HEADER LYASE 11-SEP-05 2C14
TITLE 5-(4-CARBOXY-2-OXO-BUTYLAMINO)-4-OXO-PENTANOIC ACID ACID BOUND TO
TITLE 2 PORPHOBILINOGEN SYNTHASE FROM PSEUDOMONAS AERUGINOSA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DELTA-AMINOLEVULINIC ACID DEHYDRATASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: PORPHOBILINOGEN SYNTHASE, ALAD, ALADH;
COMPND 5 EC: 4.2.1.24;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PSEUDOMONAS AERUGINOSA;
SOURCE 3 ORGANISM_TAXID: 287;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_VECTOR: PET3A
KEYWDS ENZYME MECHANISM, METALLOENZYME, PORPHOBILINOGEN SYNTHASE,
KEYWDS 2 COCRYSTALLIZATION, LYASE, PORPHYRIN BIOSYNTHESIS
EXPDTA X-RAY DIFFRACTION
AUTHOR F.FRERE,M.NENTWICH,S.GACOND,D.W.HEINZ,R.NEIER,N.FRANKENBERG-DINKEL
REVDAT 5 13-DEC-23 2C14 1 LINK
REVDAT 4 08-MAY-19 2C14 1 REMARK LINK
REVDAT 3 24-FEB-09 2C14 1 VERSN
REVDAT 2 12-JUL-06 2C14 1 JRNL
REVDAT 1 20-JUN-06 2C14 0
JRNL AUTH F.FRERE,M.NENTWICH,S.GACOND,D.W.HEINZ,R.NEIER,
JRNL AUTH 2 N.FRANKENBERG-DINKEL
JRNL TITL PROBING THE ACTIVE SITE OF PSEUDOMONAS AERUGINOSA
JRNL TITL 2 PORPHOBILINOGEN SYNTHASE USING NEWLY DEVELOPED INHIBITORS.
JRNL REF BIOCHEMISTRY V. 45 8243 2006
JRNL REFN ISSN 0006-2960
JRNL PMID 16819823
JRNL DOI 10.1021/BI052611F
REMARK 2
REMARK 2 RESOLUTION. 1.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0005
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 89.80
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.8
REMARK 3 NUMBER OF REFLECTIONS : 52367
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.160
REMARK 3 R VALUE (WORKING SET) : 0.158
REMARK 3 FREE R VALUE : 0.201
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2802
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.90
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.95
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3664
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.2420
REMARK 3 BIN FREE R VALUE SET COUNT : 200
REMARK 3 BIN FREE R VALUE : 0.3090
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5149
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 2
REMARK 3 SOLVENT ATOMS : 723
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 18.02
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.46000
REMARK 3 B22 (A**2) : 0.46000
REMARK 3 B33 (A**2) : -0.91000
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 OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.148
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.136
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.089
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.982
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.962
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.937
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 5770 ; 0.016 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 7893 ; 1.525 ; 1.971
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 757 ; 5.917 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 284 ;35.899 ;23.239
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 951 ;14.812 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 64 ;18.464 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 858 ; 0.104 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4624 ; 0.007 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 2915 ; 0.231 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 4036 ; 0.295 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 575 ; 0.143 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 136 ; 0.203 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 65 ; 0.162 ; 0.200
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 3737 ; 0.788 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 5855 ; 1.207 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2299 ; 2.115 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2038 ; 3.128 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS. 5-(4-CARBOXY-2-OXO-BUTYLAMINO)-4-OXO- PENTANOIC ACID
REMARK 3 WAS INITIALLY BOUND TO K 205 AND K260 VIA SCHIFF BASES. A ALDOLE
REMARK 3 ADDITION RESULTED IN THE MODIFIED RESIDUE IN POSITION 205 THAT
REMARK 3 IS ADDITIONALLY BOUND TO THE AMINO MOIETY OF K260 VIA A SINGLE
REMARK 3 BOND.
REMARK 4
REMARK 4 2C14 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 11-SEP-05.
REMARK 100 THE DEPOSITION ID IS D_1290025607.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 09-FEB-05
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 7.50
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : BESSY
REMARK 200 BEAMLINE : 14.1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.98010
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL MONOCHROMATOR
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 55853
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900
REMARK 200 RESOLUTION RANGE LOW (A) : 40.130
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.8
REMARK 200 DATA REDUNDANCY : 7.800
REMARK 200 R MERGE (I) : 0.16000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.94
REMARK 200 COMPLETENESS FOR SHELL (%) : 95.2
REMARK 200 DATA REDUNDANCY IN SHELL : 7.00
REMARK 200 R MERGE FOR SHELL (I) : 0.48000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: PDB ENTRY 1B4K
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 46.60
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.30
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: HANGING DROP IN 24-WELL LIMBRO PLATES.
REMARK 280 DROPS MADE OF 5 MICROL PROTEIN SOLUTION (10 MG/ML PROTEIN, 50 MM
REMARK 280 TRIS-HCL, PH 7.5, 5 MM MGCL2, 1MM NACL, 1 MM 5-(4-CARBOXY-2-OXO-
REMARK 280 BUTYLAMINO)-4-OXO-PENTANOIC ACID MONOSODIUM SALT)) PLUS 5 MICROL
REMARK 280 RESERVOIR SOLUTION (18.0 % (W/V) PEG-3350, 200 MM LINO3), PH
REMARK 280 7.50, VAPOR DIFFUSION, HANGING DROP
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 4 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -Y+1/2,X+1/2,Z
REMARK 290 4555 Y+1/2,-X+1/2,Z
REMARK 290 5555 -X+1/2,Y+1/2,-Z
REMARK 290 6555 X+1/2,-Y+1/2,-Z
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-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 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 63.43850
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 63.43850
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 63.43850
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 63.43850
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 63.43850
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 63.43850
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 63.43850
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 63.43850
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 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: OCTAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: OCTAMERIC
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 350 BIOMT1 2 0.000000 -1.000000 0.000000 190.31550
REMARK 350 BIOMT2 2 1.000000 0.000000 0.000000 -63.43850
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 3 0.000000 1.000000 0.000000 63.43850
REMARK 350 BIOMT2 3 -1.000000 0.000000 0.000000 190.31550
REMARK 350 BIOMT3 3 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 4 -1.000000 0.000000 0.000000 253.75400
REMARK 350 BIOMT2 4 0.000000 -1.000000 0.000000 126.87700
REMARK 350 BIOMT3 4 0.000000 0.000000 1.000000 0.00000
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A2010 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A2015 LIES ON A SPECIAL POSITION.
REMARK 375 HOH B2014 LIES ON A SPECIAL POSITION.
REMARK 375 HOH B2016 LIES ON A SPECIAL POSITION.
REMARK 400
REMARK 400 COMPOUND
REMARK 400 ENGINEERED RESIDUE IN CHAIN A, ILE 199 TO VAL
REMARK 400 ENGINEERED RESIDUE IN CHAIN B, ILE 199 TO VAL
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 SER A 2
REMARK 465 ARG A 337
REMARK 465 MET B 1
REMARK 465 SER B 222
REMARK 465 ASN B 223
REMARK 465 LEU B 224
REMARK 465 GLY B 225
REMARK 465 LYS B 226
REMARK 465 GLY B 227
REMARK 465 ARG B 337
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 GLY A 336 CA C O
REMARK 470 GLY B 336 CA C O
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 NH1 ARG A 26 O HOH A 2062 1.48
REMARK 500 C8 CYJ B 205 NZ LYS B 260 1.89
REMARK 500
REMARK 500 REMARK: NULL
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 A 275 OG1 THR B 4 3645 2.12
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 ARG A 25 N ARG A 25 CA 0.229
REMARK 500 ALA A 204 C CYJ A 205 N 0.191
REMARK 500 ALA B 204 C CYJ B 205 N 0.216
REMARK 500 CYJ B 205 C TYR B 206 N 0.196
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 ALA A 129 144.09 179.89
REMARK 500 ALA A 204 76.12 -118.92
REMARK 500 TYR A 232 -47.50 -138.77
REMARK 500 PRO A 261 -169.95 -63.29
REMARK 500 ALA B 129 142.39 -175.86
REMARK 500 TYR B 232 -39.63 -142.26
REMARK 500 PRO B 261 -164.49 -65.82
REMARK 500 ARG B 335 69.27 -172.28
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 ALA A 204 11.60
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 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A2041 DISTANCE = 7.14 ANGSTROMS
REMARK 525 HOH A2046 DISTANCE = 6.84 ANGSTROMS
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 MG A1336 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 245 OE1
REMARK 620 2 HOH A2245 O 178.2
REMARK 620 3 HOH A2246 O 80.5 100.9
REMARK 620 4 HOH A2303 O 90.3 88.6 91.7
REMARK 620 5 HOH A2304 O 97.7 83.4 88.6 172.0
REMARK 620 6 HOH A2306 O 82.9 95.9 161.3 97.0 85.1
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B1336 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU B 245 OE1
REMARK 620 2 HOH B2258 O 175.7
REMARK 620 3 HOH B2260 O 81.5 100.4
REMARK 620 4 HOH B2308 O 98.2 85.7 86.7
REMARK 620 5 HOH B2310 O 90.4 85.7 94.5 171.4
REMARK 620 6 HOH B2311 O 80.5 98.1 160.0 87.3 94.3
REMARK 620 N 1 2 3 4 5
REMARK 700
REMARK 700 SHEET
REMARK 700 DETERMINATION METHOD: DSSP
REMARK 700 THE SHEETS PRESENTED AS "AA" IN EACH CHAIN ON SHEET RECORDS
REMARK 700 BELOW IS ACTUALLY AN 11-STRANDED BARREL THIS IS REPRESENTED BY
REMARK 700 A 12-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS
REMARK 700 ARE IDENTICAL.
REMARK 700 THE SHEETS PRESENTED AS "BA" IN EACH CHAIN ON SHEET RECORDS
REMARK 700 BELOW IS ACTUALLY AN 11-STRANDED BARREL THIS IS REPRESENTED BY
REMARK 700 A 12-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS
REMARK 700 ARE IDENTICAL.
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A1336
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B1336
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1B4K RELATED DB: PDB
REMARK 900 HIGH RESOLUTION CRYSTAL STRUCTURE OF A MG2- DEPENDENT 5-
REMARK 900 AMINOLEVULINIC ACID DEHYDRATASE
REMARK 900 RELATED ID: 1GZG RELATED DB: PDB
REMARK 900 COMPLEX OF A MG2-DEPENDENT PORPHOBILINOGEN SYNTHASE (MUTANT D139N)
REMARK 900 WITH 5-FLUOROLEVULINIC ACID
REMARK 900 RELATED ID: 1W56 RELATED DB: PDB
REMARK 900 STEPWISE INTRODUCTION OF ZINC BINDING SITE INTO PORPHOBILINOGEN
REMARK 900 SYNTHASE OF PSEUDOMONAS AERUGINOSA (MUTANTIONS A129C AND D131C)
REMARK 900 RELATED ID: 1W5M RELATED DB: PDB
REMARK 900 STEPWISE INTRODUCTION OF ZINC BINDING SITE INTO PORPHOBILINOGEN
REMARK 900 SYNTHASE OF PSEUDOMONAS AERUGINOSA (MUTANTIONS A129C AND D139C)
REMARK 900 RELATED ID: 1W5N RELATED DB: PDB
REMARK 900 STEPWISE INTRODUCTION OF ZINC BINDING SITE INTO PORPHOBILINOGEN
REMARK 900 SYNTHASE OF PSEUDOMONAS AERUGINOSA (MUTANTIONS D131C AND D139C)
REMARK 900 RELATED ID: 1W5O RELATED DB: PDB
REMARK 900 STEPWISE INTRODUCTION OF ZINC BINDING SITE INTO PORPHOBILINOGEN
REMARK 900 SYNTHASE OF PSEUDOMONAS AERUGINOSA (MUTANTIONS A129C, D131C AND
REMARK 900 D139C )
REMARK 900 RELATED ID: 1W5P RELATED DB: PDB
REMARK 900 STEPWISE INTRODUCTION OF ZINC BINDING SITE INTO PORPHOBILINOGEN
REMARK 900 SYNTHASE OF PSEUDOMONAS AERUGINOSA (MUTANTIONS A129C, D131C, D139C,
REMARK 900 P132E)
REMARK 900 RELATED ID: 1W5Q RELATED DB: PDB
REMARK 900 STEPWISE INTRODUCTION OF ZINC BINDING SITE INTO PORPHOBILINOGEN
REMARK 900 SYNTHASE OF PSEUDOMONAS AERUGINOSA (MUTANTIONS A129C, D131C, D139C,
REMARK 900 P132E, K229R)
REMARK 900 RELATED ID: 1W54 RELATED DB: PDB
REMARK 900 STEPWISE INTRODUCTION OF A ZINC BINDING SITE INTO PORPHOBILINOGEN
REMARK 900 SYNTHASE FROM PSEUDOMONAS AERUGINOSA (MUTATION D139C)
REMARK 900 RELATED ID: 2C13 RELATED DB: PDB
REMARK 900 5-HYDROXY-LEVULINIC ACID BOUND TO PORPHOBILINOGEN SYNTHASE FROM
REMARK 900 PSEUDOMONAS AERUGINOSA
REMARK 900 RELATED ID: 2C15 RELATED DB: PDB
REMARK 900 5-(4-CARBOXY-2-OXO-BUTOXY)-4-OXO- PENTANOIC ACID ACID BOUND TO
REMARK 900 PORPHOBILINOGEN SYNTHASE FROM PSEUDOMONAS AERUGINOSA
REMARK 900 RELATED ID: 2C16 RELATED DB: PDB
REMARK 900 5-(4-CARBOXY-2-OXO-BUTANE-1-SULFINYL)-4 -OXO-PENTANOIC ACID ACID
REMARK 900 BOUND TO PORPHOBILINOGEN SYNTHASE FROM PSEUDOMONAS AERUGINOSA
REMARK 900 RELATED ID: 2C18 RELATED DB: PDB
REMARK 900 5-(4-CARBOXY-2-OXO-BUTANE-1-SULFONYL)-4 -OXO-PENTANOIC ACID BOUND
REMARK 900 TO PORPHOBILINOGEN SYNTHASE FROM PSEUDOMONAS AERUGINOSA
REMARK 900 RELATED ID: 2C19 RELATED DB: PDB
REMARK 900 5-(4-CARBOXY-2-OXO-BUTYLSULFANYL)-4-OXO- PENTANOIC ACID ACID BOUND
REMARK 900 TO PORPHOBILINOGEN SYNTHASE FROM PSEUDOMONAS AERUGINOSA
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 I199V EXCHANGE AS CLONING ARTEFACT
DBREF 2C14 A 1 337 UNP Q59643 HEM2_PSEAE 1 337
DBREF 2C14 B 1 337 UNP Q59643 HEM2_PSEAE 1 337
SEQADV 2C14 VAL A 199 UNP Q59643 ILE 199 ENGINEERED MUTATION
SEQADV 2C14 VAL B 199 UNP Q59643 ILE 199 ENGINEERED MUTATION
SEQRES 1 A 337 MET SER PHE THR PRO ALA ASN ARG ALA TYR PRO TYR THR
SEQRES 2 A 337 ARG LEU ARG ARG ASN ARG ARG ASP ASP PHE SER ARG ARG
SEQRES 3 A 337 LEU VAL ARG GLU ASN VAL LEU THR VAL ASP ASP LEU ILE
SEQRES 4 A 337 LEU PRO VAL PHE VAL LEU ASP GLY VAL ASN GLN ARG GLU
SEQRES 5 A 337 SER ILE PRO SER MET PRO GLY VAL GLU ARG LEU SER ILE
SEQRES 6 A 337 ASP GLN LEU LEU ILE GLU ALA GLU GLU TRP VAL ALA LEU
SEQRES 7 A 337 GLY ILE PRO ALA LEU ALA LEU PHE PRO VAL THR PRO VAL
SEQRES 8 A 337 GLU LYS LYS SER LEU ASP ALA ALA GLU ALA TYR ASN PRO
SEQRES 9 A 337 GLU GLY ILE ALA GLN ARG ALA THR ARG ALA LEU ARG GLU
SEQRES 10 A 337 ARG PHE PRO GLU LEU GLY ILE ILE THR ASP VAL ALA LEU
SEQRES 11 A 337 ASP PRO PHE THR THR HIS GLY GLN ASP GLY ILE LEU ASP
SEQRES 12 A 337 ASP ASP GLY TYR VAL LEU ASN ASP VAL SER ILE ASP VAL
SEQRES 13 A 337 LEU VAL ARG GLN ALA LEU SER HIS ALA GLU ALA GLY ALA
SEQRES 14 A 337 GLN VAL VAL ALA PRO SER ASP MET MET ASP GLY ARG ILE
SEQRES 15 A 337 GLY ALA ILE ARG GLU ALA LEU GLU SER ALA GLY HIS THR
SEQRES 16 A 337 ASN VAL ARG VAL MET ALA TYR SER ALA CYJ TYR ALA SER
SEQRES 17 A 337 ALA TYR TYR GLY PRO PHE ARG ASP ALA VAL GLY SER ALA
SEQRES 18 A 337 SER ASN LEU GLY LYS GLY ASN LYS ALA THR TYR GLN MET
SEQRES 19 A 337 ASP PRO ALA ASN SER ASP GLU ALA LEU HIS GLU VAL ALA
SEQRES 20 A 337 ALA ASP LEU ALA GLU GLY ALA ASP MET VAL MET VAL LYS
SEQRES 21 A 337 PRO GLY MET PRO TYR LEU ASP ILE VAL ARG ARG VAL LYS
SEQRES 22 A 337 ASP GLU PHE ARG ALA PRO THR PHE VAL TYR GLN VAL SER
SEQRES 23 A 337 GLY GLU TYR ALA MET HIS MET GLY ALA ILE GLN ASN GLY
SEQRES 24 A 337 TRP LEU ALA GLU SER VAL ILE LEU GLU SER LEU THR ALA
SEQRES 25 A 337 PHE LYS ARG ALA GLY ALA ASP GLY ILE LEU THR TYR PHE
SEQRES 26 A 337 ALA LYS GLN ALA ALA GLU GLN LEU ARG ARG GLY ARG
SEQRES 1 B 337 MET SER PHE THR PRO ALA ASN ARG ALA TYR PRO TYR THR
SEQRES 2 B 337 ARG LEU ARG ARG ASN ARG ARG ASP ASP PHE SER ARG ARG
SEQRES 3 B 337 LEU VAL ARG GLU ASN VAL LEU THR VAL ASP ASP LEU ILE
SEQRES 4 B 337 LEU PRO VAL PHE VAL LEU ASP GLY VAL ASN GLN ARG GLU
SEQRES 5 B 337 SER ILE PRO SER MET PRO GLY VAL GLU ARG LEU SER ILE
SEQRES 6 B 337 ASP GLN LEU LEU ILE GLU ALA GLU GLU TRP VAL ALA LEU
SEQRES 7 B 337 GLY ILE PRO ALA LEU ALA LEU PHE PRO VAL THR PRO VAL
SEQRES 8 B 337 GLU LYS LYS SER LEU ASP ALA ALA GLU ALA TYR ASN PRO
SEQRES 9 B 337 GLU GLY ILE ALA GLN ARG ALA THR ARG ALA LEU ARG GLU
SEQRES 10 B 337 ARG PHE PRO GLU LEU GLY ILE ILE THR ASP VAL ALA LEU
SEQRES 11 B 337 ASP PRO PHE THR THR HIS GLY GLN ASP GLY ILE LEU ASP
SEQRES 12 B 337 ASP ASP GLY TYR VAL LEU ASN ASP VAL SER ILE ASP VAL
SEQRES 13 B 337 LEU VAL ARG GLN ALA LEU SER HIS ALA GLU ALA GLY ALA
SEQRES 14 B 337 GLN VAL VAL ALA PRO SER ASP MET MET ASP GLY ARG ILE
SEQRES 15 B 337 GLY ALA ILE ARG GLU ALA LEU GLU SER ALA GLY HIS THR
SEQRES 16 B 337 ASN VAL ARG VAL MET ALA TYR SER ALA CYJ TYR ALA SER
SEQRES 17 B 337 ALA TYR TYR GLY PRO PHE ARG ASP ALA VAL GLY SER ALA
SEQRES 18 B 337 SER ASN LEU GLY LYS GLY ASN LYS ALA THR TYR GLN MET
SEQRES 19 B 337 ASP PRO ALA ASN SER ASP GLU ALA LEU HIS GLU VAL ALA
SEQRES 20 B 337 ALA ASP LEU ALA GLU GLY ALA ASP MET VAL MET VAL LYS
SEQRES 21 B 337 PRO GLY MET PRO TYR LEU ASP ILE VAL ARG ARG VAL LYS
SEQRES 22 B 337 ASP GLU PHE ARG ALA PRO THR PHE VAL TYR GLN VAL SER
SEQRES 23 B 337 GLY GLU TYR ALA MET HIS MET GLY ALA ILE GLN ASN GLY
SEQRES 24 B 337 TRP LEU ALA GLU SER VAL ILE LEU GLU SER LEU THR ALA
SEQRES 25 B 337 PHE LYS ARG ALA GLY ALA ASP GLY ILE LEU THR TYR PHE
SEQRES 26 B 337 ALA LYS GLN ALA ALA GLU GLN LEU ARG ARG GLY ARG
MODRES 2C14 CYJ A 205 LYS
MODRES 2C14 CYJ B 205 LYS
HET CYJ A 205 24
HET CYJ B 205 24
HET MG A1336 1
HET MG B1336 1
HETNAM CYJ (Z)-N~6~-[(4R,5S)-5-(2-CARBOXYETHYL)-4-(CARBOXYMETHYL)
HETNAM 2 CYJ PIPERIDIN-3-YLIDENE]-L-LYSINE
HETNAM MG MAGNESIUM ION
HETSYN CYJ 2-AMINO-6-(3-CARBOXY-1-[(4-CARBOXY-2-OXO-BUTYLAMINO)-
HETSYN 2 CYJ METHYL]-PROPYLIDENEAMINO)-HEXANOIC ACID
FORMUL 1 CYJ 2(C16 H27 N3 O6)
FORMUL 3 MG 2(MG 2+)
FORMUL 5 HOH *723(H2 O)
HELIX 1 1 ASP A 21 ARG A 29 1 9
HELIX 2 2 THR A 34 ASP A 36 5 3
HELIX 3 3 ILE A 65 LEU A 78 1 14
HELIX 4 4 PRO A 90 LYS A 94 5 5
HELIX 5 5 ALA A 98 ASN A 103 5 6
HELIX 6 6 GLY A 106 PHE A 119 1 14
HELIX 7 7 LEU A 149 GLY A 168 1 20
HELIX 8 8 GLY A 180 ALA A 192 1 13
HELIX 9 9 TYR A 211 VAL A 218 1 8
HELIX 10 10 SER A 220 GLY A 225 1 6
HELIX 11 11 SER A 239 GLU A 252 1 14
HELIX 12 12 GLY A 262 PRO A 264 5 3
HELIX 13 13 TYR A 265 ARG A 277 1 13
HELIX 14 14 VAL A 285 ASN A 298 1 14
HELIX 15 15 SER A 304 GLY A 317 1 14
HELIX 16 16 PHE A 325 ARG A 335 1 11
HELIX 17 17 ASP B 21 ARG B 29 1 9
HELIX 18 18 THR B 34 ASP B 36 5 3
HELIX 19 19 ILE B 65 GLY B 79 1 15
HELIX 20 20 PRO B 90 LYS B 94 5 5
HELIX 21 21 ALA B 98 ASN B 103 5 6
HELIX 22 22 GLY B 106 PHE B 119 1 14
HELIX 23 23 LEU B 149 GLY B 168 1 20
HELIX 24 24 GLY B 180 ALA B 192 1 13
HELIX 25 25 SER B 208 TYR B 210 5 3
HELIX 26 26 TYR B 211 VAL B 218 1 8
HELIX 27 27 ASN B 228 TYR B 232 5 5
HELIX 28 28 SER B 239 GLU B 252 1 14
HELIX 29 29 GLY B 262 PRO B 264 5 3
HELIX 30 30 TYR B 265 ARG B 277 1 13
HELIX 31 31 VAL B 285 ASN B 298 1 14
HELIX 32 32 SER B 304 GLY B 317 1 14
HELIX 33 33 PHE B 325 ARG B 335 1 11
SHEET 1 AA12 LEU A 38 LEU A 45 0
SHEET 2 AA12 GLY A 320 THR A 323 1 O ILE A 321 N ILE A 39
SHEET 3 AA12 THR A 280 GLN A 284 1 O VAL A 282 N LEU A 322
SHEET 4 AA12 MET A 256 VAL A 259 1 O VAL A 257 N PHE A 281
SHEET 5 AA12 ARG A 198 ALA A 204 1 O ALA A 201 N MET A 258
SHEET 6 AA12 VAL A 171 PRO A 174 1 O VAL A 172 N MET A 200
SHEET 7 AA12 GLY A 123 VAL A 128 1 O ILE A 124 N VAL A 171
SHEET 8 AA12 ALA A 82 PRO A 87 1 O LEU A 83 N ILE A 125
SHEET 9 AA12 LEU A 38 LEU A 45 1 O LEU A 38 N ALA A 82
SHEET 10 AA12 GLY A 320 THR A 323 1 O ILE A 321 N ILE A 39
SHEET 11 AA12 THR A 280 GLN A 284 1 O VAL A 282 N LEU A 322
SHEET 12 AA12 LEU A 38 LEU A 45 0
SHEET 1 BA12 LEU B 38 LEU B 45 0
SHEET 2 BA12 GLY B 320 THR B 323 1 O ILE B 321 N ILE B 39
SHEET 3 BA12 THR B 280 GLN B 284 1 O VAL B 282 N LEU B 322
SHEET 4 BA12 MET B 256 VAL B 259 1 O VAL B 257 N PHE B 281
SHEET 5 BA12 ARG B 198 ALA B 204 1 O ALA B 201 N MET B 258
SHEET 6 BA12 VAL B 171 PRO B 174 1 O VAL B 172 N MET B 200
SHEET 7 BA12 GLY B 123 VAL B 128 1 O ILE B 124 N VAL B 171
SHEET 8 BA12 ALA B 82 PRO B 87 1 O LEU B 83 N ILE B 125
SHEET 9 BA12 LEU B 38 LEU B 45 1 O LEU B 38 N ALA B 82
SHEET 10 BA12 GLY B 320 THR B 323 1 O ILE B 321 N ILE B 39
SHEET 11 BA12 THR B 280 GLN B 284 1 O VAL B 282 N LEU B 322
SHEET 12 BA12 LEU B 38 LEU B 45 0
LINK C ALA A 204 N CYJ A 205 1555 1555 1.53
LINK C CYJ A 205 N TYR A 206 1555 1555 1.43
LINK C8 CYJ A 205 NZ LYS A 260 1555 1555 1.77
LINK C ALA B 204 N CYJ B 205 1555 1555 1.55
LINK C CYJ B 205 N TYR B 206 1555 1555 1.53
LINK OE1 GLU A 245 MG MG A1336 1555 1555 2.02
LINK MG MG A1336 O HOH A2245 1555 1555 2.19
LINK MG MG A1336 O HOH A2246 1555 1555 2.17
LINK MG MG A1336 O HOH A2303 1555 1555 2.06
LINK MG MG A1336 O HOH A2304 1555 1555 2.20
LINK MG MG A1336 O HOH A2306 1555 1555 2.22
LINK OE1 GLU B 245 MG MG B1336 1555 1555 2.05
LINK MG MG B1336 O HOH B2258 1555 1555 2.19
LINK MG MG B1336 O HOH B2260 1555 1555 2.18
LINK MG MG B1336 O HOH B2308 1555 1555 2.07
LINK MG MG B1336 O HOH B2310 1555 1555 2.25
LINK MG MG B1336 O HOH B2311 1555 1555 2.21
CISPEP 1 TYR A 10 PRO A 11 0 1.94
CISPEP 2 LYS A 260 PRO A 261 0 -7.59
CISPEP 3 TYR B 10 PRO B 11 0 -0.72
CISPEP 4 LYS B 260 PRO B 261 0 -6.00
SITE 1 AC1 6 GLU A 245 HOH A2245 HOH A2246 HOH A2303
SITE 2 AC1 6 HOH A2304 HOH A2306
SITE 1 AC2 6 GLU B 245 HOH B2258 HOH B2260 HOH B2308
SITE 2 AC2 6 HOH B2310 HOH B2311
CRYST1 126.877 126.877 86.098 90.00 90.00 90.00 P 4 21 2 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 0.007882 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007882 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011615 0.00000
MTRIX1 1 -0.836420 0.548070 -0.004240 198.32870 1
MTRIX2 1 0.548070 0.836430 -0.000330 -59.24349 1
MTRIX3 1 0.003370 -0.002600 -0.999990 -17.45602 1
(ATOM LINES ARE NOT SHOWN.)
END