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 200 DATA REDUNDANCY : 8.000
REMARK 200 R MERGE (I) : 0.12600
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.26
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.3
REMARK 200 DATA REDUNDANCY IN SHELL : 5.10
REMARK 200 R MERGE FOR SHELL (I) : 0.39800
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.200
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: SNB
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: THE FILE CONTAINS FRIEDEL PAIRS.
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 71.86
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.37
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.0M SODIUM/POTASSIUM PHOSPHATE, PH
REMARK 280 6.9, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z+1/2
REMARK 290 6555 -X,-Y+1/2,Z
REMARK 290 7555 -X+1/2,Y,-Z
REMARK 290 8555 X,-Y,-Z+1/2
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 50.81900
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 115.86850
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 106.63600
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 115.86850
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 50.81900
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 106.63600
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 50.81900
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 106.63600
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 115.86850
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 106.63600
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 50.81900
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 115.86850
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 8360 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 46020 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -57.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A -19
REMARK 465 GLY A -18
REMARK 465 SER A -17
REMARK 465 SER A -16
REMARK 465 HIS A -15
REMARK 465 HIS A -14
REMARK 465 HIS A -13
REMARK 465 HIS A -12
REMARK 465 HIS A -11
REMARK 465 HIS A -10
REMARK 465 SER A -9
REMARK 465 SER A -8
REMARK 465 GLY A -7
REMARK 465 LEU A -6
REMARK 465 VAL A -5
REMARK 465 PRO A -4
REMARK 465 ALA A -3
REMARK 465 GLY A -2
REMARK 465 SER A -1
REMARK 465 HIS A 0
REMARK 465 MET A 1
REMARK 465 ALA A 2
REMARK 465 TRP A 3
REMARK 465 VAL A 4
REMARK 465 VAL A 5
REMARK 465 SER A 493
REMARK 465 VAL A 494
REMARK 465 ALA A 495
REMARK 465 VAL A 496
REMARK 465 GLY A 497
REMARK 465 GLY A 498
REMARK 465 ASP A 499
REMARK 465 THR A 500
REMARK 465 ASP A 617
REMARK 465 MET B -19
REMARK 465 GLY B -18
REMARK 465 SER B -17
REMARK 465 SER B -16
REMARK 465 HIS B -15
REMARK 465 HIS B -14
REMARK 465 HIS B -13
REMARK 465 HIS B -12
REMARK 465 HIS B -11
REMARK 465 HIS B -10
REMARK 465 SER B -9
REMARK 465 SER B -8
REMARK 465 GLY B -7
REMARK 465 LEU B -6
REMARK 465 VAL B -5
REMARK 465 PRO B -4
REMARK 465 ALA B -3
REMARK 465 GLY B -2
REMARK 465 SER B -1
REMARK 465 HIS B 0
REMARK 465 MET B 1
REMARK 465 ALA B 2
REMARK 465 TRP B 3
REMARK 465 VAL B 4
REMARK 465 VAL B 5
REMARK 465 SER B 493
REMARK 465 VAL B 494
REMARK 465 ALA B 495
REMARK 465 VAL B 496
REMARK 465 GLY B 497
REMARK 465 GLY B 498
REMARK 465 ASP B 499
REMARK 465 THR B 500
REMARK 465 LYS B 615
REMARK 465 LEU B 616
REMARK 465 ASP B 617
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 VAL A 492 CG1 CG2
REMARK 470 ARG A 501 CG CD NE CZ NH1 NH2
REMARK 470 SER A 502 OG
REMARK 470 ARG B 501 CG CD NE CZ NH1 NH2
REMARK 470 SER B 502 OG
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 OE1 GLU B 107 OE1 GLU B 107 8565 1.59
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 PRO B 527 C - N - CA ANGL. DEV. = 9.7 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 ILE A 20 -72.36 -48.65
REMARK 500 CYS A 48 -122.34 -115.78
REMARK 500 PRO A 50 28.53 -77.50
REMARK 500 ILE A 55 -74.57 -32.00
REMARK 500 MET A 71 -32.64 -24.93
REMARK 500 GLN A 81 96.53 176.83
REMARK 500 LYS A 83 154.83 169.38
REMARK 500 ASN A 86 61.33 62.78
REMARK 500 ARG A 88 38.74 -90.25
REMARK 500 ASN A 118 -2.95 71.72
REMARK 500 GLN A 123 69.42 -104.98
REMARK 500 THR A 155 54.50 -152.57
REMARK 500 THR A 158 38.13 -80.14
REMARK 500 LEU A 160 109.83 -44.88
REMARK 500 PRO A 179 -159.55 -77.35
REMARK 500 GLU A 182 -45.64 -133.58
REMARK 500 ASP A 192 33.47 77.37
REMARK 500 ALA A 204 -165.69 -70.03
REMARK 500 PHE A 213 36.91 -88.54
REMARK 500 ALA A 215 45.91 -85.92
REMARK 500 GLU A 217 -179.66 -57.69
REMARK 500 ALA A 219 78.04 -112.87
REMARK 500 THR A 232 -169.61 -75.51
REMARK 500 LYS A 242 144.11 -39.39
REMARK 500 THR A 254 -176.74 -64.66
REMARK 500 ALA A 270 1.16 -67.40
REMARK 500 LEU A 275 76.52 -103.96
REMARK 500 ARG A 282 40.05 -104.32
REMARK 500 PRO A 285 -87.49 -64.13
REMARK 500 LYS A 290 -18.93 -42.85
REMARK 500 PRO A 295 5.50 -50.91
REMARK 500 LEU A 319 34.38 -152.71
REMARK 500 PRO A 356 119.69 -31.87
REMARK 500 PHE A 436 26.12 -70.46
REMARK 500 TYR A 442 43.38 -142.34
REMARK 500 ILE A 446 78.47 -108.73
REMARK 500 ASP A 449 -50.56 -138.21
REMARK 500 LEU A 515 7.95 -64.07
REMARK 500 GLU A 520 -67.58 -91.48
REMARK 500 PRO A 530 -48.64 -22.77
REMARK 500 GLN A 539 -33.90 -38.59
REMARK 500 LEU A 552 -8.44 -55.29
REMARK 500 GLU A 560 -15.09 -49.09
REMARK 500 TYR A 570 20.78 -70.76
REMARK 500 THR A 577 141.75 -27.93
REMARK 500 LYS A 588 49.04 35.31
REMARK 500 LYS A 615 -69.64 -133.98
REMARK 500 ILE B 20 -72.60 -47.99
REMARK 500 CYS B 48 -123.59 -115.29
REMARK 500 PRO B 50 23.80 -74.92
REMARK 500
REMARK 500 THIS ENTRY HAS 89 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD A 618
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD B 618
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 619
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 620
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 B 619
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2ZXI RELATED DB: PDB
DBREF 2ZXH A 1 617 UNP O66962 MNMG_AQUAE 1 617
DBREF 2ZXH B 1 617 UNP O66962 MNMG_AQUAE 1 617
SEQADV 2ZXH MET A -19 UNP O66962 EXPRESSION TAG
SEQADV 2ZXH GLY A -18 UNP O66962 EXPRESSION TAG
SEQADV 2ZXH SER A -17 UNP O66962 EXPRESSION TAG
SEQADV 2ZXH SER A -16 UNP O66962 EXPRESSION TAG
SEQADV 2ZXH HIS A -15 UNP O66962 EXPRESSION TAG
SEQADV 2ZXH HIS A -14 UNP O66962 EXPRESSION TAG
SEQADV 2ZXH HIS A -13 UNP O66962 EXPRESSION TAG
SEQADV 2ZXH HIS A -12 UNP O66962 EXPRESSION TAG
SEQADV 2ZXH HIS A -11 UNP O66962 EXPRESSION TAG
SEQADV 2ZXH HIS A -10 UNP O66962 EXPRESSION TAG
SEQADV 2ZXH SER A -9 UNP O66962 EXPRESSION TAG
SEQADV 2ZXH SER A -8 UNP O66962 EXPRESSION TAG
SEQADV 2ZXH GLY A -7 UNP O66962 EXPRESSION TAG
SEQADV 2ZXH LEU A -6 UNP O66962 EXPRESSION TAG
SEQADV 2ZXH VAL A -5 UNP O66962 EXPRESSION TAG
SEQADV 2ZXH PRO A -4 UNP O66962 EXPRESSION TAG
SEQADV 2ZXH ALA A -3 UNP O66962 EXPRESSION TAG
SEQADV 2ZXH GLY A -2 UNP O66962 EXPRESSION TAG
SEQADV 2ZXH SER A -1 UNP O66962 EXPRESSION TAG
SEQADV 2ZXH HIS A 0 UNP O66962 EXPRESSION TAG
SEQADV 2ZXH MET B -19 UNP O66962 EXPRESSION TAG
SEQADV 2ZXH GLY B -18 UNP O66962 EXPRESSION TAG
SEQADV 2ZXH SER B -17 UNP O66962 EXPRESSION TAG
SEQADV 2ZXH SER B -16 UNP O66962 EXPRESSION TAG
SEQADV 2ZXH HIS B -15 UNP O66962 EXPRESSION TAG
SEQADV 2ZXH HIS B -14 UNP O66962 EXPRESSION TAG
SEQADV 2ZXH HIS B -13 UNP O66962 EXPRESSION TAG
SEQADV 2ZXH HIS B -12 UNP O66962 EXPRESSION TAG
SEQADV 2ZXH HIS B -11 UNP O66962 EXPRESSION TAG
SEQADV 2ZXH HIS B -10 UNP O66962 EXPRESSION TAG
SEQADV 2ZXH SER B -9 UNP O66962 EXPRESSION TAG
SEQADV 2ZXH SER B -8 UNP O66962 EXPRESSION TAG
SEQADV 2ZXH GLY B -7 UNP O66962 EXPRESSION TAG
SEQADV 2ZXH LEU B -6 UNP O66962 EXPRESSION TAG
SEQADV 2ZXH VAL B -5 UNP O66962 EXPRESSION TAG
SEQADV 2ZXH PRO B -4 UNP O66962 EXPRESSION TAG
SEQADV 2ZXH ALA B -3 UNP O66962 EXPRESSION TAG
SEQADV 2ZXH GLY B -2 UNP O66962 EXPRESSION TAG
SEQADV 2ZXH SER B -1 UNP O66962 EXPRESSION TAG
SEQADV 2ZXH HIS B 0 UNP O66962 EXPRESSION TAG
SEQRES 1 A 637 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 A 637 LEU VAL PRO ALA GLY SER HIS MET ALA TRP VAL VAL ASP
SEQRES 3 A 637 GLU PHE ASP VAL VAL VAL ILE GLY GLY GLY HIS ALA GLY
SEQRES 4 A 637 ILE GLU ALA ALA LEU ALA ALA ALA ARG MET GLY ALA LYS
SEQRES 5 A 637 THR ALA MET PHE VAL LEU ASN ALA ASP THR ILE GLY GLN
SEQRES 6 A 637 MET SER CYS ASN PRO ALA ILE GLY GLY ILE ALA LYS GLY
SEQRES 7 A 637 ILE VAL VAL ARG GLU ILE ASP ALA LEU GLY GLY GLU MET
SEQRES 8 A 637 GLY LYS ALA ILE ASP GLN THR GLY ILE GLN PHE LYS MET
SEQRES 9 A 637 LEU ASN THR ARG LYS GLY LYS ALA VAL GLN SER PRO ARG
SEQRES 10 A 637 ALA GLN ALA ASP LYS LYS ARG TYR ARG GLU TYR MET LYS
SEQRES 11 A 637 LYS VAL CYS GLU ASN GLN GLU ASN LEU TYR ILE LYS GLN
SEQRES 12 A 637 GLU GLU VAL VAL ASP ILE ILE VAL LYS ASN ASN GLN VAL
SEQRES 13 A 637 VAL GLY VAL ARG THR ASN LEU GLY VAL GLU TYR LYS THR
SEQRES 14 A 637 LYS ALA VAL VAL VAL THR THR GLY THR PHE LEU ASN GLY
SEQRES 15 A 637 VAL ILE TYR ILE GLY ASP LYS MET ILE PRO GLY GLY ARG
SEQRES 16 A 637 LEU GLY GLU PRO ARG SER GLU GLY LEU SER ASP PHE TYR
SEQRES 17 A 637 ARG ARG PHE ASP PHE PRO LEU ILE ARG PHE LYS THR GLY
SEQRES 18 A 637 THR PRO ALA ARG LEU ASP LYS ARG THR ILE ASP PHE SER
SEQRES 19 A 637 ALA LEU GLU VAL ALA PRO GLY ASP ASP PRO PRO PRO LYS
SEQRES 20 A 637 PHE SER PHE TRP THR GLU PRO VAL GLY SER TYR TRP PHE
SEQRES 21 A 637 PRO LYS GLY LYS GLU GLN VAL ASN CYS TRP ILE THR TYR
SEQRES 22 A 637 THR THR PRO LYS THR HIS GLU ILE ILE ARG LYS ASN LEU
SEQRES 23 A 637 HIS ARG THR ALA LEU TYR GLY GLY LEU ILE LYS GLY ILE
SEQRES 24 A 637 GLY PRO ARG TYR CYS PRO SER ILE GLU ASP LYS ILE VAL
SEQRES 25 A 637 LYS PHE PRO ASP LYS GLU ARG HIS GLN ILE PHE LEU GLU
SEQRES 26 A 637 PRO GLU GLY LEU ASP THR ILE GLU ILE TYR PRO ASN GLY
SEQRES 27 A 637 LEU SER THR SER LEU PRO GLU GLU VAL GLN TRP GLU MET
SEQRES 28 A 637 TYR ARG SER ILE PRO GLY LEU GLU ASN VAL VAL LEU ILE
SEQRES 29 A 637 ARG PRO ALA TYR ALA ILE GLU TYR ASP VAL VAL PRO PRO
SEQRES 30 A 637 THR GLU LEU TYR PRO THR LEU GLU THR LYS LYS ILE ARG
SEQRES 31 A 637 GLY LEU PHE HIS ALA GLY ASN PHE ASN GLY THR THR GLY
SEQRES 32 A 637 TYR GLU GLU ALA ALA GLY GLN GLY ILE VAL ALA GLY ILE
SEQRES 33 A 637 ASN ALA ALA LEU ARG ALA PHE GLY LYS GLU PRO ILE TYR
SEQRES 34 A 637 LEU ARG ARG ASP GLU SER TYR ILE GLY VAL MET ILE ASP
SEQRES 35 A 637 ASP LEU THR THR LYS GLY VAL THR GLU PRO TYR ARG LEU
SEQRES 36 A 637 PHE THR SER ARG SER GLU TYR ARG LEU TYR ILE ARG GLN
SEQRES 37 A 637 ASP ASN ALA ILE LEU ARG LEU ALA LYS LEU GLY ARG GLU
SEQRES 38 A 637 LEU GLY LEU LEU SER GLU GLU GLN TYR LYS LEU VAL LYS
SEQRES 39 A 637 GLU LEU GLU ARG GLU ILE GLU LYS TRP LYS GLU PHE TYR
SEQRES 40 A 637 LYS SER GLU ARG VAL SER VAL ALA VAL GLY GLY ASP THR
SEQRES 41 A 637 ARG SER TYR SER VAL ALA THR LEU MET THR MET ASN TYR
SEQRES 42 A 637 THR LEU ASP ASP VAL LYS GLU LYS PHE GLY TYR GLU VAL
SEQRES 43 A 637 PRO GLN HIS PRO TYR VAL LYS GLU GLU VAL GLU ILE GLN
SEQRES 44 A 637 LEU LYS TYR GLU PRO TYR ILE GLU ARG GLU ARG LYS LEU
SEQRES 45 A 637 ASN GLU LYS LEU LYS LYS LEU GLU ASP THR LYS ILE PRO
SEQRES 46 A 637 PRO ASP ILE ASP TYR ASP LYS ILE PRO GLY LEU THR LYS
SEQRES 47 A 637 GLU ALA ARG GLU LYS LEU LYS LYS PHE LYS PRO ILE THR
SEQRES 48 A 637 VAL GLY GLN ALA SER ARG ILE ASP GLY ILE THR PRO ALA
SEQRES 49 A 637 ALA ILE THR ALA LEU LEU VAL TYR LEU GLY LYS LEU ASP
SEQRES 1 B 637 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 B 637 LEU VAL PRO ALA GLY SER HIS MET ALA TRP VAL VAL ASP
SEQRES 3 B 637 GLU PHE ASP VAL VAL VAL ILE GLY GLY GLY HIS ALA GLY
SEQRES 4 B 637 ILE GLU ALA ALA LEU ALA ALA ALA ARG MET GLY ALA LYS
SEQRES 5 B 637 THR ALA MET PHE VAL LEU ASN ALA ASP THR ILE GLY GLN
SEQRES 6 B 637 MET SER CYS ASN PRO ALA ILE GLY GLY ILE ALA LYS GLY
SEQRES 7 B 637 ILE VAL VAL ARG GLU ILE ASP ALA LEU GLY GLY GLU MET
SEQRES 8 B 637 GLY LYS ALA ILE ASP GLN THR GLY ILE GLN PHE LYS MET
SEQRES 9 B 637 LEU ASN THR ARG LYS GLY LYS ALA VAL GLN SER PRO ARG
SEQRES 10 B 637 ALA GLN ALA ASP LYS LYS ARG TYR ARG GLU TYR MET LYS
SEQRES 11 B 637 LYS VAL CYS GLU ASN GLN GLU ASN LEU TYR ILE LYS GLN
SEQRES 12 B 637 GLU GLU VAL VAL ASP ILE ILE VAL LYS ASN ASN GLN VAL
SEQRES 13 B 637 VAL GLY VAL ARG THR ASN LEU GLY VAL GLU TYR LYS THR
SEQRES 14 B 637 LYS ALA VAL VAL VAL THR THR GLY THR PHE LEU ASN GLY
SEQRES 15 B 637 VAL ILE TYR ILE GLY ASP LYS MET ILE PRO GLY GLY ARG
SEQRES 16 B 637 LEU GLY GLU PRO ARG SER GLU GLY LEU SER ASP PHE TYR
SEQRES 17 B 637 ARG ARG PHE ASP PHE PRO LEU ILE ARG PHE LYS THR GLY
SEQRES 18 B 637 THR PRO ALA ARG LEU ASP LYS ARG THR ILE ASP PHE SER
SEQRES 19 B 637 ALA LEU GLU VAL ALA PRO GLY ASP ASP PRO PRO PRO LYS
SEQRES 20 B 637 PHE SER PHE TRP THR GLU PRO VAL GLY SER TYR TRP PHE
SEQRES 21 B 637 PRO LYS GLY LYS GLU GLN VAL ASN CYS TRP ILE THR TYR
SEQRES 22 B 637 THR THR PRO LYS THR HIS GLU ILE ILE ARG LYS ASN LEU
SEQRES 23 B 637 HIS ARG THR ALA LEU TYR GLY GLY LEU ILE LYS GLY ILE
SEQRES 24 B 637 GLY PRO ARG TYR CYS PRO SER ILE GLU ASP LYS ILE VAL
SEQRES 25 B 637 LYS PHE PRO ASP LYS GLU ARG HIS GLN ILE PHE LEU GLU
SEQRES 26 B 637 PRO GLU GLY LEU ASP THR ILE GLU ILE TYR PRO ASN GLY
SEQRES 27 B 637 LEU SER THR SER LEU PRO GLU GLU VAL GLN TRP GLU MET
SEQRES 28 B 637 TYR ARG SER ILE PRO GLY LEU GLU ASN VAL VAL LEU ILE
SEQRES 29 B 637 ARG PRO ALA TYR ALA ILE GLU TYR ASP VAL VAL PRO PRO
SEQRES 30 B 637 THR GLU LEU TYR PRO THR LEU GLU THR LYS LYS ILE ARG
SEQRES 31 B 637 GLY LEU PHE HIS ALA GLY ASN PHE ASN GLY THR THR GLY
SEQRES 32 B 637 TYR GLU GLU ALA ALA GLY GLN GLY ILE VAL ALA GLY ILE
SEQRES 33 B 637 ASN ALA ALA LEU ARG ALA PHE GLY LYS GLU PRO ILE TYR
SEQRES 34 B 637 LEU ARG ARG ASP GLU SER TYR ILE GLY VAL MET ILE ASP
SEQRES 35 B 637 ASP LEU THR THR LYS GLY VAL THR GLU PRO TYR ARG LEU
SEQRES 36 B 637 PHE THR SER ARG SER GLU TYR ARG LEU TYR ILE ARG GLN
SEQRES 37 B 637 ASP ASN ALA ILE LEU ARG LEU ALA LYS LEU GLY ARG GLU
SEQRES 38 B 637 LEU GLY LEU LEU SER GLU GLU GLN TYR LYS LEU VAL LYS
SEQRES 39 B 637 GLU LEU GLU ARG GLU ILE GLU LYS TRP LYS GLU PHE TYR
SEQRES 40 B 637 LYS SER GLU ARG VAL SER VAL ALA VAL GLY GLY ASP THR
SEQRES 41 B 637 ARG SER TYR SER VAL ALA THR LEU MET THR MET ASN TYR
SEQRES 42 B 637 THR LEU ASP ASP VAL LYS GLU LYS PHE GLY TYR GLU VAL
SEQRES 43 B 637 PRO GLN HIS PRO TYR VAL LYS GLU GLU VAL GLU ILE GLN
SEQRES 44 B 637 LEU LYS TYR GLU PRO TYR ILE GLU ARG GLU ARG LYS LEU
SEQRES 45 B 637 ASN GLU LYS LEU LYS LYS LEU GLU ASP THR LYS ILE PRO
SEQRES 46 B 637 PRO ASP ILE ASP TYR ASP LYS ILE PRO GLY LEU THR LYS
SEQRES 47 B 637 GLU ALA ARG GLU LYS LEU LYS LYS PHE LYS PRO ILE THR
SEQRES 48 B 637 VAL GLY GLN ALA SER ARG ILE ASP GLY ILE THR PRO ALA
SEQRES 49 B 637 ALA ILE THR ALA LEU LEU VAL TYR LEU GLY LYS LEU ASP
HET FAD A 618 53
HET PO4 A 619 5
HET PO4 A 620 5
HET FAD B 618 53
HET PO4 B 619 5
HETNAM FAD FLAVIN-ADENINE DINUCLEOTIDE
HETNAM PO4 PHOSPHATE ION
FORMUL 3 FAD 2(C27 H33 N9 O15 P2)
FORMUL 4 PO4 3(O4 P 3-)
HELIX 1 1 GLY A 16 MET A 29 1 14
HELIX 2 2 ASN A 39 ILE A 43 5 5
HELIX 3 3 ALA A 56 GLY A 68 1 13
HELIX 4 4 GLU A 70 THR A 78 1 9
HELIX 5 5 ASP A 101 ASN A 115 1 15
HELIX 6 6 GLY A 183 PHE A 191 1 9
HELIX 7 7 ARG A 209 ILE A 211 5 3
HELIX 8 8 THR A 255 ASN A 265 1 11
HELIX 9 9 LEU A 266 THR A 269 5 4
HELIX 10 10 PRO A 324 ARG A 333 1 10
HELIX 11 11 PRO A 356 LEU A 360 5 5
HELIX 12 12 GLY A 376 GLY A 380 5 5
HELIX 13 13 GLY A 383 GLY A 404 1 22
HELIX 14 14 SER A 415 GLY A 428 1 14
HELIX 15 15 ASN A 450 GLY A 463 1 14
HELIX 16 16 SER A 466 GLU A 490 1 25
HELIX 17 17 VAL A 505 ASN A 512 5 8
HELIX 18 18 ASP A 516 LYS A 521 1 6
HELIX 19 19 HIS A 529 ASN A 553 1 25
HELIX 20 20 ASN A 553 THR A 562 1 10
HELIX 21 21 THR A 577 PHE A 587 1 11
HELIX 22 22 THR A 591 ILE A 598 1 8
HELIX 23 23 THR A 602 GLY A 614 1 13
HELIX 24 24 GLY B 16 MET B 29 1 14
HELIX 25 25 ASN B 39 ILE B 43 5 5
HELIX 26 26 ALA B 56 GLY B 68 1 13
HELIX 27 27 GLU B 70 THR B 78 1 9
HELIX 28 28 ASP B 101 ASN B 115 1 15
HELIX 29 29 GLY B 183 PHE B 191 1 9
HELIX 30 30 ARG B 209 ILE B 211 5 3
HELIX 31 31 THR B 255 ASN B 265 1 11
HELIX 32 32 LEU B 266 THR B 269 5 4
HELIX 33 33 GLY B 280 CYS B 284 5 5
HELIX 34 34 PRO B 324 ARG B 333 1 10
HELIX 35 35 PRO B 356 LEU B 360 5 5
HELIX 36 36 GLY B 376 GLY B 380 5 5
HELIX 37 37 GLY B 383 GLY B 404 1 22
HELIX 38 38 SER B 415 GLY B 428 1 14
HELIX 39 39 ASN B 450 GLY B 463 1 14
HELIX 40 40 SER B 466 GLU B 490 1 25
HELIX 41 41 SER B 504 MET B 509 1 6
HELIX 42 42 THR B 510 ASN B 512 5 3
HELIX 43 43 ASP B 516 LYS B 521 1 6
HELIX 44 44 HIS B 529 ASN B 553 1 25
HELIX 45 45 ASN B 553 THR B 562 1 10
HELIX 46 46 THR B 577 PHE B 587 1 11
HELIX 47 47 THR B 591 ILE B 598 1 8
HELIX 48 48 THR B 602 GLY B 614 1 13
SHEET 1 A 6 LEU A 119 LYS A 122 0
SHEET 2 A 6 THR A 33 PHE A 36 1 N THR A 33 O TYR A 120
SHEET 3 A 6 GLU A 7 ILE A 13 1 N VAL A 12 O ALA A 34
SHEET 4 A 6 GLU A 146 VAL A 154 1 O LYS A 148 N PHE A 8
SHEET 5 A 6 GLN A 135 THR A 141 -1 N VAL A 139 O TYR A 147
SHEET 6 A 6 VAL A 126 LYS A 132 -1 N ILE A 130 O VAL A 137
SHEET 1 B 5 LEU A 119 LYS A 122 0
SHEET 2 B 5 THR A 33 PHE A 36 1 N THR A 33 O TYR A 120
SHEET 3 B 5 GLU A 7 ILE A 13 1 N VAL A 12 O ALA A 34
SHEET 4 B 5 GLU A 146 VAL A 154 1 O LYS A 148 N PHE A 8
SHEET 5 B 5 LEU A 372 HIS A 374 1 O PHE A 373 N VAL A 152
SHEET 1 C 3 ALA A 51 GLY A 53 0
SHEET 2 C 3 SER A 95 ALA A 100 -1 O ALA A 98 N ILE A 52
SHEET 3 C 3 GLY A 79 GLN A 81 -1 N ILE A 80 O GLN A 99
SHEET 1 D 3 ALA A 51 GLY A 53 0
SHEET 2 D 3 SER A 95 ALA A 100 -1 O ALA A 98 N ILE A 52
SHEET 3 D 3 MET A 84 LEU A 85 -1 N LEU A 85 O SER A 95
SHEET 1 E 4 LYS A 169 PRO A 172 0
SHEET 2 E 4 VAL A 163 ILE A 166 -1 N ILE A 164 O ILE A 171
SHEET 3 E 4 TYR A 348 VAL A 354 -1 O ALA A 349 N TYR A 165
SHEET 4 E 4 ILE A 196 THR A 202 -1 N THR A 200 O ILE A 350
SHEET 1 F 6 GLU A 217 ALA A 219 0
SHEET 2 F 6 CYS A 249 TYR A 253 -1 O CYS A 249 N ALA A 219
SHEET 3 F 6 GLN A 301 PRO A 306 -1 O LEU A 304 N TRP A 250
SHEET 4 F 6 GLU A 313 ASN A 317 -1 O TYR A 315 N GLU A 305
SHEET 5 F 6 ARG A 205 ASP A 207 -1 N LEU A 206 O ILE A 314
SHEET 6 F 6 LEU A 343 ARG A 345 -1 O ILE A 344 N ARG A 205
SHEET 1 G 6 LEU B 119 LYS B 122 0
SHEET 2 G 6 THR B 33 PHE B 36 1 N THR B 33 O TYR B 120
SHEET 3 G 6 GLU B 7 ILE B 13 1 N VAL B 12 O ALA B 34
SHEET 4 G 6 GLU B 146 VAL B 154 1 O LYS B 148 N PHE B 8
SHEET 5 G 6 GLN B 135 THR B 141 -1 N VAL B 139 O TYR B 147
SHEET 6 G 6 VAL B 126 LYS B 132 -1 N ILE B 130 O VAL B 137
SHEET 1 H 5 LEU B 119 LYS B 122 0
SHEET 2 H 5 THR B 33 PHE B 36 1 N THR B 33 O TYR B 120
SHEET 3 H 5 GLU B 7 ILE B 13 1 N VAL B 12 O ALA B 34
SHEET 4 H 5 GLU B 146 VAL B 154 1 O LYS B 148 N PHE B 8
SHEET 5 H 5 LEU B 372 HIS B 374 1 O PHE B 373 N VAL B 152
SHEET 1 I 3 ALA B 51 GLY B 53 0
SHEET 2 I 3 SER B 95 ALA B 100 -1 O ALA B 98 N ILE B 52
SHEET 3 I 3 GLY B 79 GLN B 81 -1 N ILE B 80 O GLN B 99
SHEET 1 J 3 ALA B 51 GLY B 53 0
SHEET 2 J 3 SER B 95 ALA B 100 -1 O ALA B 98 N ILE B 52
SHEET 3 J 3 MET B 84 LEU B 85 -1 N LEU B 85 O SER B 95
SHEET 1 K 4 LYS B 169 PRO B 172 0
SHEET 2 K 4 VAL B 163 ILE B 166 -1 N ILE B 164 O ILE B 171
SHEET 3 K 4 TYR B 348 VAL B 354 -1 O ALA B 349 N TYR B 165
SHEET 4 K 4 ILE B 196 THR B 202 -1 N THR B 200 O ILE B 350
SHEET 1 L 6 GLU B 217 ALA B 219 0
SHEET 2 L 6 CYS B 249 TYR B 253 -1 O CYS B 249 N ALA B 219
SHEET 3 L 6 GLN B 301 PRO B 306 -1 O LEU B 304 N TRP B 250
SHEET 4 L 6 GLU B 313 ASN B 317 -1 O TYR B 315 N GLU B 305
SHEET 5 L 6 ARG B 205 ASP B 207 -1 N LEU B 206 O ILE B 314
SHEET 6 L 6 LEU B 343 ARG B 345 -1 O ILE B 344 N ARG B 205
CISPEP 1 ASP A 223 PRO A 224 0 -0.08
CISPEP 2 GLU A 233 PRO A 234 0 -0.07
CISPEP 3 ASP B 223 PRO B 224 0 -0.12
CISPEP 4 GLU B 233 PRO B 234 0 0.08
SITE 1 AC1 28 ILE A 13 GLY A 14 GLY A 15 GLY A 16
SITE 2 AC1 28 HIS A 17 ALA A 18 VAL A 37 LEU A 38
SITE 3 AC1 28 LYS A 57 GLU A 125 VAL A 126 THR A 155
SITE 4 AC1 28 THR A 156 GLY A 157 PHE A 159 ARG A 175
SITE 5 AC1 28 SER A 181 THR A 200 GLY A 201 THR A 202
SITE 6 AC1 28 TYR A 348 ILE A 350 GLY A 376 ASN A 377
SITE 7 AC1 28 THR A 382 GLY A 383 ALA A 387 ARG A 434
SITE 1 AC2 27 ILE B 13 GLY B 14 GLY B 15 GLY B 16
SITE 2 AC2 27 HIS B 17 ALA B 18 LEU B 38 CYS B 48
SITE 3 AC2 27 LYS B 57 GLU B 124 VAL B 126 THR B 155
SITE 4 AC2 27 THR B 156 GLY B 157 THR B 158 PHE B 159
SITE 5 AC2 27 SER B 181 THR B 200 GLY B 201 TYR B 348
SITE 6 AC2 27 ILE B 350 GLY B 376 ASN B 377 THR B 382
SITE 7 AC2 27 GLY B 383 ALA B 387 ARG B 434
SITE 1 AC3 4 LYS A 89 ARG A 439 LYS B 277 ASP B 296
SITE 1 AC4 3 LYS A 277 ASP A 296 ARG B 439
SITE 1 AC5 6 PRO B 281 ARG B 282 LYS B 297 ARG B 299
SITE 2 AC5 6 HIS B 300 GLN B 301
CRYST1 101.638 213.272 231.737 90.00 90.00 90.00 I 21 21 21 16
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 0.009839 0.000000 0.000000 0.00000
SCALE2 0.000000 0.004689 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004315 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
