HEADER MANGANESE SUPEROXIDE DISMUTASE 05-FEB-02 1GV3
TITLE THE 2.0 ANGSTROM RESOLUTION STRUCTURE OF THE CATALYTIC
TITLE 2 PORTION OF A CYANOBACTERIAL MEMBRANE-BOUND MANGANESE
TITLE 3 SUPEROXIDE DISMUTASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MANGANESE SUPEROXIDE DISMUTASE;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: HELICAL HAIRPIN, ALPHA/BETA DOMAIN, RESIDUES
COMPND 5 30-270;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ANABAENA SP.;
SOURCE 3 ORGANISM_TAXID: 103690;
SOURCE 4 STRAIN: PCC 7120;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET-3A
KEYWDS MANGANESE SUPEROXIDE DISMUTASE, ANABAENA PCC 7120, CRYSTAL
KEYWDS 2 STRUCTURE
EXPDTA X-RAY DIFFRACTION
AUTHOR W.ATZENHOFER,G.REGELSBERGER,U.JACOB,R.HUBER,G.A.PESCHEK,
AUTHOR 2 C.OBINGER
REVDAT 3 24-FEB-09 1GV3 1 VERSN
REVDAT 2 16-JAN-03 1GV3 1 COMPND DBREF
REVDAT 1 08-AUG-02 1GV3 0
JRNL AUTH W.ATZENHOFER,G.REGELSBERGER,U.JACOB,G.A.PESCHEK,
JRNL AUTH 2 P.FURTMULLER,R.HUBER,C.OBINGER
JRNL TITL THE 2.0A RESOLUTION STRUCTURE OF THE CATALYTIC
JRNL TITL 2 PORTION OF A CYANOBACTERIAL MEMBRANE-BOUND
JRNL TITL 3 MANGANESE SUPEROXIDE DISMUTASE
JRNL REF J.MOL.BIOL. V. 321 479 2002
JRNL REFN ISSN 0022-2836
JRNL PMID 12162960
JRNL DOI 10.1016/S0022-2836(02)00624-1
REMARK 2
REMARK 2 RESOLUTION. 2.0 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1
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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 100
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.0
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 10000
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 93.9
REMARK 3 NUMBER OF REFLECTIONS : 33267
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING SET) : 0.188
REMARK 3 FREE R VALUE : 0.211
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.191
REMARK 3 BIN FREE R VALUE : 0.212
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3440
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 2
REMARK 3 SOLVENT ATOMS : 166
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) : 1.69
REMARK 3 B22 (A**2) : 1.69
REMARK 3 B33 (A**2) : -3.39
REMARK 3 B12 (A**2) : 0.34
REMARK 3 B13 (A**2) : 0.00
REMARK 3 B23 (A**2) : 0.00
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.0057
REMARK 3 BOND ANGLES (DEGREES) : 1.248
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 1.33 ; 1.50
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.33 ; 2.00
REMARK 3 SIDE-CHAIN BOND (A**2) : 2.13 ; 2.00
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 3.55 ; 2.50
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : NULL
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 : NULL
REMARK 3 PARAMETER FILE 2 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 2 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1GV3 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 05-FEB-02.
REMARK 100 THE PDBE ID CODE IS EBI-9391.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-AUG-01
REMARK 200 TEMPERATURE (KELVIN) : 287.0
REMARK 200 PH : 7.50
REMARK 200 NUMBER OF CRYSTALS USED : 3
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU ROTATING ANODE
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.518
REMARK 200 MONOCHROMATOR : GRAPHIT
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : NULL
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 35333
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.030
REMARK 200 RESOLUTION RANGE LOW (A) : 30.570
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 93.9
REMARK 200 DATA REDUNDANCY : 2.500
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: 1MNG
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): NULL
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): NULL
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: H 3
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z
REMARK 290 3555 -X+Y,-X,Z
REMARK 290 4555 X+2/3,Y+1/3,Z+1/3
REMARK 290 5555 -Y+2/3,X-Y+1/3,Z+1/3
REMARK 290 6555 -X+Y+2/3,-X+1/3,Z+1/3
REMARK 290 7555 X+1/3,Y+2/3,Z+2/3
REMARK 290 8555 -Y+1/3,X-Y+2/3,Z+2/3
REMARK 290 9555 -X+Y+1/3,-X+2/3,Z+2/3
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 75.66000
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 43.68232
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 23.09333
REMARK 290 SMTRY1 5 -0.500000 -0.866025 0.000000 75.66000
REMARK 290 SMTRY2 5 0.866025 -0.500000 0.000000 43.68232
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 23.09333
REMARK 290 SMTRY1 6 -0.500000 0.866025 0.000000 75.66000
REMARK 290 SMTRY2 6 -0.866025 -0.500000 0.000000 43.68232
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 23.09333
REMARK 290 SMTRY1 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 87.36464
REMARK 290 SMTRY3 7 0.000000 0.000000 1.000000 46.18667
REMARK 290 SMTRY1 8 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 8 0.866025 -0.500000 0.000000 87.36464
REMARK 290 SMTRY3 8 0.000000 0.000000 1.000000 46.18667
REMARK 290 SMTRY1 9 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 -0.500000 0.000000 87.36464
REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 46.18667
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 GENERATING THE BIOMOLECULE
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: PQS
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 1
REMARK 465 ALA A 2
REMARK 465 ALA A 3
REMARK 465 ASN A 4
REMARK 465 SER A 5
REMARK 465 LEU A 6
REMARK 465 PRO A 7
REMARK 465 THR A 8
REMARK 465 ASN A 9
REMARK 465 VAL A 10
REMARK 465 ALA A 11
REMARK 465 SER A 12
REMARK 465 PRO A 13
REMARK 465 VAL A 14
REMARK 465 GLN A 15
REMARK 465 THR A 16
REMARK 465 THR A 17
REMARK 465 THR A 18
REMARK 465 PRO A 19
REMARK 465 THR A 20
REMARK 465 THR A 21
REMARK 465 ASP A 22
REMARK 465 LYS A 23
REMARK 465 ARG A 24
REMARK 465 GLN A 239
REMARK 465 SER A 240
REMARK 465 ASN A 241
REMARK 465 SER A 242
REMARK 465 HIS A 243
REMARK 465 HIS A 244
REMARK 465 HIS A 245
REMARK 465 HIS A 246
REMARK 465 HIS A 247
REMARK 465 HIS A 248
REMARK 465 MET B 1
REMARK 465 ALA B 2
REMARK 465 ALA B 3
REMARK 465 ASN B 4
REMARK 465 SER B 5
REMARK 465 LEU B 6
REMARK 465 PRO B 7
REMARK 465 THR B 8
REMARK 465 ASN B 9
REMARK 465 VAL B 10
REMARK 465 ALA B 11
REMARK 465 SER B 12
REMARK 465 PRO B 13
REMARK 465 VAL B 14
REMARK 465 GLN B 15
REMARK 465 THR B 16
REMARK 465 THR B 17
REMARK 465 THR B 18
REMARK 465 PRO B 19
REMARK 465 THR B 20
REMARK 465 THR B 21
REMARK 465 ASP B 22
REMARK 465 LYS B 23
REMARK 465 ARG B 24
REMARK 465 GLN B 239
REMARK 465 SER B 240
REMARK 465 ASN B 241
REMARK 465 SER B 242
REMARK 465 HIS B 243
REMARK 465 HIS B 244
REMARK 465 HIS B 245
REMARK 465 HIS B 246
REMARK 465 HIS B 247
REMARK 465 HIS B 248
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 ARG A 238 CA C O CB CG CD NE CZ NH1 NH2
REMARK 470 ARG B 238 CA C O CB CG CD NE CZ NH1 NH2
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 CG1 ILE A 29 - O HOH A 2078 1.40
REMARK 500 CD1 ILE A 29 - O HOH A 2078 1.31
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 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 ALA A 53 -46.24 -146.27
REMARK 500 LYS A 65 -60.39 -104.32
REMARK 500 ASN A 184 -116.84 45.69
REMARK 500 TYR A 206 -2.57 -145.33
REMARK 500 GLN A 211 -123.60 54.98
REMARK 500 ALA B 53 -44.49 -144.86
REMARK 500 ASN B 184 -117.69 46.45
REMARK 500 TYR B 206 -2.10 -147.90
REMARK 500 GLN B 211 -128.90 56.08
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 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 MN A1238 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 117 NE2
REMARK 620 2 HIS A 204 NE2 137.0
REMARK 620 3 HIS A 62 NE2 86.7 87.8
REMARK 620 4 ASP A 200 OD2 105.8 116.5 87.2
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN B1238 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 200 OD2
REMARK 620 2 HIS B 117 NE2 107.9
REMARK 620 3 HIS B 62 NE2 92.5 86.1
REMARK 620 4 HIS B 204 NE2 115.0 137.1 94.0
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN A1238
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN B1238
DBREF 1GV3 A 1 1 PDB 1GV3 1GV3 1 1
DBREF 1GV3 A 2 242 UNP Q8Z0M1 Q8Z0M1_ANASP 30 270
DBREF 1GV3 A 243 248 PDB 1GV3 1GV3 243 248
DBREF 1GV3 B 1 1 PDB 1GV3 1GV3 1 1
DBREF 1GV3 B 2 242 UNP Q8Z0M1 Q8Z0M1_ANASP 30 270
DBREF 1GV3 B 243 248 PDB 1GV3 1GV3 243 248
SEQADV 1GV3 VAL A 179 UNP Q8Z0M1 ILE 207 CONFLICT
SEQADV 1GV3 ASN A 187 UNP Q8Z0M1 SER 215 CONFLICT
SEQADV 1GV3 VAL B 179 UNP Q8Z0M1 ILE 207 CONFLICT
SEQADV 1GV3 ASN B 187 UNP Q8Z0M1 SER 215 CONFLICT
SEQRES 1 A 248 MET ALA ALA ASN SER LEU PRO THR ASN VAL ALA SER PRO
SEQRES 2 A 248 VAL GLN THR THR THR PRO THR THR ASP LYS ARG SER ILE
SEQRES 3 A 248 GLY PHE ILE ASP ARG GLN LEU GLY THR ASN PRO ALA GLU
SEQRES 4 A 248 LEU PRO PRO LEU PRO TYR GLY TYR ASP ALA LEU GLU LYS
SEQRES 5 A 248 ALA ILE ASP ALA GLU THR MET LYS LEU HIS HIS ASP LYS
SEQRES 6 A 248 HIS HIS ALA ALA TYR VAL ASN ASN LEU ASN ASN ALA LEU
SEQRES 7 A 248 LYS LYS HIS PRO GLU LEU GLN ASN SER SER VAL GLU ALA
SEQRES 8 A 248 LEU LEU ARG ASP LEU ASN SER VAL PRO GLU ASP ILE ARG
SEQRES 9 A 248 THR THR VAL ARG ASN ASN GLY GLY GLY HIS LEU ASN HIS
SEQRES 10 A 248 THR ILE PHE TRP GLN ILE MET SER PRO ASP GLY GLY GLY
SEQRES 11 A 248 GLN PRO THR GLY ASP ILE ALA GLN GLU ILE ASN GLN THR
SEQRES 12 A 248 PHE GLY SER PHE GLU GLU PHE LYS LYS GLN PHE ASN GLN
SEQRES 13 A 248 ALA GLY GLY ASP ARG PHE GLY SER GLY TRP VAL TRP LEU
SEQRES 14 A 248 VAL ARG ASN PRO GLN GLY GLN LEU GLN VAL VAL SER THR
SEQRES 15 A 248 PRO ASN GLN ASP ASN PRO ILE MET GLU GLY SER TYR PRO
SEQRES 16 A 248 ILE MET GLY ASN ASP VAL TRP GLU HIS ALA TYR TYR LEU
SEQRES 17 A 248 ARG TYR GLN ASN ARG ARG PRO GLU TYR LEU ASN ASN TRP
SEQRES 18 A 248 TRP ASN VAL VAL ASN TRP SER GLU ILE ASN ARG ARG THR
SEQRES 19 A 248 GLN ALA SER ARG GLN SER ASN SER HIS HIS HIS HIS HIS
SEQRES 20 A 248 HIS
SEQRES 1 B 248 MET ALA ALA ASN SER LEU PRO THR ASN VAL ALA SER PRO
SEQRES 2 B 248 VAL GLN THR THR THR PRO THR THR ASP LYS ARG SER ILE
SEQRES 3 B 248 GLY PHE ILE ASP ARG GLN LEU GLY THR ASN PRO ALA GLU
SEQRES 4 B 248 LEU PRO PRO LEU PRO TYR GLY TYR ASP ALA LEU GLU LYS
SEQRES 5 B 248 ALA ILE ASP ALA GLU THR MET LYS LEU HIS HIS ASP LYS
SEQRES 6 B 248 HIS HIS ALA ALA TYR VAL ASN ASN LEU ASN ASN ALA LEU
SEQRES 7 B 248 LYS LYS HIS PRO GLU LEU GLN ASN SER SER VAL GLU ALA
SEQRES 8 B 248 LEU LEU ARG ASP LEU ASN SER VAL PRO GLU ASP ILE ARG
SEQRES 9 B 248 THR THR VAL ARG ASN ASN GLY GLY GLY HIS LEU ASN HIS
SEQRES 10 B 248 THR ILE PHE TRP GLN ILE MET SER PRO ASP GLY GLY GLY
SEQRES 11 B 248 GLN PRO THR GLY ASP ILE ALA GLN GLU ILE ASN GLN THR
SEQRES 12 B 248 PHE GLY SER PHE GLU GLU PHE LYS LYS GLN PHE ASN GLN
SEQRES 13 B 248 ALA GLY GLY ASP ARG PHE GLY SER GLY TRP VAL TRP LEU
SEQRES 14 B 248 VAL ARG ASN PRO GLN GLY GLN LEU GLN VAL VAL SER THR
SEQRES 15 B 248 PRO ASN GLN ASP ASN PRO ILE MET GLU GLY SER TYR PRO
SEQRES 16 B 248 ILE MET GLY ASN ASP VAL TRP GLU HIS ALA TYR TYR LEU
SEQRES 17 B 248 ARG TYR GLN ASN ARG ARG PRO GLU TYR LEU ASN ASN TRP
SEQRES 18 B 248 TRP ASN VAL VAL ASN TRP SER GLU ILE ASN ARG ARG THR
SEQRES 19 B 248 GLN ALA SER ARG GLN SER ASN SER HIS HIS HIS HIS HIS
SEQRES 20 B 248 HIS
HET MN A1238 1
HET MN B1238 1
HETNAM MN MANGANESE (II) ION
FORMUL 3 MN 2(MN 2+)
FORMUL 5 HOH *166(H2 O1)
HELIX 1 1 ASP A 55 LYS A 65 1 11
HELIX 2 2 LYS A 65 LYS A 80 1 16
HELIX 3 3 HIS A 81 SER A 87 5 7
HELIX 4 4 SER A 88 ASP A 95 1 8
HELIX 5 5 LEU A 96 VAL A 99 5 4
HELIX 6 6 ILE A 103 ILE A 123 1 21
HELIX 7 7 THR A 133 GLY A 145 1 13
HELIX 8 8 SER A 146 ARG A 161 1 16
HELIX 9 9 ASN A 187 GLY A 192 5 6
HELIX 10 10 TRP A 202 ALA A 205 5 4
HELIX 11 11 TYR A 206 GLN A 211 1 6
HELIX 12 12 ARG A 213 TRP A 221 1 9
HELIX 13 13 TRP A 222 VAL A 224 5 3
HELIX 14 14 ASN A 226 SER A 237 1 12
HELIX 15 15 ASP B 55 LYS B 65 1 11
HELIX 16 16 LYS B 65 LYS B 80 1 16
HELIX 17 17 HIS B 81 GLN B 85 5 5
HELIX 18 18 SER B 88 ASP B 95 1 8
HELIX 19 19 LEU B 96 VAL B 99 5 4
HELIX 20 20 ILE B 103 ILE B 123 1 21
HELIX 21 21 THR B 133 GLY B 145 1 13
HELIX 22 22 SER B 146 ARG B 161 1 16
HELIX 23 23 ASN B 187 GLY B 192 5 6
HELIX 24 24 TRP B 202 ALA B 205 5 4
HELIX 25 25 TYR B 206 GLN B 211 1 6
HELIX 26 26 ARG B 213 TRP B 222 1 10
HELIX 27 27 ASN B 226 SER B 237 1 12
SHEET 1 AA 3 LEU A 177 PRO A 183 0
SHEET 2 AA 3 GLY A 165 ARG A 171 -1 O TRP A 166 N THR A 182
SHEET 3 AA 3 TYR A 194 ASP A 200 -1 O TYR A 194 N ARG A 171
SHEET 1 BA 3 LEU B 177 PRO B 183 0
SHEET 2 BA 3 GLY B 165 ARG B 171 -1 O TRP B 166 N THR B 182
SHEET 3 BA 3 TYR B 194 ASP B 200 -1 O TYR B 194 N ARG B 171
LINK MN MN A1238 NE2 HIS A 117 1555 1555 2.16
LINK MN MN A1238 NE2 HIS A 204 1555 1555 2.23
LINK MN MN A1238 NE2 HIS A 62 1555 1555 2.20
LINK MN MN A1238 OD2 ASP A 200 1555 1555 2.02
LINK MN MN B1238 NE2 HIS B 117 1555 1555 2.20
LINK MN MN B1238 NE2 HIS B 62 1555 1555 2.15
LINK MN MN B1238 NE2 HIS B 204 1555 1555 2.17
LINK MN MN B1238 OD2 ASP B 200 1555 1555 1.99
CISPEP 1 ASN A 36 PRO A 37 0 -0.32
CISPEP 2 ASN B 36 PRO B 37 0 -0.31
SITE 1 AC1 5 HIS A 62 HIS A 117 ASP A 200 HIS A 204
SITE 2 AC1 5 HOH A2079
SITE 1 AC2 5 HIS B 62 HIS B 117 ASP B 200 HIS B 204
SITE 2 AC2 5 HOH B2087
CRYST1 151.320 151.320 69.280 90.00 90.00 120.00 H 3 18
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 0.006608 0.003815 0.000000 0.00000
SCALE2 0.000000 0.007631 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014434 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
