HEADER OXIDOREDUCTASE 28-MAY-02 1LVN
TITLE CRYSTAL STRUCTURE OF E. COLI AMINE OXIDASE COMPLEXED WITH
TITLE 2 TRANYLCYPROMINE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: COPPER AMINE OXIDASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: TYRAMINE OXIDASE, 2-PHENYLENTHYLAMINE OXIDASE;
COMPND 5 EC: 1.4.3.6;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 CELLULAR_LOCATION: PERIPLASM;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: JM109;
SOURCE 8 EXPRESSION_SYSTEM_CELLULAR_LOCATION: PERIPLASM;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PKK233-3
KEYWDS INHIBITOR COMPLEX, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR C.M.WILMOT,S.E.PHILLIPS
REVDAT 5 15-NOV-23 1LVN 1 REMARK SEQADV LINK ATOM
REVDAT 4 11-OCT-17 1LVN 1 REMARK
REVDAT 3 24-FEB-09 1LVN 1 VERSN
REVDAT 2 04-JAN-05 1LVN 1 JRNL REMARK
REVDAT 1 05-AUG-03 1LVN 0
JRNL AUTH C.M.WILMOT,C.G.SAYSELL,A.BLESSINGTON,D.A.CONN,C.R.KURTIS,
JRNL AUTH 2 M.J.MCPHERSON,P.F.KNOWLES,S.E.PHILLIPS
JRNL TITL MEDICAL IMPLICATIONS FROM THE CRYSTAL STRUCTURE OF A
JRNL TITL 2 COPPER-CONTAINING AMINE OXIDASE COMPLEXED WITH THE
JRNL TITL 3 ANTIDEPRESSANT DRUG TRANYLCYPROMINE.
JRNL REF FEBS LETT. V. 576 301 2004
JRNL REFN ISSN 0014-5793
JRNL PMID 15498552
JRNL DOI 10.1016/J.FEBSLET.2004.09.031
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH C.G.SAYSELL,W.S.TAMBYRAJAH,J.M.MURRAY,C.M.WILMOT,
REMARK 1 AUTH 2 S.E.PHILLIPS,M.J.MCPHERSON,P.F.KNOWLES
REMARK 1 TITL PROBING THE CATALYTIC MECHANISM OF ESCHERICHIA COLI AMINE
REMARK 1 TITL 2 OXIDASE USING MUTATIONAL VARIANTS AND A REVERSIBLE INHIBITOR
REMARK 1 TITL 3 AS A SUBSTRATE ANALOGUE.
REMARK 1 REF BIOCHEM.J. V. 365 809 2002
REMARK 1 REFN ISSN 0264-6021
REMARK 1 REFERENCE 2
REMARK 1 AUTH C.M.WILMOT,J.M.MURRAY,G.ALTON,M.R.PARSONS,M.A.CONVERY,
REMARK 1 AUTH 2 V.BLAKELEY,A.S.CORNER,M.M.PALCIC,P.F.KNOWLES,M.J.MCPHERSON,
REMARK 1 AUTH 3 S.E.V.PHILLIPS
REMARK 1 TITL CATALYTIC MECHANISM OF THE QUINOENZYME AMINE OXIDASE FROM
REMARK 1 TITL 2 ESCHERICHIA COLI: EXPLORING THE REDUCTIVE HALF-REACTION.
REMARK 1 REF BIOCHEMISTRY V. 36 1608 1997
REMARK 1 REFN ISSN 0006-2960
REMARK 1 DOI 10.1021/BI962205J
REMARK 1 REFERENCE 3
REMARK 1 AUTH M.R.PARSONS,M.A.CONVERY,C.M.WILMOT,K.D.S.YADAV,V.BLAKELEY,
REMARK 1 AUTH 2 A.S.CORNER,S.E.PHILLIPS,M.J.MCPHERSON,P.F.KNOWLES
REMARK 1 TITL CRYSTAL STRUCTURE OF A QUINOENZYME: COPPER AMINE OXIDASE OF
REMARK 1 TITL 2 ESCHERICHIA COLI AT 2 ANGSTROMS RESOLUTION.
REMARK 1 REF STRUCTURE V. 3 1171 1995
REMARK 1 REFN ISSN 0969-2126
REMARK 1 REFERENCE 4
REMARK 1 AUTH J.M.MURRAY,C.G.SAYSELL,C.M.WILMOT,W.S.TAMBYRAJAH,J.JAEGER,
REMARK 1 AUTH 2 P.F.KNOWLES,S.E.PHILLIPS,M.J.MCPHERSON
REMARK 1 TITL THE ACTIVE SITE BASE CONTROLS COFACTOR REACTIVITY IN
REMARK 1 TITL 2 ESCHERICHIA COLI AMINE OXIDASE: X-RAY CRYSTALLOGRAPHIC
REMARK 1 TITL 3 STUDIES WITH MUTATIONAL VARIANTS.
REMARK 1 REF BIOCHEMISTRY V. 38 8217 1999
REMARK 1 REFN ISSN 0006-2960
REMARK 1 DOI 10.1021/BI9900469
REMARK 1 REFERENCE 5
REMARK 1 AUTH C.M.WILMOT,J.HAJDU,M.J.MCPHERSON,P.F.KNOWLES,S.E.PHILLIPS
REMARK 1 TITL VISUALIZATION OF DIOXYGEN BOUND TO COPPER DURING ENZYME
REMARK 1 TITL 2 CATALYSIS.
REMARK 1 REF SCIENCE V. 286 1724 1999
REMARK 1 REFN ISSN 0036-8075
REMARK 1 DOI 10.1126/SCIENCE.286.5445.1724
REMARK 2
REMARK 2 RESOLUTION. 2.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
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 AND HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 89.4
REMARK 3 NUMBER OF REFLECTIONS : 63358
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : FREE R
REMARK 3 FREE R VALUE TEST SET SELECTION : BY COMPARISON TO A COMPLETE
REMARK 3 DUMMY REFLECTION SET TO 1.8
REMARK 3 ANGSTROMS FOR THE CELL AND
REMARK 3 SPACE GROUP WITH THE
REMARK 3 REFLECTIONS RANDOMLY FLAGGED
REMARK 3 TO GIVE A MINIMUM OF 2000
REMARK 3 REFLECTIONS IN THE TEST SET
REMARK 3 AT 2.6 ANGSTROMS. THIS GAVE A
REMARK 3 PERCENTAGE OF 3.6% OF
REMARK 3 REFLECTIONS, WHICH WAS THE
REMARK 3 OVERALL PERCENT VALUE IN THE
REMARK 3 TEST SET TO 1.8 ANGSTROMS.
REMARK 3 R VALUE (WORKING SET) : 0.185
REMARK 3 FREE R VALUE : 0.229
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 3.200
REMARK 3 FREE R VALUE TEST SET COUNT : 2236
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) : NULL
REMARK 3 BIN FREE R VALUE : NULL
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 : 11365
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 6
REMARK 3 SOLVENT ATOMS : 1447
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 36.60
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.92100
REMARK 3 B22 (A**2) : 8.22900
REMARK 3 B33 (A**2) : -9.15000
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) : 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) : 0.008
REMARK 3 BOND ANGLES (DEGREES) : 1.600
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) : 1.208 ; 2.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.025 ; 4.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 2.326 ; 4.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 3.400 ; 5.500
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 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 CYCLES OF POSITIONAL POWELL MINIMIZATION AND INDIVIDUAL
REMARK 3 TEMPERATURE FACTOR REFINEMENT, WITH A MLF TARGET, AND
REMARK 3 AN OVERALL ANISOTROPIC TEMPERATURE FACTOR CORRECTION.
REMARK 3 COPPER ION RESTRAINTS WERE WEAKENED BY ADJUSTMENT OF
REMARK 3 THE NON-BONDED PARAMTERES, TO ENABLE THE COPPER ION/LIGAND
REMARK 3 DISTANCES TO REFLECT THE DATA MORE ACCURATELY.
REMARK 4
REMARK 4 1LVN COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 21-JUN-02.
REMARK 100 THE DEPOSITION ID IS D_1000016318.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 20-OCT-96
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 7.20
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SRS
REMARK 200 BEAMLINE : PX9.6
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.87
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MAR SCANNER 300 MM PLATE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM, ROTAVATA
REMARK 200 DATA SCALING SOFTWARE : CCP4 (AGROVATA, ROTAVATA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 64108
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.400
REMARK 200 RESOLUTION RANGE LOW (A) : 100.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 90.1
REMARK 200 DATA REDUNDANCY : 2.560
REMARK 200 R MERGE (I) : 0.07500
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 7.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.49
REMARK 200 COMPLETENESS FOR SHELL (%) : 80.6
REMARK 200 DATA REDUNDANCY IN SHELL : 2.10
REMARK 200 R MERGE FOR SHELL (I) : 0.25100
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.900
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: 1SPU
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 0.55
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.76
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.3M SODIUM CITRATE, 0.1M HEPES
REMARK 280 BUFFER, PH 7.2, INHIBITOR SOAKING SOLUTION 10:1 RATIO OF RACEMIC
REMARK 280 TRANYLCYPROMINE TO ENZYME MADE UP IN 1.4M SODIUM CITRATE, 0.1M
REMARK 280 HEPES BUFFER, PH 7.2. CRYSTAL SOAKED FOR 20 DAYS.CRYOPROTECTANT
REMARK 280 20% GLYCEROL, 1.4M SODIUM CITRATE BUFFER, PH 7.2, PH 7.20,
REMARK 280 SITTING DROP, TEMPERATURE 291.0K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 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
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 67.61800
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 39.81400
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 83.24100
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 39.81400
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 67.61800
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 83.24100
REMARK 290 SMTRY3 4 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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 16070 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 49890 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -112.0 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 HIS A 1
REMARK 465 GLY A 2
REMARK 465 GLY A 3
REMARK 465 GLU A 4
REMARK 465 ALA A 5
REMARK 465 HIS A 6
REMARK 465 LYS A 725
REMARK 465 ASP A 726
REMARK 465 LYS A 727
REMARK 465 HIS B 1
REMARK 465 GLY B 2
REMARK 465 GLY B 3
REMARK 465 GLU B 4
REMARK 465 ALA B 5
REMARK 465 ASP B 726
REMARK 465 LYS B 727
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O HOH A 1454 O HOH B 2737 2.03
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 A 311 C - N - CA ANGL. DEV. = 11.3 DEGREES
REMARK 500 PRO B 311 C - N - CA ANGL. DEV. = 9.1 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 ASP A 35 -120.64 57.92
REMARK 500 ASN A 143 19.28 58.11
REMARK 500 ASN A 172 55.77 35.66
REMARK 500 ASP A 182 -9.67 68.27
REMARK 500 ARG A 212 17.99 -65.61
REMARK 500 ASP A 231 27.82 48.58
REMARK 500 LYS A 277 120.41 -179.68
REMARK 500 ARG A 326 -127.30 53.64
REMARK 500 THR A 344 58.09 37.06
REMARK 500 VAL A 356 -52.96 -123.08
REMARK 500 TRP A 376 -32.79 -130.97
REMARK 500 VAL A 536 96.76 -61.14
REMARK 500 PRO A 582 -7.99 -58.75
REMARK 500 PRO A 623 -8.24 -56.82
REMARK 500 LEU A 631 79.89 -115.33
REMARK 500 TYR A 654 73.50 -116.17
REMARK 500 ASP B 35 -121.59 63.98
REMARK 500 ASP B 147 35.93 71.30
REMARK 500 ASP B 182 -9.66 60.47
REMARK 500 LYS B 277 135.54 -176.34
REMARK 500 ARG B 326 -124.07 58.42
REMARK 500 THR B 344 59.61 36.32
REMARK 500 GLU B 359 139.29 -170.84
REMARK 500 SER B 361 176.06 175.79
REMARK 500 TRP B 376 -39.59 -137.07
REMARK 500 LYS B 379 99.14 -69.25
REMARK 500 LEU B 382 66.32 -106.96
REMARK 500 ASP B 535 76.55 -116.85
REMARK 500 VAL B 536 90.03 -59.17
REMARK 500 PRO B 645 -14.98 -48.75
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 CU A 801 CU
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 524 NE2
REMARK 620 2 HIS A 526 NE2 103.0
REMARK 620 3 HIS A 689 ND1 99.4 147.5
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 802 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 533 OD2
REMARK 620 2 LEU A 534 O 105.5
REMARK 620 3 ASP A 535 OD2 87.3 78.5
REMARK 620 4 ASP A 678 OD2 96.4 156.5 94.3
REMARK 620 5 ALA A 679 O 91.2 91.1 168.6 97.1
REMARK 620 6 HOH A1142 O 178.2 74.3 94.4 84.0 87.0
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 803 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 573 OE1
REMARK 620 2 TYR A 667 O 101.5
REMARK 620 3 GLU A 672 OE2 87.6 127.9
REMARK 620 4 HOH A1305 O 163.4 91.1 76.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CU B 801 CU
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 526 NE2
REMARK 620 2 HIS B 689 ND1 154.3
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 802 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 533 OD2
REMARK 620 2 LEU B 534 O 109.6
REMARK 620 3 ASP B 535 OD2 92.7 78.5
REMARK 620 4 ASP B 678 OD2 97.3 152.4 94.7
REMARK 620 5 ALA B 679 O 89.6 92.6 171.0 93.6
REMARK 620 6 HOH B2151 O 173.2 71.5 94.1 82.5 83.6
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 803 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU B 573 OE1
REMARK 620 2 GLU B 573 OE2 48.6
REMARK 620 3 TYR B 667 O 102.8 77.5
REMARK 620 4 GLU B 672 OE2 103.5 105.3 146.5
REMARK 620 5 HOH B2176 O 76.6 115.6 86.3 119.9
REMARK 620 6 HOH B2180 O 165.9 142.1 76.1 83.2 89.3
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 CU A 801
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 802
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 803
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU B 801
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 802
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 803
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1OAC RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF A QUINOENZYME: COPPER AMINE OXIDASE OF
REMARK 900 ESCHERICHIA COLI AT 2 A RESOLUTION.
REMARK 900 RELATED ID: 1SPU RELATED DB: PDB
REMARK 900 STRUCTURE OF OXIDOREDUCTASE
REMARK 900 RELATED ID: 1D6U RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF E. COLI AMINE OXIDASE ANAEROBICALLY REDUCED
REMARK 900 WITH -PHENYLETHYLAMINE
REMARK 900 RELATED ID: 1D6Y RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF E. COLI COPPER-CONTAINING AMINE OXIDASE
REMARK 900 ANAEROBICALLY REDUCED WITH B-PHENYLETHYLAMINE AND COMPLEXED WITH
REMARK 900 NITRIC OXIDE.
REMARK 900 RELATED ID: 1D6Z RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE AEROBICALLY FREEZE TRAPPED RATE-
REMARK 900 DETERMINING CATALYTIC INTERMEDIATE OF E. COLI COPPER- CONTAINING
REMARK 900 AMINE OXIDASE.
REMARK 900 RELATED ID: 1DYU RELATED DB: PDB
REMARK 900 THE ACTIVE SITE BASE CONTROLS COFACTOR REACTIVITY IN ESCHERICHIA
REMARK 900 COLI AMINE OXIDASE: X-RAY CRYSTALLOGRAPHIC STUDIES WITH MUTATIONAL
REMARK 900 VARIANTS.
DBREF 1LVN A 1 727 UNP P46883 AMO_ECOLI 31 757
DBREF 1LVN B 1 727 UNP P46883 AMO_ECOLI 31 757
SEQADV 1LVN TYT A 466 UNP P46883 TYR 496 MODIFIED RESIDUE
SEQADV 1LVN TYT B 466 UNP P46883 TYR 496 MODIFIED RESIDUE
SEQRES 1 A 727 HIS GLY GLY GLU ALA HIS MET VAL PRO MET ASP LYS THR
SEQRES 2 A 727 LEU LYS GLU PHE GLY ALA ASP VAL GLN TRP ASP ASP TYR
SEQRES 3 A 727 ALA GLN LEU PHE THR LEU ILE LYS ASP GLY ALA TYR VAL
SEQRES 4 A 727 LYS VAL LYS PRO GLY ALA GLN THR ALA ILE VAL ASN GLY
SEQRES 5 A 727 GLN PRO LEU ALA LEU GLN VAL PRO VAL VAL MET LYS ASP
SEQRES 6 A 727 ASN LYS ALA TRP VAL SER ASP THR PHE ILE ASN ASP VAL
SEQRES 7 A 727 PHE GLN SER GLY LEU ASP GLN THR PHE GLN VAL GLU LYS
SEQRES 8 A 727 ARG PRO HIS PRO LEU ASN ALA LEU THR ALA ASP GLU ILE
SEQRES 9 A 727 LYS GLN ALA VAL GLU ILE VAL LYS ALA SER ALA ASP PHE
SEQRES 10 A 727 LYS PRO ASN THR ARG PHE THR GLU ILE SER LEU LEU PRO
SEQRES 11 A 727 PRO ASP LYS GLU ALA VAL TRP ALA PHE ALA LEU GLU ASN
SEQRES 12 A 727 LYS PRO VAL ASP GLN PRO ARG LYS ALA ASP VAL ILE MET
SEQRES 13 A 727 LEU ASP GLY LYS HIS ILE ILE GLU ALA VAL VAL ASP LEU
SEQRES 14 A 727 GLN ASN ASN LYS LEU LEU SER TRP GLN PRO ILE LYS ASP
SEQRES 15 A 727 ALA HIS GLY MET VAL LEU LEU ASP ASP PHE ALA SER VAL
SEQRES 16 A 727 GLN ASN ILE ILE ASN ASN SER GLU GLU PHE ALA ALA ALA
SEQRES 17 A 727 VAL LYS LYS ARG GLY ILE THR ASP ALA LYS LYS VAL ILE
SEQRES 18 A 727 THR THR PRO LEU THR VAL GLY TYR PHE ASP GLY LYS ASP
SEQRES 19 A 727 GLY LEU LYS GLN ASP ALA ARG LEU LEU LYS VAL ILE SER
SEQRES 20 A 727 TYR LEU ASP VAL GLY ASP GLY ASN TYR TRP ALA HIS PRO
SEQRES 21 A 727 ILE GLU ASN LEU VAL ALA VAL VAL ASP LEU GLU GLN LYS
SEQRES 22 A 727 LYS ILE VAL LYS ILE GLU GLU GLY PRO VAL VAL PRO VAL
SEQRES 23 A 727 PRO MET THR ALA ARG PRO PHE ASP GLY ARG ASP ARG VAL
SEQRES 24 A 727 ALA PRO ALA VAL LYS PRO MET GLN ILE ILE GLU PRO GLU
SEQRES 25 A 727 GLY LYS ASN TYR THR ILE THR GLY ASP MET ILE HIS TRP
SEQRES 26 A 727 ARG ASN TRP ASP PHE HIS LEU SER MET ASN SER ARG VAL
SEQRES 27 A 727 GLY PRO MET ILE SER THR VAL THR TYR ASN ASP ASN GLY
SEQRES 28 A 727 THR LYS ARG LYS VAL MET TYR GLU GLY SER LEU GLY GLY
SEQRES 29 A 727 MET ILE VAL PRO TYR GLY ASP PRO ASP ILE GLY TRP TYR
SEQRES 30 A 727 PHE LYS ALA TYR LEU ASP SER GLY ASP TYR GLY MET GLY
SEQRES 31 A 727 THR LEU THR SER PRO ILE ALA ARG GLY LYS ASP ALA PRO
SEQRES 32 A 727 SER ASN ALA VAL LEU LEU ASN GLU THR ILE ALA ASP TYR
SEQRES 33 A 727 THR GLY VAL PRO MET GLU ILE PRO ARG ALA ILE ALA VAL
SEQRES 34 A 727 PHE GLU ARG TYR ALA GLY PRO GLU TYR LYS HIS GLN GLU
SEQRES 35 A 727 MET GLY GLN PRO ASN VAL SER THR GLU ARG ARG GLU LEU
SEQRES 36 A 727 VAL VAL ARG TRP ILE SER THR VAL GLY ASN TYT ASP TYR
SEQRES 37 A 727 ILE PHE ASP TRP ILE PHE HIS GLU ASN GLY THR ILE GLY
SEQRES 38 A 727 ILE ASP ALA GLY ALA THR GLY ILE GLU ALA VAL LYS GLY
SEQRES 39 A 727 VAL LYS ALA LYS THR MET HIS ASP GLU THR ALA LYS ASP
SEQRES 40 A 727 ASP THR ARG TYR GLY THR LEU ILE ASP HIS ASN ILE VAL
SEQRES 41 A 727 GLY THR THR HIS GLN HIS ILE TYR ASN PHE ARG LEU ASP
SEQRES 42 A 727 LEU ASP VAL ASP GLY GLU ASN ASN SER LEU VAL ALA MET
SEQRES 43 A 727 ASP PRO VAL VAL LYS PRO ASN THR ALA GLY GLY PRO ARG
SEQRES 44 A 727 THR SER THR MET GLN VAL ASN GLN TYR ASN ILE GLY ASN
SEQRES 45 A 727 GLU GLN ASP ALA ALA GLN LYS PHE ASP PRO GLY THR ILE
SEQRES 46 A 727 ARG LEU LEU SER ASN PRO ASN LYS GLU ASN ARG MET GLY
SEQRES 47 A 727 ASN PRO VAL SER TYR GLN ILE ILE PRO TYR ALA GLY GLY
SEQRES 48 A 727 THR HIS PRO VAL ALA LYS GLY ALA GLN PHE ALA PRO ASP
SEQRES 49 A 727 GLU TRP ILE TYR HIS ARG LEU SER PHE MET ASP LYS GLN
SEQRES 50 A 727 LEU TRP VAL THR ARG TYR HIS PRO GLY GLU ARG PHE PRO
SEQRES 51 A 727 GLU GLY LYS TYR PRO ASN ARG SER THR HIS ASP THR GLY
SEQRES 52 A 727 LEU GLY GLN TYR SER LYS ASP ASN GLU SER LEU ASP ASN
SEQRES 53 A 727 THR ASP ALA VAL VAL TRP MET THR THR GLY THR THR HIS
SEQRES 54 A 727 VAL ALA ARG ALA GLU GLU TRP PRO ILE MET PRO THR GLU
SEQRES 55 A 727 TRP VAL HIS THR LEU LEU LYS PRO TRP ASN PHE PHE ASP
SEQRES 56 A 727 GLU THR PRO THR LEU GLY ALA LEU LYS LYS ASP LYS
SEQRES 1 B 727 HIS GLY GLY GLU ALA HIS MET VAL PRO MET ASP LYS THR
SEQRES 2 B 727 LEU LYS GLU PHE GLY ALA ASP VAL GLN TRP ASP ASP TYR
SEQRES 3 B 727 ALA GLN LEU PHE THR LEU ILE LYS ASP GLY ALA TYR VAL
SEQRES 4 B 727 LYS VAL LYS PRO GLY ALA GLN THR ALA ILE VAL ASN GLY
SEQRES 5 B 727 GLN PRO LEU ALA LEU GLN VAL PRO VAL VAL MET LYS ASP
SEQRES 6 B 727 ASN LYS ALA TRP VAL SER ASP THR PHE ILE ASN ASP VAL
SEQRES 7 B 727 PHE GLN SER GLY LEU ASP GLN THR PHE GLN VAL GLU LYS
SEQRES 8 B 727 ARG PRO HIS PRO LEU ASN ALA LEU THR ALA ASP GLU ILE
SEQRES 9 B 727 LYS GLN ALA VAL GLU ILE VAL LYS ALA SER ALA ASP PHE
SEQRES 10 B 727 LYS PRO ASN THR ARG PHE THR GLU ILE SER LEU LEU PRO
SEQRES 11 B 727 PRO ASP LYS GLU ALA VAL TRP ALA PHE ALA LEU GLU ASN
SEQRES 12 B 727 LYS PRO VAL ASP GLN PRO ARG LYS ALA ASP VAL ILE MET
SEQRES 13 B 727 LEU ASP GLY LYS HIS ILE ILE GLU ALA VAL VAL ASP LEU
SEQRES 14 B 727 GLN ASN ASN LYS LEU LEU SER TRP GLN PRO ILE LYS ASP
SEQRES 15 B 727 ALA HIS GLY MET VAL LEU LEU ASP ASP PHE ALA SER VAL
SEQRES 16 B 727 GLN ASN ILE ILE ASN ASN SER GLU GLU PHE ALA ALA ALA
SEQRES 17 B 727 VAL LYS LYS ARG GLY ILE THR ASP ALA LYS LYS VAL ILE
SEQRES 18 B 727 THR THR PRO LEU THR VAL GLY TYR PHE ASP GLY LYS ASP
SEQRES 19 B 727 GLY LEU LYS GLN ASP ALA ARG LEU LEU LYS VAL ILE SER
SEQRES 20 B 727 TYR LEU ASP VAL GLY ASP GLY ASN TYR TRP ALA HIS PRO
SEQRES 21 B 727 ILE GLU ASN LEU VAL ALA VAL VAL ASP LEU GLU GLN LYS
SEQRES 22 B 727 LYS ILE VAL LYS ILE GLU GLU GLY PRO VAL VAL PRO VAL
SEQRES 23 B 727 PRO MET THR ALA ARG PRO PHE ASP GLY ARG ASP ARG VAL
SEQRES 24 B 727 ALA PRO ALA VAL LYS PRO MET GLN ILE ILE GLU PRO GLU
SEQRES 25 B 727 GLY LYS ASN TYR THR ILE THR GLY ASP MET ILE HIS TRP
SEQRES 26 B 727 ARG ASN TRP ASP PHE HIS LEU SER MET ASN SER ARG VAL
SEQRES 27 B 727 GLY PRO MET ILE SER THR VAL THR TYR ASN ASP ASN GLY
SEQRES 28 B 727 THR LYS ARG LYS VAL MET TYR GLU GLY SER LEU GLY GLY
SEQRES 29 B 727 MET ILE VAL PRO TYR GLY ASP PRO ASP ILE GLY TRP TYR
SEQRES 30 B 727 PHE LYS ALA TYR LEU ASP SER GLY ASP TYR GLY MET GLY
SEQRES 31 B 727 THR LEU THR SER PRO ILE ALA ARG GLY LYS ASP ALA PRO
SEQRES 32 B 727 SER ASN ALA VAL LEU LEU ASN GLU THR ILE ALA ASP TYR
SEQRES 33 B 727 THR GLY VAL PRO MET GLU ILE PRO ARG ALA ILE ALA VAL
SEQRES 34 B 727 PHE GLU ARG TYR ALA GLY PRO GLU TYR LYS HIS GLN GLU
SEQRES 35 B 727 MET GLY GLN PRO ASN VAL SER THR GLU ARG ARG GLU LEU
SEQRES 36 B 727 VAL VAL ARG TRP ILE SER THR VAL GLY ASN TYT ASP TYR
SEQRES 37 B 727 ILE PHE ASP TRP ILE PHE HIS GLU ASN GLY THR ILE GLY
SEQRES 38 B 727 ILE ASP ALA GLY ALA THR GLY ILE GLU ALA VAL LYS GLY
SEQRES 39 B 727 VAL LYS ALA LYS THR MET HIS ASP GLU THR ALA LYS ASP
SEQRES 40 B 727 ASP THR ARG TYR GLY THR LEU ILE ASP HIS ASN ILE VAL
SEQRES 41 B 727 GLY THR THR HIS GLN HIS ILE TYR ASN PHE ARG LEU ASP
SEQRES 42 B 727 LEU ASP VAL ASP GLY GLU ASN ASN SER LEU VAL ALA MET
SEQRES 43 B 727 ASP PRO VAL VAL LYS PRO ASN THR ALA GLY GLY PRO ARG
SEQRES 44 B 727 THR SER THR MET GLN VAL ASN GLN TYR ASN ILE GLY ASN
SEQRES 45 B 727 GLU GLN ASP ALA ALA GLN LYS PHE ASP PRO GLY THR ILE
SEQRES 46 B 727 ARG LEU LEU SER ASN PRO ASN LYS GLU ASN ARG MET GLY
SEQRES 47 B 727 ASN PRO VAL SER TYR GLN ILE ILE PRO TYR ALA GLY GLY
SEQRES 48 B 727 THR HIS PRO VAL ALA LYS GLY ALA GLN PHE ALA PRO ASP
SEQRES 49 B 727 GLU TRP ILE TYR HIS ARG LEU SER PHE MET ASP LYS GLN
SEQRES 50 B 727 LEU TRP VAL THR ARG TYR HIS PRO GLY GLU ARG PHE PRO
SEQRES 51 B 727 GLU GLY LYS TYR PRO ASN ARG SER THR HIS ASP THR GLY
SEQRES 52 B 727 LEU GLY GLN TYR SER LYS ASP ASN GLU SER LEU ASP ASN
SEQRES 53 B 727 THR ASP ALA VAL VAL TRP MET THR THR GLY THR THR HIS
SEQRES 54 B 727 VAL ALA ARG ALA GLU GLU TRP PRO ILE MET PRO THR GLU
SEQRES 55 B 727 TRP VAL HIS THR LEU LEU LYS PRO TRP ASN PHE PHE ASP
SEQRES 56 B 727 GLU THR PRO THR LEU GLY ALA LEU LYS LYS ASP LYS
MODRES 1LVN TYT A 466 TYR TYROSINE DERIVATIVE
MODRES 1LVN TYT B 466 TYR TYROSINE DERIVATIVE
HET TYT A 466 23
HET TYT B 466 23
HET CU A 801 1
HET CA A 802 1
HET CA A 803 1
HET CU B 801 1
HET CA B 802 1
HET CA B 803 1
HETNAM TYT TYROSINE DERIVATIVE
HETNAM CU COPPER (II) ION
HETNAM CA CALCIUM ION
HETSYN TYT 2-AMINO-3-[4-HYDROXY-6-OXO-3-(2-PHENYL-
HETSYN 2 TYT CYCLOPROPYLIMINO)-CYCLOHEXA-1,4-DIENYL]-PROPIONIC ACID
FORMUL 1 TYT 2(C18 H20 N2 O4)
FORMUL 3 CU 2(CU 2+)
FORMUL 4 CA 4(CA 2+)
FORMUL 9 HOH *1447(H2 O)
HELIX 1 1 MET A 10 GLY A 18 1 9
HELIX 2 2 THR A 73 GLN A 80 1 8
HELIX 3 3 THR A 100 ALA A 113 1 14
HELIX 4 4 ASP A 132 ASN A 143 1 12
HELIX 5 5 LEU A 188 ASN A 201 1 14
HELIX 6 6 SER A 202 ARG A 212 1 11
HELIX 7 7 ASP A 216 LYS A 218 5 3
HELIX 8 8 ASN A 255 HIS A 259 5 5
HELIX 9 9 LEU A 382 GLY A 388 1 7
HELIX 10 10 THR A 504 THR A 509 1 6
HELIX 11 11 ASN A 572 ALA A 577 1 6
HELIX 12 12 GLU A 625 LEU A 631 1 7
HELIX 13 13 SER A 632 LYS A 636 5 5
HELIX 14 14 GLY A 663 ASP A 670 1 8
HELIX 15 15 ARG A 692 TRP A 696 5 5
HELIX 16 16 MET B 10 GLY B 18 1 9
HELIX 17 17 THR B 73 GLN B 80 1 8
HELIX 18 18 THR B 100 LYS B 112 1 13
HELIX 19 19 ASP B 132 ASN B 143 1 12
HELIX 20 20 LEU B 188 ASN B 201 1 14
HELIX 21 21 SER B 202 LYS B 211 1 10
HELIX 22 22 ASP B 216 LYS B 218 5 3
HELIX 23 23 ASN B 255 ALA B 258 5 4
HELIX 24 24 LEU B 382 GLY B 388 1 7
HELIX 25 25 THR B 504 THR B 509 1 6
HELIX 26 26 ASN B 572 ALA B 577 1 6
HELIX 27 27 GLU B 625 LEU B 631 1 7
HELIX 28 28 GLY B 663 LYS B 669 1 7
HELIX 29 29 ARG B 692 TRP B 696 5 5
SHEET 1 A 3 VAL A 8 PRO A 9 0
SHEET 2 A 3 ALA A 68 VAL A 70 -1 N VAL A 70 O VAL A 8
SHEET 3 A 3 VAL A 62 MET A 63 -1 O VAL A 62 N TRP A 69
SHEET 1 B 5 ASP A 20 ASP A 24 0
SHEET 2 B 5 LEU A 29 LYS A 34 -1 O LEU A 29 N ASP A 24
SHEET 3 B 5 ALA A 37 VAL A 41 -1 N ALA A 37 O LYS A 34
SHEET 4 B 5 THR A 47 VAL A 50 -1 N ILE A 49 O LYS A 40
SHEET 5 B 5 GLN A 53 ALA A 56 -1 O GLN A 53 N VAL A 50
SHEET 1 C23 PHE A 87 GLN A 88 0
SHEET 2 C23 TYR A 316 THR A 319 1 O ILE A 318 N GLN A 88
SHEET 3 C23 MET A 322 TRP A 325 -1 N MET A 322 O THR A 319
SHEET 4 C23 TRP A 328 ASN A 335 -1 N TRP A 328 O TRP A 325
SHEET 5 C23 GLY A 339 ASP A 349 -1 N GLY A 339 O ASN A 335
SHEET 6 C23 THR A 352 PRO A 368 -1 O THR A 352 N ASP A 349
SHEET 7 C23 ALA A 380 TYR A 381 -1 O TYR A 381 N VAL A 367
SHEET 8 C23 THR A 352 PRO A 368 -1 N VAL A 367 O TYR A 381
SHEET 9 C23 HIS A 524 LEU A 534 -1 N GLN A 525 O PRO A 368
SHEET 10 C23 THR A 677 HIS A 689 -1 O VAL A 681 N LEU A 532
SHEET 11 C23 LEU A 638 ARG A 642 -1 O TRP A 639 N TRP A 682
SHEET 12 C23 THR A 677 HIS A 689 -1 N VAL A 680 O THR A 641
SHEET 13 C23 ASN A 540 PRO A 552 -1 N ASN A 541 O THR A 677
SHEET 14 C23 SER A 561 ILE A 570 -1 N THR A 562 O LYS A 551
SHEET 15 C23 ASN A 540 PRO A 552 -1 O LEU A 543 N ILE A 570
SHEET 16 C23 ILE A 585 GLU A 594 -1 O ILE A 585 N MET A 546
SHEET 17 C23 PRO A 600 ILE A 606 -1 N VAL A 601 O LYS A 593
SHEET 18 C23 MET A 699 TRP A 711 -1 O LEU A 707 N ILE A 606
SHEET 19 C23 ILE A 480 GLY A 488 -1 N ILE A 480 O LEU A 708
SHEET 20 C23 TYR A 468 HIS A 475 1 O ILE A 469 N GLY A 485
SHEET 21 C23 VAL A 448 SER A 461 -1 O LEU A 455 N PHE A 474
SHEET 22 C23 PRO A 420 HIS A 440 -1 O ALA A 426 N ILE A 460
SHEET 23 C23 VAL A 407 ALA A 414 -1 N VAL A 407 O VAL A 429
SHEET 1 D 4 ARG A 122 LEU A 129 0
SHEET 2 D 4 LYS A 151 ASP A 158 -1 O LYS A 151 N LEU A 129
SHEET 3 D 4 HIS A 161 ASP A 168 -1 O HIS A 161 N ASP A 158
SHEET 4 D 4 LYS A 173 ILE A 180 -1 O LYS A 173 N ASP A 168
SHEET 1 E 4 VAL A 220 LEU A 225 0
SHEET 2 E 4 LEU A 242 LEU A 249 -1 N LYS A 244 O LEU A 225
SHEET 3 E 4 LEU A 264 ASP A 269 -1 O ALA A 266 N VAL A 245
SHEET 4 E 4 LYS A 274 GLU A 280 -1 O LYS A 274 N ASP A 269
SHEET 1 F 2 ARG A 298 VAL A 299 0
SHEET 2 F 2 ALA B 722 LEU B 723 -1 N ALA B 722 O VAL A 299
SHEET 1 G 2 GLN A 307 ILE A 309 0
SHEET 2 G 2 GLN B 307 ILE B 309 -1 O GLN B 307 N ILE A 309
SHEET 1 H 3 VAL A 492 GLY A 494 0
SHEET 2 H 3 ILE A 519 THR A 522 -1 O VAL A 520 N LYS A 493
SHEET 3 H 3 GLY A 512 ASP A 516 -1 O THR A 513 N GLY A 521
SHEET 1 I 3 MET B 7 PRO B 9 0
SHEET 2 I 3 LYS B 67 SER B 71 -1 O VAL B 70 N VAL B 8
SHEET 3 I 3 VAL B 62 LYS B 64 -1 O VAL B 62 N TRP B 69
SHEET 1 J 5 ASP B 20 ASP B 24 0
SHEET 2 J 5 LEU B 29 LYS B 34 -1 O LEU B 29 N ASP B 24
SHEET 3 J 5 ALA B 37 VAL B 41 -1 O ALA B 37 N LYS B 34
SHEET 4 J 5 THR B 47 VAL B 50 -1 N ILE B 49 O LYS B 40
SHEET 5 J 5 GLN B 53 ALA B 56 -1 O GLN B 53 N VAL B 50
SHEET 1 K23 PHE B 87 GLN B 88 0
SHEET 2 K23 TYR B 316 THR B 319 1 O ILE B 318 N GLN B 88
SHEET 3 K23 MET B 322 TRP B 325 -1 O MET B 322 N THR B 319
SHEET 4 K23 TRP B 328 ASN B 335 -1 N TRP B 328 O TRP B 325
SHEET 5 K23 GLY B 339 ASP B 349 -1 O GLY B 339 N ASN B 335
SHEET 6 K23 THR B 352 PRO B 368 -1 O THR B 352 N ASP B 349
SHEET 7 K23 ALA B 380 TYR B 381 -1 O TYR B 381 N VAL B 367
SHEET 8 K23 THR B 352 PRO B 368 -1 N VAL B 367 O TYR B 381
SHEET 9 K23 HIS B 524 LEU B 534 -1 N GLN B 525 O PRO B 368
SHEET 10 K23 THR B 677 HIS B 689 -1 O VAL B 681 N LEU B 532
SHEET 11 K23 LEU B 638 ARG B 642 -1 O TRP B 639 N TRP B 682
SHEET 12 K23 THR B 677 HIS B 689 -1 O VAL B 680 N THR B 641
SHEET 13 K23 ASN B 540 PRO B 552 -1 N ASN B 541 O THR B 677
SHEET 14 K23 SER B 561 ILE B 570 -1 N THR B 562 O LYS B 551
SHEET 15 K23 ASN B 540 PRO B 552 -1 O LEU B 543 N ILE B 570
SHEET 16 K23 ILE B 585 GLU B 594 -1 O ILE B 585 N MET B 546
SHEET 17 K23 PRO B 600 ILE B 606 -1 N VAL B 601 O LYS B 593
SHEET 18 K23 MET B 699 TRP B 711 -1 O LEU B 707 N ILE B 606
SHEET 19 K23 ILE B 480 GLY B 488 -1 N ILE B 480 O LEU B 708
SHEET 20 K23 TYR B 468 HIS B 475 1 O ILE B 469 N GLY B 485
SHEET 21 K23 VAL B 448 SER B 461 -1 O LEU B 455 N PHE B 474
SHEET 22 K23 PRO B 420 HIS B 440 -1 O ALA B 426 N ILE B 460
SHEET 23 K23 VAL B 407 ALA B 414 -1 N VAL B 407 O VAL B 429
SHEET 1 L 4 ARG B 122 LEU B 129 0
SHEET 2 L 4 LYS B 151 ASP B 158 -1 O LYS B 151 N LEU B 129
SHEET 3 L 4 HIS B 161 ASP B 168 -1 O HIS B 161 N ASP B 158
SHEET 4 L 4 LYS B 173 ILE B 180 -1 O LYS B 173 N ASP B 168
SHEET 1 M 3 VAL B 220 ILE B 221 0
SHEET 2 M 3 LEU B 242 LEU B 249 -1 O TYR B 248 N ILE B 221
SHEET 3 M 3 PRO B 224 LEU B 225 -1 N LEU B 225 O LYS B 244
SHEET 1 N 4 VAL B 492 GLY B 494 0
SHEET 2 N 4 ILE B 519 THR B 522 -1 O VAL B 520 N LYS B 493
SHEET 3 N 4 GLY B 512 ASP B 516 -1 O THR B 513 N GLY B 521
SHEET 4 N 4 LYS B 274 GLU B 280 -1 O LYS B 274 N ASP B 269
LINK C ASN A 465 N TYT A 466 1555 1555 1.33
LINK C TYT A 466 N ASP A 467 1555 1555 1.33
LINK C ASN B 465 N TYT B 466 1555 1555 1.33
LINK C TYT B 466 N ASP B 467 1555 1555 1.33
LINK NE2 HIS A 524 CU CU A 801 1555 1555 2.27
LINK NE2 HIS A 526 CU CU A 801 1555 1555 2.04
LINK OD2 ASP A 533 CA CA A 802 1555 1555 2.39
LINK O LEU A 534 CA CA A 802 1555 1555 2.45
LINK OD2 ASP A 535 CA CA A 802 1555 1555 2.36
LINK OE1 GLU A 573 CA CA A 803 1555 1555 2.66
LINK O TYR A 667 CA CA A 803 1555 1555 2.33
LINK OE2 GLU A 672 CA CA A 803 1555 1555 2.85
LINK OD2 ASP A 678 CA CA A 802 1555 1555 2.35
LINK O ALA A 679 CA CA A 802 1555 1555 2.38
LINK ND1 HIS A 689 CU CU A 801 1555 1555 2.27
LINK CA CA A 802 O HOH A1142 1555 1555 2.65
LINK CA CA A 803 O HOH A1305 1555 1555 2.72
LINK NE2 HIS B 526 CU CU B 801 1555 1555 2.10
LINK OD2 ASP B 533 CA CA B 802 1555 1555 2.31
LINK O LEU B 534 CA CA B 802 1555 1555 2.54
LINK OD2 ASP B 535 CA CA B 802 1555 1555 2.39
LINK OE1 GLU B 573 CA CA B 803 1555 1555 2.50
LINK OE2 GLU B 573 CA CA B 803 1555 1555 2.79
LINK O TYR B 667 CA CA B 803 1555 1555 2.46
LINK OE2 GLU B 672 CA CA B 803 1555 1555 2.63
LINK OD2 ASP B 678 CA CA B 802 1555 1555 2.42
LINK O ALA B 679 CA CA B 802 1555 1555 2.26
LINK ND1 HIS B 689 CU CU B 801 1555 1555 2.14
LINK CA CA B 802 O HOH B2151 1555 1555 2.53
LINK CA CA B 803 O HOH B2176 1555 1555 2.64
LINK CA CA B 803 O HOH B2180 1555 1555 2.94
CISPEP 1 TRP A 696 PRO A 697 0 -0.36
CISPEP 2 TRP B 696 PRO B 697 0 -2.49
SITE 1 AC1 4 HIS A 524 HIS A 526 HIS A 689 HOH A1466
SITE 1 AC2 6 ASP A 533 LEU A 534 ASP A 535 ASP A 678
SITE 2 AC2 6 ALA A 679 HOH A1142
SITE 1 AC3 4 GLU A 573 TYR A 667 GLU A 672 HOH A1305
SITE 1 AC4 4 HIS B 524 HIS B 526 HIS B 689 HOH B2423
SITE 1 AC5 6 ASP B 533 LEU B 534 ASP B 535 ASP B 678
SITE 2 AC5 6 ALA B 679 HOH B2151
SITE 1 AC6 5 GLU B 573 TYR B 667 GLU B 672 HOH B2176
SITE 2 AC6 5 HOH B2180
CRYST1 135.236 166.482 79.628 90.00 90.00 90.00 P 21 21 21 8
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 0.007390 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006010 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012560 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
