HEADER METAL BINDING PROTEIN 21-OCT-11 3UAB
TITLE MULTICOPPER OXIDASE CUEO MUTANT C500SE506Q (DATA2)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BLUE COPPER OXIDASE CUEO;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: COPPER EFFLUX OXIDASE;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 83333;
SOURCE 4 STRAIN: K12;
SOURCE 5 GENE: CUEO, YACK, B0123, JW0119;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS MULTICOPPER OXIDASE, METAL BINDING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR H.KOMORI,K.KATAOKA,T.SAKURAI,Y.HIGUCHI
REVDAT 2 20-MAR-24 3UAB 1 REMARK SEQADV LINK
REVDAT 1 11-APR-12 3UAB 0
JRNL AUTH H.KOMORI,R.SUGIYAMA,K.KATAOKA,Y.HIGUCHI,T.SAKURAI
JRNL TITL AN O-CENTERED STRUCTURE OF THE TRINUCLEAR COPPER CENTER IN
JRNL TITL 2 THE CYS500SER/GLU506GLN MUTANT OF CUEO AND STRUCTURAL
JRNL TITL 3 CHANGES IN LOW TO HIGH X-RAY DOSE CONDITIONS.
JRNL REF ANGEW.CHEM.INT.ED.ENGL. V. 51 1861 2012
JRNL REFN ISSN 1433-7851
JRNL PMID 22250058
JRNL DOI 10.1002/ANIE.201107739
REMARK 2
REMARK 2 RESOLUTION. 1.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : SHELXL-97
REMARK 3 AUTHORS : G.M.SHELDRICK
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 10.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 94.4
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (NO CUTOFF).
REMARK 3 R VALUE (WORKING + TEST SET, NO CUTOFF) : NULL
REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : 0.143
REMARK 3 FREE R VALUE (NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : NULL
REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : 108346
REMARK 3
REMARK 3 FIT/AGREEMENT OF MODEL FOR DATA WITH F>4SIG(F).
REMARK 3 R VALUE (WORKING + TEST SET, F>4SIG(F)) : NULL
REMARK 3 R VALUE (WORKING SET, F>4SIG(F)) : 0.134
REMARK 3 FREE R VALUE (F>4SIG(F)) : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%, F>4SIG(F)) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT (F>4SIG(F)) : NULL
REMARK 3 TOTAL NUMBER OF REFLECTIONS (F>4SIG(F)) : 87741
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3655
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 9
REMARK 3 SOLVENT ATOMS : 449
REMARK 3
REMARK 3 MODEL REFINEMENT.
REMARK 3 OCCUPANCY SUM OF NON-HYDROGEN ATOMS : 4109.4
REMARK 3 OCCUPANCY SUM OF HYDROGEN ATOMS : 0.00
REMARK 3 NUMBER OF DISCRETELY DISORDERED RESIDUES : 33
REMARK 3 NUMBER OF LEAST-SQUARES PARAMETERS : 36016
REMARK 3 NUMBER OF RESTRAINTS : 45701
REMARK 3
REMARK 3 RMS DEVIATIONS FROM RESTRAINT TARGET VALUES.
REMARK 3 BOND LENGTHS (A) : 0.012
REMARK 3 ANGLE DISTANCES (A) : 0.029
REMARK 3 SIMILAR DISTANCES (NO TARGET VALUES) (A) : 0.000
REMARK 3 DISTANCES FROM RESTRAINT PLANES (A) : 0.032
REMARK 3 ZERO CHIRAL VOLUMES (A**3) : 0.065
REMARK 3 NON-ZERO CHIRAL VOLUMES (A**3) : 0.077
REMARK 3 ANTI-BUMPING DISTANCE RESTRAINTS (A) : 0.024
REMARK 3 RIGID-BOND ADP COMPONENTS (A**2) : 0.004
REMARK 3 SIMILAR ADP COMPONENTS (A**2) : 0.052
REMARK 3 APPROXIMATELY ISOTROPIC ADPS (A**2) : 0.000
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED: NULL
REMARK 3
REMARK 3 STEREOCHEMISTRY TARGET VALUES : ENGH & HUBER
REMARK 3 SPECIAL CASE: NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3UAB COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 10-NOV-11.
REMARK 100 THE DEPOSITION ID IS D_1000068504.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : NULL
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SPRING-8
REMARK 200 BEAMLINE : BL26B2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.8000
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : NULL
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 114331
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.300
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 (%) : 99.3
REMARK 200 DATA REDUNDANCY : NULL
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: AB INITIO PHASING
REMARK 200 SOFTWARE USED: SHELX
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 44.92
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.23
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 45.58850
REMARK 290 SMTRY3 2 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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
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 SER A 382
REMARK 465 GLN A 383
REMARK 465 MET A 384
REMARK 465 MET A 385
REMARK 465 GLY A 386
REMARK 465 HIS A 387
REMARK 465 MET A 388
REMARK 465 GLY A 389
REMARK 465 HIS A 390
REMARK 465 GLY A 391
REMARK 465 ASN A 392
REMARK 465 MET A 393
REMARK 465 ASN A 394
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 CE MET A 303 SD MET A 364 1.82
REMARK 500 SD MET A 303 CE MET A 364 1.82
REMARK 500 CE MET A 303 CE MET A 364 2.12
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 31 NE - CZ - NH2 ANGL. DEV. = -3.5 DEGREES
REMARK 500 ARG A 47 NE - CZ - NH1 ANGL. DEV. = -5.3 DEGREES
REMARK 500 ARG A 47 NE - CZ - NH2 ANGL. DEV. = 5.2 DEGREES
REMARK 500 TYR A 221 CB - CG - CD1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 TYR A 221 CG - CD1 - CE1 ANGL. DEV. = 5.0 DEGREES
REMARK 500 PHE A 404 CB - CG - CD2 ANGL. DEV. = 4.7 DEGREES
REMARK 500 GLY A 517 CA - C - O ANGL. DEV. = 13.3 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 LEU A 74 -137.05 57.76
REMARK 500 ASP A 132 56.06 -143.94
REMARK 500 ILE A 178 -72.06 -119.83
REMARK 500 ALA A 241 -17.49 -144.64
REMARK 500 SER A 259 -166.65 -118.57
REMARK 500
REMARK 500 REMARK: NULL
REMARK 600
REMARK 600 HETEROGEN
REMARK 600
REMARK 600 OXT (ACT A1007) AND O (HOH A2002) ARE IN ALTERNATE CONFORMATIONS
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 CU A1004 CU
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 101 NE2
REMARK 620 2 HIS A 446 NE2 167.3
REMARK 620 3 O A1006 O 84.7 85.3
REMARK 620 4 ACT A1007 OXT 98.2 93.6 164.0
REMARK 620 5 HOH A2002 O 97.1 94.3 167.8 3.8
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CU A1002 CU
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 103 ND1
REMARK 620 2 HIS A 141 NE2 136.7
REMARK 620 3 HIS A 501 NE2 97.2 117.1
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CU A1002 CU
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 103 ND1
REMARK 620 2 HIS A 141 NE2 106.3
REMARK 620 3 HIS A 501 NE2 94.2 103.6
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CU A1003 CU
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 143 NE2
REMARK 620 2 HIS A 448 NE2 94.5
REMARK 620 3 HIS A 499 NE2 104.1 100.0
REMARK 620 4 O A1005 O 95.0 163.0 91.3
REMARK 620 5 O A1006 O 129.6 91.7 123.9 71.5
REMARK 620 N 1 2 3 4
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU A 1002
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU A 1003
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU A 1004
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE O A 1005
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE O A 1006
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A 1007
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3UAA RELATED DB: PDB
REMARK 900 RELATED ID: 3UAC RELATED DB: PDB
REMARK 900 RELATED ID: 3UAD RELATED DB: PDB
REMARK 900 RELATED ID: 3UAE RELATED DB: PDB
DBREF 3UAB A 29 516 UNP P36649 CUEO_ECOLI 29 516
SEQADV 3UAB SER A 500 UNP P36649 CYS 500 ENGINEERED MUTATION
SEQADV 3UAB GLN A 506 UNP P36649 GLU 506 ENGINEERED MUTATION
SEQADV 3UAB GLY A 517 UNP P36649 EXPRESSION TAG
SEQRES 1 A 489 ALA GLU ARG PRO THR LEU PRO ILE PRO ASP LEU LEU THR
SEQRES 2 A 489 THR ASP ALA ARG ASN ARG ILE GLN LEU THR ILE GLY ALA
SEQRES 3 A 489 GLY GLN SER THR PHE GLY GLY LYS THR ALA THR THR TRP
SEQRES 4 A 489 GLY TYR ASN GLY ASN LEU LEU GLY PRO ALA VAL LYS LEU
SEQRES 5 A 489 GLN ARG GLY LYS ALA VAL THR VAL ASP ILE TYR ASN GLN
SEQRES 6 A 489 LEU THR GLU GLU THR THR LEU HIS TRP HIS GLY LEU GLU
SEQRES 7 A 489 VAL PRO GLY GLU VAL ASP GLY GLY PRO GLN GLY ILE ILE
SEQRES 8 A 489 PRO PRO GLY GLY LYS ARG SER VAL THR LEU ASN VAL ASP
SEQRES 9 A 489 GLN PRO ALA ALA THR CYS TRP PHE HIS PRO HIS GLN HIS
SEQRES 10 A 489 GLY LYS THR GLY ARG GLN VAL ALA MET GLY LEU ALA GLY
SEQRES 11 A 489 LEU VAL VAL ILE GLU ASP ASP GLU ILE LEU LYS LEU MET
SEQRES 12 A 489 LEU PRO LYS GLN TRP GLY ILE ASP ASP VAL PRO VAL ILE
SEQRES 13 A 489 VAL GLN ASP LYS LYS PHE SER ALA ASP GLY GLN ILE ASP
SEQRES 14 A 489 TYR GLN LEU ASP VAL MET THR ALA ALA VAL GLY TRP PHE
SEQRES 15 A 489 GLY ASP THR LEU LEU THR ASN GLY ALA ILE TYR PRO GLN
SEQRES 16 A 489 HIS ALA ALA PRO ARG GLY TRP LEU ARG LEU ARG LEU LEU
SEQRES 17 A 489 ASN GLY CYS ASN ALA ARG SER LEU ASN PHE ALA THR SER
SEQRES 18 A 489 ASP ASN ARG PRO LEU TYR VAL ILE ALA SER ASP GLY GLY
SEQRES 19 A 489 LEU LEU PRO GLU PRO VAL LYS VAL SER GLU LEU PRO VAL
SEQRES 20 A 489 LEU MET GLY GLU ARG PHE GLU VAL LEU VAL GLU VAL ASN
SEQRES 21 A 489 ASP ASN LYS PRO PHE ASP LEU VAL THR LEU PRO VAL SER
SEQRES 22 A 489 GLN MET GLY MET ALA ILE ALA PRO PHE ASP LYS PRO HIS
SEQRES 23 A 489 PRO VAL MET ARG ILE GLN PRO ILE ALA ILE SER ALA SER
SEQRES 24 A 489 GLY ALA LEU PRO ASP THR LEU SER SER LEU PRO ALA LEU
SEQRES 25 A 489 PRO SER LEU GLU GLY LEU THR VAL ARG LYS LEU GLN LEU
SEQRES 26 A 489 SER MET ASP PRO MET LEU ASP MET MET GLY MET GLN MET
SEQRES 27 A 489 LEU MET GLU LYS TYR GLY ASP GLN ALA MET ALA GLY MET
SEQRES 28 A 489 ASP HIS SER GLN MET MET GLY HIS MET GLY HIS GLY ASN
SEQRES 29 A 489 MET ASN HIS MET ASN HIS GLY GLY LYS PHE ASP PHE HIS
SEQRES 30 A 489 HIS ALA ASN LYS ILE ASN GLY GLN ALA PHE ASP MET ASN
SEQRES 31 A 489 LYS PRO MET PHE ALA ALA ALA LYS GLY GLN TYR GLU ARG
SEQRES 32 A 489 TRP VAL ILE SER GLY VAL GLY ASP MET MET LEU HIS PRO
SEQRES 33 A 489 PHE HIS ILE HIS GLY THR GLN PHE ARG ILE LEU SER GLU
SEQRES 34 A 489 ASN GLY LYS PRO PRO ALA ALA HIS ARG ALA GLY TRP LYS
SEQRES 35 A 489 ASP THR VAL LYS VAL GLU GLY ASN VAL SER GLU VAL LEU
SEQRES 36 A 489 VAL LYS PHE ASN HIS ASP ALA PRO LYS GLU HIS ALA TYR
SEQRES 37 A 489 MET ALA HIS SER HIS LEU LEU GLU HIS GLN ASP THR GLY
SEQRES 38 A 489 MET MET LEU GLY PHE THR VAL GLY
HET CU A1002 2
HET CU A1003 1
HET CU A1004 1
HET O A1005 1
HET O A1006 1
HET ACT A1007 4
HETNAM CU COPPER (II) ION
HETNAM O OXYGEN ATOM
HETNAM ACT ACETATE ION
FORMUL 2 CU 3(CU 2+)
FORMUL 5 O 2(O)
FORMUL 7 ACT C2 H3 O2 1-
FORMUL 8 HOH *449(H2 O)
HELIX 1 1 PRO A 108 ASP A 112 5 5
HELIX 2 2 LYS A 147 MET A 154 1 8
HELIX 3 3 ASP A 164 LEU A 170 1 7
HELIX 4 4 ASP A 201 GLY A 208 1 8
HELIX 5 5 ASP A 356 GLY A 372 1 17
HELIX 6 6 ASP A 373 ALA A 377 5 5
HELIX 7 7 GLY A 399 ALA A 407 5 9
HELIX 8 8 ALA A 463 ALA A 467 5 5
HELIX 9 9 PRO A 491 ALA A 495 5 5
HELIX 10 10 LEU A 502 ASP A 507 1 6
SHEET 1 A 5 LEU A 39 LEU A 40 0
SHEET 2 A 5 ALA A 77 GLN A 81 1 O LYS A 79 N LEU A 40
SHEET 3 A 5 GLY A 158 GLU A 163 1 O LEU A 159 N VAL A 78
SHEET 4 A 5 ALA A 136 HIS A 141 -1 N ALA A 136 O ILE A 162
SHEET 5 A 5 HIS A 101 HIS A 103 -1 N HIS A 101 O HIS A 141
SHEET 1 B 4 LYS A 62 TYR A 69 0
SHEET 2 B 4 ARG A 47 PHE A 59 -1 N GLY A 55 O THR A 66
SHEET 3 B 4 ALA A 85 ASN A 92 1 O TYR A 91 N ILE A 52
SHEET 4 B 4 LYS A 124 ASN A 130 -1 O VAL A 127 N VAL A 88
SHEET 1 C 6 THR A 213 THR A 216 0
SHEET 2 C 6 ASP A 180 LYS A 188 -1 N GLN A 186 O LEU A 215
SHEET 3 C 6 GLN A 223 ASN A 237 1 O ARG A 234 N VAL A 183
SHEET 4 C 6 ARG A 280 VAL A 287 -1 O PHE A 281 N LEU A 235
SHEET 5 C 6 LEU A 254 SER A 259 -1 N TYR A 255 O LEU A 284
SHEET 6 C 6 GLY A 262 VAL A 270 -1 O VAL A 268 N VAL A 256
SHEET 1 D 7 THR A 213 THR A 216 0
SHEET 2 D 7 ASP A 180 LYS A 188 -1 N GLN A 186 O LEU A 215
SHEET 3 D 7 GLN A 223 ASN A 237 1 O ARG A 234 N VAL A 183
SHEET 4 D 7 HIS A 314 SER A 325 1 O ARG A 318 N HIS A 224
SHEET 5 D 7 PHE A 293 THR A 297 -1 N LEU A 295 O VAL A 316
SHEET 6 D 7 LEU A 244 THR A 248 -1 N ALA A 247 O VAL A 296
SHEET 7 D 7 LEU A 273 VAL A 275 -1 O LEU A 273 N PHE A 246
SHEET 1 E 5 LYS A 409 ILE A 410 0
SHEET 2 E 5 THR A 347 SER A 354 -1 N SER A 354 O LYS A 409
SHEET 3 E 5 GLU A 430 SER A 435 1 O VAL A 433 N ARG A 349
SHEET 4 E 5 VAL A 479 VAL A 484 -1 O SER A 480 N ILE A 434
SHEET 5 E 5 ARG A 453 SER A 456 -1 N ARG A 453 O LEU A 483
SHEET 1 F 5 PHE A 422 ALA A 424 0
SHEET 2 F 5 MET A 511 VAL A 516 1 O THR A 515 N ALA A 424
SHEET 3 F 5 TYR A 496 SER A 500 -1 N TYR A 496 O PHE A 514
SHEET 4 F 5 HIS A 443 ILE A 447 -1 N HIS A 446 O HIS A 499
SHEET 5 F 5 THR A 472 VAL A 475 -1 O VAL A 473 N PHE A 445
LINK NE2 HIS A 101 CU CU A1004 1555 1555 2.01
LINK ND1 HIS A 103 CU B CU A1002 1555 1555 1.86
LINK ND1 HIS A 103 CU A CU A1002 1555 1555 2.04
LINK NE2 HIS A 141 CU B CU A1002 1555 1555 1.87
LINK NE2 HIS A 141 CU A CU A1002 1555 1555 2.29
LINK NE2 HIS A 143 CU CU A1003 1555 1555 2.11
LINK NE2 HIS A 446 CU CU A1004 1555 1555 1.97
LINK NE2 HIS A 448 CU CU A1003 1555 1555 2.02
LINK NE2 HIS A 499 CU CU A1003 1555 1555 2.18
LINK NE2 HIS A 501 CU A CU A1002 1555 1555 2.09
LINK NE2 HIS A 501 CU B CU A1002 1555 1555 2.16
LINK CU CU A1003 O O A1005 1555 1555 1.88
LINK CU CU A1003 O O A1006 1555 1555 2.20
LINK CU CU A1004 O O A1006 1555 1555 1.97
LINK CU CU A1004 OXTAACT A1007 1555 1555 1.99
LINK CU CU A1004 O BHOH A2002 1555 1555 2.11
CISPEP 1 ALA A 308 PRO A 309 0 6.44
SITE 1 AC1 7 HIS A 103 TRP A 139 HIS A 141 HIS A 501
SITE 2 AC1 7 CU A1003 O A1005 O A1006
SITE 1 AC2 8 HIS A 143 HIS A 446 HIS A 448 HIS A 499
SITE 2 AC2 8 CU A1002 CU A1004 O A1005 O A1006
SITE 1 AC3 8 HIS A 101 HIS A 103 HIS A 446 HIS A 448
SITE 2 AC3 8 CU A1003 O A1006 ACT A1007 HOH A2002
SITE 1 AC4 8 HIS A 141 HIS A 143 HIS A 499 HIS A 501
SITE 2 AC4 8 CU A1002 CU A1003 O A1006 HOH A2001
SITE 1 AC5 9 HIS A 101 HIS A 103 HIS A 141 HIS A 446
SITE 2 AC5 9 HIS A 448 CU A1002 CU A1003 CU A1004
SITE 3 AC5 9 O A1005
SITE 1 AC6 11 HIS A 101 HIS A 103 GLY A 104 ASP A 112
SITE 2 AC6 11 HIS A 446 HIS A 448 GLY A 449 THR A 450
SITE 3 AC6 11 CU A1004 HOH A2002 HOH A2004
CRYST1 50.467 91.177 53.300 90.00 102.90 90.00 P 1 21 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 0.019815 0.000000 0.004538 0.00000
SCALE2 0.000000 0.010968 0.000000 0.00000
SCALE3 0.000000 0.000000 0.019248 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
