HEADER HYDROLASE 20-JAN-14 4OIW
TITLE STRUCTURAL AND KINETIC BASES FOR THE METAL PREFERENCE OF THE M18
TITLE 2 AMINOPEPTIDASE FROM PSEUDOMONAS AERUGINOSA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROBABLE M18 FAMILY AMINOPEPTIDASE 2;
COMPND 3 CHAIN: A, B, C, D, E, F;
COMPND 4 EC: 3.4.11.-;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PSEUDOMONAS AERUGINOSA;
SOURCE 3 ORGANISM_TAXID: 208964;
SOURCE 4 STRAIN: ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228;
SOURCE 5 GENE: APEB, PA3247, PSEUDOMONAS AERUGINOSA;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21-DE3;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PVFT1S
KEYWDS DODECAMERIC TET STRUCTURE, ASPARTYL AMINOPEPTIDASE, PSEUDOMONAS
KEYWDS 2 AERUGINOSA, HISTIDINE MUTATION, M18 FAMILY, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR D.D.NGUYEN,R.PANDIAN,D.D.KIM,S.C.HA,H.J.YOON,K.S.KIM,K.H.YUN,J.H.KIM,
AUTHOR 2 K.K.KIM
REVDAT 5 08-NOV-23 4OIW 1 REMARK SEQADV LINK
REVDAT 4 17-SEP-14 4OIW 1 JRNL
REVDAT 3 23-APR-14 4OIW 1 JRNL
REVDAT 2 09-APR-14 4OIW 1 JRNL
REVDAT 1 02-APR-14 4OIW 0
JRNL AUTH D.D.NGUYEN,R.PANDIAN,D.KIM,S.C.HA,H.J.YOON,K.S.KIM,K.H.YUN,
JRNL AUTH 2 J.H.KIM,K.K.KIM
JRNL TITL STRUCTURAL AND KINETIC BASES FOR THE METAL PREFERENCE OF THE
JRNL TITL 2 M18 AMINOPEPTIDASE FROM PSEUDOMONAS AERUGINOSA
JRNL REF BIOCHEM.BIOPHYS.RES.COMMUN. V. 447 101 2014
JRNL REFN ISSN 0006-291X
JRNL PMID 24704201
JRNL DOI 10.1016/J.BBRC.2014.03.109
REMARK 2
REMARK 2 RESOLUTION. 2.44 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.6.0117
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) : 2.44
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 48.79
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.0
REMARK 3 NUMBER OF REFLECTIONS : 95594
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) : 0.150
REMARK 3 R VALUE (WORKING SET) : 0.148
REMARK 3 FREE R VALUE : 0.197
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 5026
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) : 2.44
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.51
REMARK 3 REFLECTION IN BIN (WORKING SET) : 4902
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 67.07
REMARK 3 BIN R VALUE (WORKING SET) : 0.2160
REMARK 3 BIN FREE R VALUE SET COUNT : 266
REMARK 3 BIN FREE R VALUE : 0.2780
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 18936
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 6
REMARK 3 SOLVENT ATOMS : 890
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 39.36
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -3.71000
REMARK 3 B22 (A**2) : 2.53000
REMARK 3 B33 (A**2) : 1.18000
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): 0.412
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.225
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.141
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.104
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.966
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.945
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 19320 ; 0.015 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 18372 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 26232 ; 1.743 ; 1.957
REMARK 3 BOND ANGLES OTHERS (DEGREES): 41964 ; 0.852 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 2430 ; 7.387 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 966 ;37.534 ;23.168
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 3036 ;15.860 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 198 ;18.817 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 2922 ; 0.100 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 22404 ; 0.008 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 4698 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
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): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
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): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
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
REMARK 4
REMARK 4 4OIW COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 21-JAN-14.
REMARK 100 THE DEPOSITION ID IS D_1000084549.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 24-FEB-09
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SPRING-8
REMARK 200 BEAMLINE : BL45PX
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.7321
REMARK 200 MONOCHROMATOR : 0.17 2.3 KEV
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS V
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 95594
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.440
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.1
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) : 2.55
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.64
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.1
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: CNS
REMARK 200 STARTING MODEL: 4NJR
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 51.23
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.52
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 30%(V/V) 2-PROPANOL, 0.1M HEPES 7.5,
REMARK 280 0.2M MGCL2, 10MM SPERMIDINE, 0.1MM ZNCL2, MICROBATCH
REMARK 280 CRYSTALLIZATION, TEMPERATURE 295K, PH 7.5
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 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 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 86.34650
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 86.34650
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 75.01000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 109.13350
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 75.01000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 109.13350
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 86.34650
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 75.01000
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 109.13350
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 86.34650
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 75.01000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 109.13350
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: DODECAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DODECAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 81350 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 151760 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -654.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F
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 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 86.34650
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 GLY A -1
REMARK 465 SER A 0
REMARK 465 GLY A 268
REMARK 465 SER A 269
REMARK 465 CYS A 270
REMARK 465 SER A 271
REMARK 465 HIS A 272
REMARK 465 CYS A 273
REMARK 465 GLY A 274
REMARK 465 ALA A 275
REMARK 465 ASP A 276
REMARK 465 GLY A 373
REMARK 465 CYS A 374
REMARK 465 GLY A 375
REMARK 465 SER A 376
REMARK 465 THR A 377
REMARK 465 ILE A 378
REMARK 465 GLY A 379
REMARK 465 PRO A 380
REMARK 465 ILE A 381
REMARK 465 THR A 382
REMARK 465 ALA A 383
REMARK 465 SER A 384
REMARK 465 GLY B -1
REMARK 465 SER B 0
REMARK 465 GLY B 268
REMARK 465 SER B 269
REMARK 465 CYS B 270
REMARK 465 SER B 271
REMARK 465 HIS B 272
REMARK 465 CYS B 273
REMARK 465 GLY B 274
REMARK 465 ALA B 275
REMARK 465 ASP B 276
REMARK 465 GLY B 373
REMARK 465 CYS B 374
REMARK 465 GLY B 375
REMARK 465 SER B 376
REMARK 465 THR B 377
REMARK 465 ILE B 378
REMARK 465 GLY B 379
REMARK 465 PRO B 380
REMARK 465 ILE B 381
REMARK 465 THR B 382
REMARK 465 ALA B 383
REMARK 465 SER B 384
REMARK 465 GLY C -1
REMARK 465 SER C 0
REMARK 465 GLY C 268
REMARK 465 SER C 269
REMARK 465 CYS C 270
REMARK 465 SER C 271
REMARK 465 HIS C 272
REMARK 465 CYS C 273
REMARK 465 GLY C 274
REMARK 465 ALA C 275
REMARK 465 ASP C 276
REMARK 465 GLY C 373
REMARK 465 CYS C 374
REMARK 465 GLY C 375
REMARK 465 SER C 376
REMARK 465 THR C 377
REMARK 465 ILE C 378
REMARK 465 GLY C 379
REMARK 465 PRO C 380
REMARK 465 ILE C 381
REMARK 465 THR C 382
REMARK 465 ALA C 383
REMARK 465 SER C 384
REMARK 465 GLY D -1
REMARK 465 SER D 0
REMARK 465 GLY D 268
REMARK 465 SER D 269
REMARK 465 CYS D 270
REMARK 465 SER D 271
REMARK 465 HIS D 272
REMARK 465 CYS D 273
REMARK 465 GLY D 274
REMARK 465 ALA D 275
REMARK 465 ASP D 276
REMARK 465 GLY D 373
REMARK 465 CYS D 374
REMARK 465 GLY D 375
REMARK 465 SER D 376
REMARK 465 THR D 377
REMARK 465 ILE D 378
REMARK 465 GLY D 379
REMARK 465 PRO D 380
REMARK 465 ILE D 381
REMARK 465 THR D 382
REMARK 465 ALA D 383
REMARK 465 SER D 384
REMARK 465 GLY E -1
REMARK 465 SER E 0
REMARK 465 GLY E 268
REMARK 465 SER E 269
REMARK 465 CYS E 270
REMARK 465 SER E 271
REMARK 465 HIS E 272
REMARK 465 CYS E 273
REMARK 465 GLY E 274
REMARK 465 ALA E 275
REMARK 465 ASP E 276
REMARK 465 GLY E 373
REMARK 465 CYS E 374
REMARK 465 GLY E 375
REMARK 465 SER E 376
REMARK 465 THR E 377
REMARK 465 ILE E 378
REMARK 465 GLY E 379
REMARK 465 PRO E 380
REMARK 465 ILE E 381
REMARK 465 THR E 382
REMARK 465 ALA E 383
REMARK 465 SER E 384
REMARK 465 GLY F -1
REMARK 465 SER F 0
REMARK 465 GLY F 268
REMARK 465 SER F 269
REMARK 465 CYS F 270
REMARK 465 SER F 271
REMARK 465 HIS F 272
REMARK 465 CYS F 273
REMARK 465 GLY F 274
REMARK 465 ALA F 275
REMARK 465 ASP F 276
REMARK 465 GLY F 373
REMARK 465 CYS F 374
REMARK 465 GLY F 375
REMARK 465 SER F 376
REMARK 465 THR F 377
REMARK 465 ILE F 378
REMARK 465 GLY F 379
REMARK 465 PRO F 380
REMARK 465 ILE F 381
REMARK 465 THR F 382
REMARK 465 ALA F 383
REMARK 465 SER F 384
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 621 O HOH A 641 1.90
REMARK 500 OE1 GLU A 265 O HOH A 621 1.90
REMARK 500 OE1 GLU F 265 O HOH F 610 1.97
REMARK 500 OE1 GLU E 265 O HOH E 633 1.98
REMARK 500 OE2 GLU C 265 O HOH C 625 2.03
REMARK 500 O HOH A 664 O HOH C 633 2.04
REMARK 500 O HOH F 610 O HOH F 636 2.06
REMARK 500 O HOH A 752 O HOH A 753 2.12
REMARK 500 O HOH E 633 O HOH E 634 2.12
REMARK 500 O HOH D 617 O HOH D 694 2.13
REMARK 500 O HOH A 601 O HOH A 643 2.16
REMARK 500 O GLU A 290 O HOH A 625 2.17
REMARK 500 O HOH A 660 O HOH B 768 2.18
REMARK 500 OE2 GLU C 265 O HOH C 616 2.18
REMARK 500 NH2 ARG E 36 O HOH E 690 2.19
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 GLU E 228 CD GLU E 228 OE1 0.081
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 65 NE - CZ - NH1 ANGL. DEV. = 4.2 DEGREES
REMARK 500 ARG A 65 NE - CZ - NH2 ANGL. DEV. = -3.9 DEGREES
REMARK 500 ARG A 69 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES
REMARK 500 ARG A 198 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 GLU B 4 C - N - CA ANGL. DEV. = 15.2 DEGREES
REMARK 500 GLY B 183 N - CA - C ANGL. DEV. = -15.8 DEGREES
REMARK 500 ARG B 341 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 ARG C 139 NE - CZ - NH2 ANGL. DEV. = -3.9 DEGREES
REMARK 500 ASP D 254 CB - CG - OD1 ANGL. DEV. = 6.8 DEGREES
REMARK 500 PRO D 278 C - N - CA ANGL. DEV. = 9.7 DEGREES
REMARK 500 ARG F 68 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 ARG F 68 NE - CZ - NH2 ANGL. DEV. = -3.3 DEGREES
REMARK 500 ASP F 254 CB - CG - OD1 ANGL. DEV. = 5.4 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 ASN A 57 18.19 59.96
REMARK 500 ASP A 58 28.23 43.89
REMARK 500 ARG A 144 -51.67 72.22
REMARK 500 LEU A 208 -61.98 -97.60
REMARK 500 ASP A 254 43.76 -144.05
REMARK 500 ASP A 371 30.38 -93.67
REMARK 500 HIS A 401 3.65 84.74
REMARK 500 ARG B 2 -119.54 85.88
REMARK 500 ALA B 3 -15.51 -173.78
REMARK 500 GLU B 4 82.62 92.72
REMARK 500 LEU B 5 -32.36 98.14
REMARK 500 ASP B 58 26.12 49.75
REMARK 500 SER B 59 -8.45 -140.43
REMARK 500 CYS B 87 -169.28 -164.16
REMARK 500 ARG B 144 -48.51 69.34
REMARK 500 ASN B 158 61.15 -162.71
REMARK 500 ALA B 181 158.76 -48.61
REMARK 500 LEU B 208 -64.68 -99.06
REMARK 500 ASP B 254 37.54 -146.84
REMARK 500 GLU B 266 23.81 -77.90
REMARK 500 TYR B 316 44.72 -148.12
REMARK 500 ASN B 339 35.50 -78.47
REMARK 500 HIS B 401 -1.53 87.94
REMARK 500 ASP C 58 21.94 48.98
REMARK 500 CYS C 87 -172.22 -172.60
REMARK 500 SER C 123 -163.74 -119.05
REMARK 500 ARG C 144 -47.78 64.31
REMARK 500 ASN C 158 69.70 -158.91
REMARK 500 ALA C 181 -166.92 -67.79
REMARK 500 TYR C 316 42.51 -147.58
REMARK 500 ASP C 318 -9.91 -59.36
REMARK 500 ASN C 339 34.79 -87.79
REMARK 500 ALA C 399 36.21 71.86
REMARK 500 HIS C 401 4.59 89.12
REMARK 500 ASN D 57 16.99 54.44
REMARK 500 ARG D 144 -55.52 66.34
REMARK 500 ASN D 158 67.83 -152.86
REMARK 500 ASP D 254 48.73 -143.81
REMARK 500 GLU D 290 157.30 -41.65
REMARK 500 TYR D 316 50.94 -144.62
REMARK 500 ASN D 339 38.32 -83.51
REMARK 500 THR D 344 130.15 -32.86
REMARK 500 HIS D 401 2.11 86.40
REMARK 500 GLU E 47 -90.96 -109.70
REMARK 500 THR E 48 122.50 168.05
REMARK 500 ASN E 57 12.71 56.85
REMARK 500 ASN E 93 78.83 -117.35
REMARK 500 SER E 123 -165.06 -126.69
REMARK 500 ARG E 144 -51.50 75.01
REMARK 500 ASN E 158 67.38 -155.20
REMARK 500
REMARK 500 THIS ENTRY HAS 69 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 MET A 1 ARG A 2 131.29
REMARK 500 PRO A 182 GLY A 183 -30.91
REMARK 500 PHE A 366 VAL A 367 147.52
REMARK 500 PRO D 182 GLY D 183 -47.23
REMARK 500 PRO E 182 GLY E 183 -30.00
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 ZN A 501 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 236 OD2
REMARK 620 2 GLU A 266 OE2 109.8
REMARK 620 3 HIS A 401 NE2 89.4 123.4
REMARK 620 4 HOH A 601 O 98.3 93.4 137.3
REMARK 620 5 HOH A 643 O 109.0 132.9 82.5 55.2
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B 501 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 236 OD2
REMARK 620 2 GLU B 266 OE2 101.2
REMARK 620 3 HIS B 401 NE2 94.6 115.0
REMARK 620 4 HOH B 601 O 100.1 97.3 141.0
REMARK 620 5 HOH B 635 O 139.6 109.4 95.7 51.2
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN C 501 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP C 236 OD2
REMARK 620 2 GLU C 266 OE2 107.9
REMARK 620 3 HIS C 401 NE2 85.6 122.5
REMARK 620 4 HOH C 618 O 97.1 88.1 146.9
REMARK 620 5 HOH C 653 O 130.7 116.9 87.2 66.0
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN D 501 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP D 236 OD2
REMARK 620 2 GLU D 266 OE2 101.9
REMARK 620 3 HIS D 401 NE2 86.6 107.9
REMARK 620 4 HOH D 629 O 139.6 117.9 87.5
REMARK 620 5 HOH D 631 O 90.6 123.8 127.6 62.5
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN E 501 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP E 236 OD2
REMARK 620 2 GLU E 266 OE2 92.8
REMARK 620 3 HIS E 401 NE2 90.7 105.5
REMARK 620 4 HOH E 632 O 161.3 105.4 88.6
REMARK 620 5 HOH E 635 O 96.2 108.9 144.5 74.1
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN F 501 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP F 236 OD2
REMARK 620 2 GLU F 266 OE2 100.4
REMARK 620 3 HIS F 401 NE2 87.1 99.6
REMARK 620 4 HOH F 637 O 108.6 112.0 140.7
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 ZN A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN C 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN D 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN E 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN F 501
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4OID RELATED DB: PDB
REMARK 900 D236A MUTATION FROM ASPARTYL AMINO PEPTIDASE OF PSEUDOMONAS
REMARK 900 AERUGINOSA
REMARK 900 RELATED ID: 4NJR RELATED DB: PDB
REMARK 900 ZNZNPAAP ASPARTYL AMINO PEPTIDASE OF PSEUDOMONAS AERUGINOSA WITH
REMARK 900 ZINC IN CATALYTIC SITE
REMARK 900 RELATED ID: 4NJQ RELATED DB: PDB
REMARK 900 COCOPAAP ASPARTYL AMINO PEPTIDASE OF PSEUDOMONAS AERUGINOSA WITH
REMARK 900 ZINC IN CATALYTIC SITE
DBREF 4OIW A 1 429 UNP Q9HYZ3 APEB_PSEAE 1 429
DBREF 4OIW B 1 429 UNP Q9HYZ3 APEB_PSEAE 1 429
DBREF 4OIW C 1 429 UNP Q9HYZ3 APEB_PSEAE 1 429
DBREF 4OIW D 1 429 UNP Q9HYZ3 APEB_PSEAE 1 429
DBREF 4OIW E 1 429 UNP Q9HYZ3 APEB_PSEAE 1 429
DBREF 4OIW F 1 429 UNP Q9HYZ3 APEB_PSEAE 1 429
SEQADV 4OIW GLY A -1 UNP Q9HYZ3 EXPRESSION TAG
SEQADV 4OIW SER A 0 UNP Q9HYZ3 EXPRESSION TAG
SEQADV 4OIW ALA A 82 UNP Q9HYZ3 HIS 82 ENGINEERED MUTATION
SEQADV 4OIW GLY B -1 UNP Q9HYZ3 EXPRESSION TAG
SEQADV 4OIW SER B 0 UNP Q9HYZ3 EXPRESSION TAG
SEQADV 4OIW ALA B 82 UNP Q9HYZ3 HIS 82 ENGINEERED MUTATION
SEQADV 4OIW GLY C -1 UNP Q9HYZ3 EXPRESSION TAG
SEQADV 4OIW SER C 0 UNP Q9HYZ3 EXPRESSION TAG
SEQADV 4OIW ALA C 82 UNP Q9HYZ3 HIS 82 ENGINEERED MUTATION
SEQADV 4OIW GLY D -1 UNP Q9HYZ3 EXPRESSION TAG
SEQADV 4OIW SER D 0 UNP Q9HYZ3 EXPRESSION TAG
SEQADV 4OIW ALA D 82 UNP Q9HYZ3 HIS 82 ENGINEERED MUTATION
SEQADV 4OIW GLY E -1 UNP Q9HYZ3 EXPRESSION TAG
SEQADV 4OIW SER E 0 UNP Q9HYZ3 EXPRESSION TAG
SEQADV 4OIW ALA E 82 UNP Q9HYZ3 HIS 82 ENGINEERED MUTATION
SEQADV 4OIW GLY F -1 UNP Q9HYZ3 EXPRESSION TAG
SEQADV 4OIW SER F 0 UNP Q9HYZ3 EXPRESSION TAG
SEQADV 4OIW ALA F 82 UNP Q9HYZ3 HIS 82 ENGINEERED MUTATION
SEQRES 1 A 431 GLY SER MET ARG ALA GLU LEU ASN GLN GLY LEU ILE ASP
SEQRES 2 A 431 PHE LEU LYS ALA SER PRO THR PRO PHE HIS ALA THR ALA
SEQRES 3 A 431 SER LEU ALA ARG ARG LEU GLU ALA ALA GLY TYR ARG ARG
SEQRES 4 A 431 LEU ASP GLU ARG ASP ALA TRP HIS THR GLU THR GLY GLY
SEQRES 5 A 431 ARG TYR TYR VAL THR ARG ASN ASP SER SER LEU ILE ALA
SEQRES 6 A 431 ILE ARG LEU GLY ARG ARG SER PRO LEU GLU SER GLY PHE
SEQRES 7 A 431 ARG LEU VAL GLY ALA ALA THR ASP SER PRO CYS LEU ARG
SEQRES 8 A 431 VAL LYS PRO ASN PRO GLU ILE ALA ARG ASN GLY PHE LEU
SEQRES 9 A 431 GLN LEU GLY VAL GLU VAL TYR GLY GLY ALA LEU PHE ALA
SEQRES 10 A 431 PRO TRP PHE ASP ARG ASP LEU SER LEU ALA GLY ARG VAL
SEQRES 11 A 431 THR PHE ARG ALA ASN GLY LYS LEU GLU SER ARG LEU VAL
SEQRES 12 A 431 ASP PHE ARG LYS ALA ILE ALA VAL ILE PRO ASN LEU ALA
SEQRES 13 A 431 ILE HIS LEU ASN ARG ALA ALA ASN GLU GLY TRP PRO ILE
SEQRES 14 A 431 ASN ALA GLN ASN GLU LEU PRO PRO ILE ILE ALA GLN LEU
SEQRES 15 A 431 ALA PRO GLY GLU ALA ALA ASP PHE ARG LEU LEU LEU ASP
SEQRES 16 A 431 GLU GLN LEU LEU ARG GLU HIS GLY ILE THR ALA ASP VAL
SEQRES 17 A 431 VAL LEU ASP TYR GLU LEU SER PHE TYR ASP THR GLN SER
SEQRES 18 A 431 ALA ALA VAL VAL GLY LEU ASN ASP GLU PHE ILE ALA GLY
SEQRES 19 A 431 ALA ARG LEU ASP ASN LEU LEU SER CYS HIS ALA GLY LEU
SEQRES 20 A 431 GLU ALA LEU LEU ASN ALA GLU GLY ASP GLU ASN CYS ILE
SEQRES 21 A 431 LEU VAL CYS THR ASP HIS GLU GLU VAL GLY SER CYS SER
SEQRES 22 A 431 HIS CYS GLY ALA ASP GLY PRO PHE LEU GLU GLN VAL LEU
SEQRES 23 A 431 ARG ARG LEU LEU PRO GLU GLY ASP ALA PHE SER ARG ALA
SEQRES 24 A 431 ILE GLN ARG SER LEU LEU VAL SER ALA ASP ASN ALA HIS
SEQRES 25 A 431 GLY VAL HIS PRO ASN TYR ALA ASP ARG HIS ASP ALA ASN
SEQRES 26 A 431 HIS GLY PRO ALA LEU ASN GLY GLY PRO VAL ILE LYS ILE
SEQRES 27 A 431 ASN SER ASN GLN ARG TYR ALA THR ASN SER GLU THR ALA
SEQRES 28 A 431 GLY PHE PHE ARG HIS LEU CYS GLN ASP SER GLU VAL PRO
SEQRES 29 A 431 VAL GLN SER PHE VAL THR ARG SER ASP MET GLY CYS GLY
SEQRES 30 A 431 SER THR ILE GLY PRO ILE THR ALA SER GLN VAL GLY VAL
SEQRES 31 A 431 ARG THR VAL ASP ILE GLY LEU PRO THR PHE ALA MET HIS
SEQRES 32 A 431 SER ILE ARG GLU LEU ALA GLY SER HIS ASP LEU ALA HIS
SEQRES 33 A 431 LEU VAL LYS VAL LEU GLY ALA PHE TYR ALA SER SER GLU
SEQRES 34 A 431 LEU PRO
SEQRES 1 B 431 GLY SER MET ARG ALA GLU LEU ASN GLN GLY LEU ILE ASP
SEQRES 2 B 431 PHE LEU LYS ALA SER PRO THR PRO PHE HIS ALA THR ALA
SEQRES 3 B 431 SER LEU ALA ARG ARG LEU GLU ALA ALA GLY TYR ARG ARG
SEQRES 4 B 431 LEU ASP GLU ARG ASP ALA TRP HIS THR GLU THR GLY GLY
SEQRES 5 B 431 ARG TYR TYR VAL THR ARG ASN ASP SER SER LEU ILE ALA
SEQRES 6 B 431 ILE ARG LEU GLY ARG ARG SER PRO LEU GLU SER GLY PHE
SEQRES 7 B 431 ARG LEU VAL GLY ALA ALA THR ASP SER PRO CYS LEU ARG
SEQRES 8 B 431 VAL LYS PRO ASN PRO GLU ILE ALA ARG ASN GLY PHE LEU
SEQRES 9 B 431 GLN LEU GLY VAL GLU VAL TYR GLY GLY ALA LEU PHE ALA
SEQRES 10 B 431 PRO TRP PHE ASP ARG ASP LEU SER LEU ALA GLY ARG VAL
SEQRES 11 B 431 THR PHE ARG ALA ASN GLY LYS LEU GLU SER ARG LEU VAL
SEQRES 12 B 431 ASP PHE ARG LYS ALA ILE ALA VAL ILE PRO ASN LEU ALA
SEQRES 13 B 431 ILE HIS LEU ASN ARG ALA ALA ASN GLU GLY TRP PRO ILE
SEQRES 14 B 431 ASN ALA GLN ASN GLU LEU PRO PRO ILE ILE ALA GLN LEU
SEQRES 15 B 431 ALA PRO GLY GLU ALA ALA ASP PHE ARG LEU LEU LEU ASP
SEQRES 16 B 431 GLU GLN LEU LEU ARG GLU HIS GLY ILE THR ALA ASP VAL
SEQRES 17 B 431 VAL LEU ASP TYR GLU LEU SER PHE TYR ASP THR GLN SER
SEQRES 18 B 431 ALA ALA VAL VAL GLY LEU ASN ASP GLU PHE ILE ALA GLY
SEQRES 19 B 431 ALA ARG LEU ASP ASN LEU LEU SER CYS HIS ALA GLY LEU
SEQRES 20 B 431 GLU ALA LEU LEU ASN ALA GLU GLY ASP GLU ASN CYS ILE
SEQRES 21 B 431 LEU VAL CYS THR ASP HIS GLU GLU VAL GLY SER CYS SER
SEQRES 22 B 431 HIS CYS GLY ALA ASP GLY PRO PHE LEU GLU GLN VAL LEU
SEQRES 23 B 431 ARG ARG LEU LEU PRO GLU GLY ASP ALA PHE SER ARG ALA
SEQRES 24 B 431 ILE GLN ARG SER LEU LEU VAL SER ALA ASP ASN ALA HIS
SEQRES 25 B 431 GLY VAL HIS PRO ASN TYR ALA ASP ARG HIS ASP ALA ASN
SEQRES 26 B 431 HIS GLY PRO ALA LEU ASN GLY GLY PRO VAL ILE LYS ILE
SEQRES 27 B 431 ASN SER ASN GLN ARG TYR ALA THR ASN SER GLU THR ALA
SEQRES 28 B 431 GLY PHE PHE ARG HIS LEU CYS GLN ASP SER GLU VAL PRO
SEQRES 29 B 431 VAL GLN SER PHE VAL THR ARG SER ASP MET GLY CYS GLY
SEQRES 30 B 431 SER THR ILE GLY PRO ILE THR ALA SER GLN VAL GLY VAL
SEQRES 31 B 431 ARG THR VAL ASP ILE GLY LEU PRO THR PHE ALA MET HIS
SEQRES 32 B 431 SER ILE ARG GLU LEU ALA GLY SER HIS ASP LEU ALA HIS
SEQRES 33 B 431 LEU VAL LYS VAL LEU GLY ALA PHE TYR ALA SER SER GLU
SEQRES 34 B 431 LEU PRO
SEQRES 1 C 431 GLY SER MET ARG ALA GLU LEU ASN GLN GLY LEU ILE ASP
SEQRES 2 C 431 PHE LEU LYS ALA SER PRO THR PRO PHE HIS ALA THR ALA
SEQRES 3 C 431 SER LEU ALA ARG ARG LEU GLU ALA ALA GLY TYR ARG ARG
SEQRES 4 C 431 LEU ASP GLU ARG ASP ALA TRP HIS THR GLU THR GLY GLY
SEQRES 5 C 431 ARG TYR TYR VAL THR ARG ASN ASP SER SER LEU ILE ALA
SEQRES 6 C 431 ILE ARG LEU GLY ARG ARG SER PRO LEU GLU SER GLY PHE
SEQRES 7 C 431 ARG LEU VAL GLY ALA ALA THR ASP SER PRO CYS LEU ARG
SEQRES 8 C 431 VAL LYS PRO ASN PRO GLU ILE ALA ARG ASN GLY PHE LEU
SEQRES 9 C 431 GLN LEU GLY VAL GLU VAL TYR GLY GLY ALA LEU PHE ALA
SEQRES 10 C 431 PRO TRP PHE ASP ARG ASP LEU SER LEU ALA GLY ARG VAL
SEQRES 11 C 431 THR PHE ARG ALA ASN GLY LYS LEU GLU SER ARG LEU VAL
SEQRES 12 C 431 ASP PHE ARG LYS ALA ILE ALA VAL ILE PRO ASN LEU ALA
SEQRES 13 C 431 ILE HIS LEU ASN ARG ALA ALA ASN GLU GLY TRP PRO ILE
SEQRES 14 C 431 ASN ALA GLN ASN GLU LEU PRO PRO ILE ILE ALA GLN LEU
SEQRES 15 C 431 ALA PRO GLY GLU ALA ALA ASP PHE ARG LEU LEU LEU ASP
SEQRES 16 C 431 GLU GLN LEU LEU ARG GLU HIS GLY ILE THR ALA ASP VAL
SEQRES 17 C 431 VAL LEU ASP TYR GLU LEU SER PHE TYR ASP THR GLN SER
SEQRES 18 C 431 ALA ALA VAL VAL GLY LEU ASN ASP GLU PHE ILE ALA GLY
SEQRES 19 C 431 ALA ARG LEU ASP ASN LEU LEU SER CYS HIS ALA GLY LEU
SEQRES 20 C 431 GLU ALA LEU LEU ASN ALA GLU GLY ASP GLU ASN CYS ILE
SEQRES 21 C 431 LEU VAL CYS THR ASP HIS GLU GLU VAL GLY SER CYS SER
SEQRES 22 C 431 HIS CYS GLY ALA ASP GLY PRO PHE LEU GLU GLN VAL LEU
SEQRES 23 C 431 ARG ARG LEU LEU PRO GLU GLY ASP ALA PHE SER ARG ALA
SEQRES 24 C 431 ILE GLN ARG SER LEU LEU VAL SER ALA ASP ASN ALA HIS
SEQRES 25 C 431 GLY VAL HIS PRO ASN TYR ALA ASP ARG HIS ASP ALA ASN
SEQRES 26 C 431 HIS GLY PRO ALA LEU ASN GLY GLY PRO VAL ILE LYS ILE
SEQRES 27 C 431 ASN SER ASN GLN ARG TYR ALA THR ASN SER GLU THR ALA
SEQRES 28 C 431 GLY PHE PHE ARG HIS LEU CYS GLN ASP SER GLU VAL PRO
SEQRES 29 C 431 VAL GLN SER PHE VAL THR ARG SER ASP MET GLY CYS GLY
SEQRES 30 C 431 SER THR ILE GLY PRO ILE THR ALA SER GLN VAL GLY VAL
SEQRES 31 C 431 ARG THR VAL ASP ILE GLY LEU PRO THR PHE ALA MET HIS
SEQRES 32 C 431 SER ILE ARG GLU LEU ALA GLY SER HIS ASP LEU ALA HIS
SEQRES 33 C 431 LEU VAL LYS VAL LEU GLY ALA PHE TYR ALA SER SER GLU
SEQRES 34 C 431 LEU PRO
SEQRES 1 D 431 GLY SER MET ARG ALA GLU LEU ASN GLN GLY LEU ILE ASP
SEQRES 2 D 431 PHE LEU LYS ALA SER PRO THR PRO PHE HIS ALA THR ALA
SEQRES 3 D 431 SER LEU ALA ARG ARG LEU GLU ALA ALA GLY TYR ARG ARG
SEQRES 4 D 431 LEU ASP GLU ARG ASP ALA TRP HIS THR GLU THR GLY GLY
SEQRES 5 D 431 ARG TYR TYR VAL THR ARG ASN ASP SER SER LEU ILE ALA
SEQRES 6 D 431 ILE ARG LEU GLY ARG ARG SER PRO LEU GLU SER GLY PHE
SEQRES 7 D 431 ARG LEU VAL GLY ALA ALA THR ASP SER PRO CYS LEU ARG
SEQRES 8 D 431 VAL LYS PRO ASN PRO GLU ILE ALA ARG ASN GLY PHE LEU
SEQRES 9 D 431 GLN LEU GLY VAL GLU VAL TYR GLY GLY ALA LEU PHE ALA
SEQRES 10 D 431 PRO TRP PHE ASP ARG ASP LEU SER LEU ALA GLY ARG VAL
SEQRES 11 D 431 THR PHE ARG ALA ASN GLY LYS LEU GLU SER ARG LEU VAL
SEQRES 12 D 431 ASP PHE ARG LYS ALA ILE ALA VAL ILE PRO ASN LEU ALA
SEQRES 13 D 431 ILE HIS LEU ASN ARG ALA ALA ASN GLU GLY TRP PRO ILE
SEQRES 14 D 431 ASN ALA GLN ASN GLU LEU PRO PRO ILE ILE ALA GLN LEU
SEQRES 15 D 431 ALA PRO GLY GLU ALA ALA ASP PHE ARG LEU LEU LEU ASP
SEQRES 16 D 431 GLU GLN LEU LEU ARG GLU HIS GLY ILE THR ALA ASP VAL
SEQRES 17 D 431 VAL LEU ASP TYR GLU LEU SER PHE TYR ASP THR GLN SER
SEQRES 18 D 431 ALA ALA VAL VAL GLY LEU ASN ASP GLU PHE ILE ALA GLY
SEQRES 19 D 431 ALA ARG LEU ASP ASN LEU LEU SER CYS HIS ALA GLY LEU
SEQRES 20 D 431 GLU ALA LEU LEU ASN ALA GLU GLY ASP GLU ASN CYS ILE
SEQRES 21 D 431 LEU VAL CYS THR ASP HIS GLU GLU VAL GLY SER CYS SER
SEQRES 22 D 431 HIS CYS GLY ALA ASP GLY PRO PHE LEU GLU GLN VAL LEU
SEQRES 23 D 431 ARG ARG LEU LEU PRO GLU GLY ASP ALA PHE SER ARG ALA
SEQRES 24 D 431 ILE GLN ARG SER LEU LEU VAL SER ALA ASP ASN ALA HIS
SEQRES 25 D 431 GLY VAL HIS PRO ASN TYR ALA ASP ARG HIS ASP ALA ASN
SEQRES 26 D 431 HIS GLY PRO ALA LEU ASN GLY GLY PRO VAL ILE LYS ILE
SEQRES 27 D 431 ASN SER ASN GLN ARG TYR ALA THR ASN SER GLU THR ALA
SEQRES 28 D 431 GLY PHE PHE ARG HIS LEU CYS GLN ASP SER GLU VAL PRO
SEQRES 29 D 431 VAL GLN SER PHE VAL THR ARG SER ASP MET GLY CYS GLY
SEQRES 30 D 431 SER THR ILE GLY PRO ILE THR ALA SER GLN VAL GLY VAL
SEQRES 31 D 431 ARG THR VAL ASP ILE GLY LEU PRO THR PHE ALA MET HIS
SEQRES 32 D 431 SER ILE ARG GLU LEU ALA GLY SER HIS ASP LEU ALA HIS
SEQRES 33 D 431 LEU VAL LYS VAL LEU GLY ALA PHE TYR ALA SER SER GLU
SEQRES 34 D 431 LEU PRO
SEQRES 1 E 431 GLY SER MET ARG ALA GLU LEU ASN GLN GLY LEU ILE ASP
SEQRES 2 E 431 PHE LEU LYS ALA SER PRO THR PRO PHE HIS ALA THR ALA
SEQRES 3 E 431 SER LEU ALA ARG ARG LEU GLU ALA ALA GLY TYR ARG ARG
SEQRES 4 E 431 LEU ASP GLU ARG ASP ALA TRP HIS THR GLU THR GLY GLY
SEQRES 5 E 431 ARG TYR TYR VAL THR ARG ASN ASP SER SER LEU ILE ALA
SEQRES 6 E 431 ILE ARG LEU GLY ARG ARG SER PRO LEU GLU SER GLY PHE
SEQRES 7 E 431 ARG LEU VAL GLY ALA ALA THR ASP SER PRO CYS LEU ARG
SEQRES 8 E 431 VAL LYS PRO ASN PRO GLU ILE ALA ARG ASN GLY PHE LEU
SEQRES 9 E 431 GLN LEU GLY VAL GLU VAL TYR GLY GLY ALA LEU PHE ALA
SEQRES 10 E 431 PRO TRP PHE ASP ARG ASP LEU SER LEU ALA GLY ARG VAL
SEQRES 11 E 431 THR PHE ARG ALA ASN GLY LYS LEU GLU SER ARG LEU VAL
SEQRES 12 E 431 ASP PHE ARG LYS ALA ILE ALA VAL ILE PRO ASN LEU ALA
SEQRES 13 E 431 ILE HIS LEU ASN ARG ALA ALA ASN GLU GLY TRP PRO ILE
SEQRES 14 E 431 ASN ALA GLN ASN GLU LEU PRO PRO ILE ILE ALA GLN LEU
SEQRES 15 E 431 ALA PRO GLY GLU ALA ALA ASP PHE ARG LEU LEU LEU ASP
SEQRES 16 E 431 GLU GLN LEU LEU ARG GLU HIS GLY ILE THR ALA ASP VAL
SEQRES 17 E 431 VAL LEU ASP TYR GLU LEU SER PHE TYR ASP THR GLN SER
SEQRES 18 E 431 ALA ALA VAL VAL GLY LEU ASN ASP GLU PHE ILE ALA GLY
SEQRES 19 E 431 ALA ARG LEU ASP ASN LEU LEU SER CYS HIS ALA GLY LEU
SEQRES 20 E 431 GLU ALA LEU LEU ASN ALA GLU GLY ASP GLU ASN CYS ILE
SEQRES 21 E 431 LEU VAL CYS THR ASP HIS GLU GLU VAL GLY SER CYS SER
SEQRES 22 E 431 HIS CYS GLY ALA ASP GLY PRO PHE LEU GLU GLN VAL LEU
SEQRES 23 E 431 ARG ARG LEU LEU PRO GLU GLY ASP ALA PHE SER ARG ALA
SEQRES 24 E 431 ILE GLN ARG SER LEU LEU VAL SER ALA ASP ASN ALA HIS
SEQRES 25 E 431 GLY VAL HIS PRO ASN TYR ALA ASP ARG HIS ASP ALA ASN
SEQRES 26 E 431 HIS GLY PRO ALA LEU ASN GLY GLY PRO VAL ILE LYS ILE
SEQRES 27 E 431 ASN SER ASN GLN ARG TYR ALA THR ASN SER GLU THR ALA
SEQRES 28 E 431 GLY PHE PHE ARG HIS LEU CYS GLN ASP SER GLU VAL PRO
SEQRES 29 E 431 VAL GLN SER PHE VAL THR ARG SER ASP MET GLY CYS GLY
SEQRES 30 E 431 SER THR ILE GLY PRO ILE THR ALA SER GLN VAL GLY VAL
SEQRES 31 E 431 ARG THR VAL ASP ILE GLY LEU PRO THR PHE ALA MET HIS
SEQRES 32 E 431 SER ILE ARG GLU LEU ALA GLY SER HIS ASP LEU ALA HIS
SEQRES 33 E 431 LEU VAL LYS VAL LEU GLY ALA PHE TYR ALA SER SER GLU
SEQRES 34 E 431 LEU PRO
SEQRES 1 F 431 GLY SER MET ARG ALA GLU LEU ASN GLN GLY LEU ILE ASP
SEQRES 2 F 431 PHE LEU LYS ALA SER PRO THR PRO PHE HIS ALA THR ALA
SEQRES 3 F 431 SER LEU ALA ARG ARG LEU GLU ALA ALA GLY TYR ARG ARG
SEQRES 4 F 431 LEU ASP GLU ARG ASP ALA TRP HIS THR GLU THR GLY GLY
SEQRES 5 F 431 ARG TYR TYR VAL THR ARG ASN ASP SER SER LEU ILE ALA
SEQRES 6 F 431 ILE ARG LEU GLY ARG ARG SER PRO LEU GLU SER GLY PHE
SEQRES 7 F 431 ARG LEU VAL GLY ALA ALA THR ASP SER PRO CYS LEU ARG
SEQRES 8 F 431 VAL LYS PRO ASN PRO GLU ILE ALA ARG ASN GLY PHE LEU
SEQRES 9 F 431 GLN LEU GLY VAL GLU VAL TYR GLY GLY ALA LEU PHE ALA
SEQRES 10 F 431 PRO TRP PHE ASP ARG ASP LEU SER LEU ALA GLY ARG VAL
SEQRES 11 F 431 THR PHE ARG ALA ASN GLY LYS LEU GLU SER ARG LEU VAL
SEQRES 12 F 431 ASP PHE ARG LYS ALA ILE ALA VAL ILE PRO ASN LEU ALA
SEQRES 13 F 431 ILE HIS LEU ASN ARG ALA ALA ASN GLU GLY TRP PRO ILE
SEQRES 14 F 431 ASN ALA GLN ASN GLU LEU PRO PRO ILE ILE ALA GLN LEU
SEQRES 15 F 431 ALA PRO GLY GLU ALA ALA ASP PHE ARG LEU LEU LEU ASP
SEQRES 16 F 431 GLU GLN LEU LEU ARG GLU HIS GLY ILE THR ALA ASP VAL
SEQRES 17 F 431 VAL LEU ASP TYR GLU LEU SER PHE TYR ASP THR GLN SER
SEQRES 18 F 431 ALA ALA VAL VAL GLY LEU ASN ASP GLU PHE ILE ALA GLY
SEQRES 19 F 431 ALA ARG LEU ASP ASN LEU LEU SER CYS HIS ALA GLY LEU
SEQRES 20 F 431 GLU ALA LEU LEU ASN ALA GLU GLY ASP GLU ASN CYS ILE
SEQRES 21 F 431 LEU VAL CYS THR ASP HIS GLU GLU VAL GLY SER CYS SER
SEQRES 22 F 431 HIS CYS GLY ALA ASP GLY PRO PHE LEU GLU GLN VAL LEU
SEQRES 23 F 431 ARG ARG LEU LEU PRO GLU GLY ASP ALA PHE SER ARG ALA
SEQRES 24 F 431 ILE GLN ARG SER LEU LEU VAL SER ALA ASP ASN ALA HIS
SEQRES 25 F 431 GLY VAL HIS PRO ASN TYR ALA ASP ARG HIS ASP ALA ASN
SEQRES 26 F 431 HIS GLY PRO ALA LEU ASN GLY GLY PRO VAL ILE LYS ILE
SEQRES 27 F 431 ASN SER ASN GLN ARG TYR ALA THR ASN SER GLU THR ALA
SEQRES 28 F 431 GLY PHE PHE ARG HIS LEU CYS GLN ASP SER GLU VAL PRO
SEQRES 29 F 431 VAL GLN SER PHE VAL THR ARG SER ASP MET GLY CYS GLY
SEQRES 30 F 431 SER THR ILE GLY PRO ILE THR ALA SER GLN VAL GLY VAL
SEQRES 31 F 431 ARG THR VAL ASP ILE GLY LEU PRO THR PHE ALA MET HIS
SEQRES 32 F 431 SER ILE ARG GLU LEU ALA GLY SER HIS ASP LEU ALA HIS
SEQRES 33 F 431 LEU VAL LYS VAL LEU GLY ALA PHE TYR ALA SER SER GLU
SEQRES 34 F 431 LEU PRO
HET ZN A 501 1
HET ZN B 501 1
HET ZN C 501 1
HET ZN D 501 1
HET ZN E 501 1
HET ZN F 501 1
HETNAM ZN ZINC ION
FORMUL 7 ZN 6(ZN 2+)
FORMUL 13 HOH *890(H2 O)
HELIX 1 1 ARG A 2 ALA A 15 1 14
HELIX 2 2 THR A 18 ALA A 33 1 16
HELIX 3 3 SER A 70 GLY A 75 1 6
HELIX 4 4 PHE A 114 PHE A 118 5 5
HELIX 5 5 ALA A 154 ASN A 158 5 5
HELIX 6 6 ALA A 160 GLY A 164 5 5
HELIX 7 7 ASN A 168 LEU A 173 1 6
HELIX 8 8 ASP A 187 GLY A 201 1 15
HELIX 9 9 ARG A 234 ALA A 251 1 18
HELIX 10 10 PRO A 278 LEU A 287 1 10
HELIX 11 11 ASP A 292 GLN A 299 1 8
HELIX 12 12 TYR A 316 HIS A 320 5 5
HELIX 13 13 ASN A 345 SER A 359 1 15
HELIX 14 14 HIS A 410 ALA A 424 1 15
HELIX 15 15 ASN B 6 ALA B 15 1 10
HELIX 16 16 THR B 18 ALA B 33 1 16
HELIX 17 17 SER B 70 GLY B 75 1 6
HELIX 18 18 PHE B 114 PHE B 118 5 5
HELIX 19 19 ALA B 154 ASN B 158 5 5
HELIX 20 20 ALA B 160 GLY B 164 5 5
HELIX 21 21 ASN B 168 LEU B 173 1 6
HELIX 22 22 ASP B 187 GLY B 201 1 15
HELIX 23 23 ARG B 234 ALA B 251 1 18
HELIX 24 24 PRO B 278 LEU B 287 1 10
HELIX 25 25 ASP B 292 ARG B 300 1 9
HELIX 26 26 TYR B 316 HIS B 320 5 5
HELIX 27 27 ASN B 345 SER B 359 1 15
HELIX 28 28 HIS B 410 ALA B 424 1 15
HELIX 29 29 ARG C 2 ALA C 15 1 14
HELIX 30 30 THR C 18 ALA C 33 1 16
HELIX 31 31 SER C 70 GLY C 75 1 6
HELIX 32 32 PHE C 114 PHE C 118 5 5
HELIX 33 33 ALA C 154 ASN C 158 5 5
HELIX 34 34 ALA C 160 GLY C 164 5 5
HELIX 35 35 ASN C 168 LEU C 173 1 6
HELIX 36 36 ASP C 187 GLY C 201 1 15
HELIX 37 37 ARG C 234 ALA C 251 1 18
HELIX 38 38 PRO C 278 LEU C 287 1 10
HELIX 39 39 ASP C 292 ARG C 300 1 9
HELIX 40 40 TYR C 316 HIS C 320 5 5
HELIX 41 41 ASN C 345 SER C 359 1 15
HELIX 42 42 HIS C 410 ALA C 424 1 15
HELIX 43 43 ARG D 2 SER D 16 1 15
HELIX 44 44 THR D 18 ALA D 33 1 16
HELIX 45 45 SER D 70 GLY D 75 1 6
HELIX 46 46 PHE D 114 PHE D 118 5 5
HELIX 47 47 ALA D 154 ASN D 158 5 5
HELIX 48 48 ALA D 160 GLY D 164 5 5
HELIX 49 49 ASN D 168 LEU D 173 1 6
HELIX 50 50 ASP D 187 GLY D 201 1 15
HELIX 51 51 ARG D 234 ALA D 251 1 18
HELIX 52 52 PRO D 278 ARG D 286 1 9
HELIX 53 53 ASP D 292 ARG D 300 1 9
HELIX 54 54 TYR D 316 HIS D 320 5 5
HELIX 55 55 ASN D 345 SER D 359 1 15
HELIX 56 56 HIS D 410 ALA D 424 1 15
HELIX 57 57 ARG E 2 SER E 16 1 15
HELIX 58 58 THR E 18 ALA E 33 1 16
HELIX 59 59 SER E 70 GLY E 75 1 6
HELIX 60 60 PHE E 114 PHE E 118 5 5
HELIX 61 61 ALA E 154 ASN E 158 5 5
HELIX 62 62 ALA E 160 GLY E 164 5 5
HELIX 63 63 ASN E 168 LEU E 173 1 6
HELIX 64 64 ASP E 187 GLY E 201 1 15
HELIX 65 65 ARG E 234 ALA E 251 1 18
HELIX 66 66 PRO E 278 ARG E 286 1 9
HELIX 67 67 ASP E 292 GLN E 299 1 8
HELIX 68 68 TYR E 316 HIS E 320 5 5
HELIX 69 69 ASN E 345 GLU E 360 1 16
HELIX 70 70 HIS E 410 ALA E 424 1 15
HELIX 71 71 ARG F 2 SER F 16 1 15
HELIX 72 72 THR F 18 ALA F 33 1 16
HELIX 73 73 SER F 70 GLY F 75 1 6
HELIX 74 74 PHE F 114 PHE F 118 5 5
HELIX 75 75 ALA F 154 ASN F 158 5 5
HELIX 76 76 ALA F 160 GLY F 164 5 5
HELIX 77 77 ASN F 168 LEU F 173 1 6
HELIX 78 78 ASP F 187 GLY F 201 1 15
HELIX 79 79 ARG F 234 ALA F 251 1 18
HELIX 80 80 PRO F 278 ARG F 286 1 9
HELIX 81 81 ASP F 292 GLN F 299 1 8
HELIX 82 82 TYR F 316 HIS F 320 5 5
HELIX 83 83 ASN F 345 SER F 359 1 15
HELIX 84 84 HIS F 410 ALA F 424 1 15
SHEET 1 A 9 ARG A 36 ARG A 37 0
SHEET 2 A 9 ARG A 51 ARG A 56 1 O ARG A 51 N ARG A 36
SHEET 3 A 9 SER A 60 ARG A 65 -1 O ILE A 64 N TYR A 52
SHEET 4 A 9 ASN A 256 THR A 262 -1 O CYS A 261 N LEU A 61
SHEET 5 A 9 PHE A 76 ALA A 82 1 N VAL A 79 O VAL A 260
SHEET 6 A 9 LEU A 302 ALA A 306 1 O VAL A 304 N LEU A 78
SHEET 7 A 9 THR A 390 GLY A 394 1 O ILE A 393 N SER A 305
SHEET 8 A 9 VAL A 333 LYS A 335 -1 N LYS A 335 O ASP A 392
SHEET 9 A 9 GLN A 364 PHE A 366 1 O GLN A 364 N ILE A 334
SHEET 1 B 3 CYS A 87 ARG A 98 0
SHEET 2 B 3 PHE A 101 TYR A 109 -1 O TYR A 109 N CYS A 87
SHEET 3 B 3 ILE A 176 GLN A 179 -1 O ALA A 178 N LEU A 102
SHEET 1 C 3 LYS A 135 ASP A 142 0
SHEET 2 C 3 LEU A 122 ALA A 132 -1 N PHE A 130 O GLU A 137
SHEET 3 C 3 VAL A 206 ASP A 216 -1 O ASP A 209 N THR A 129
SHEET 1 D 5 ALA A 221 VAL A 223 0
SHEET 2 D 5 PHE A 229 GLY A 232 -1 O ALA A 231 N ALA A 221
SHEET 3 D 5 GLU A 405 GLY A 408 -1 O GLU A 405 N GLY A 232
SHEET 4 D 5 PRO A 396 PHE A 398 -1 N PHE A 398 O LEU A 406
SHEET 5 D 5 ALA A 309 HIS A 310 1 N ALA A 309 O THR A 397
SHEET 1 E 9 ARG B 36 ARG B 37 0
SHEET 2 E 9 ARG B 51 ARG B 56 1 O ARG B 51 N ARG B 36
SHEET 3 E 9 SER B 60 ARG B 65 -1 O ILE B 64 N TYR B 52
SHEET 4 E 9 CYS B 257 THR B 262 -1 O CYS B 261 N LEU B 61
SHEET 5 E 9 ARG B 77 ALA B 82 1 N ARG B 77 O ILE B 258
SHEET 6 E 9 LEU B 302 ALA B 306 1 O VAL B 304 N LEU B 78
SHEET 7 E 9 ARG B 389 GLY B 394 1 O ARG B 389 N LEU B 303
SHEET 8 E 9 VAL B 333 LYS B 335 -1 N VAL B 333 O GLY B 394
SHEET 9 E 9 GLN B 364 PHE B 366 1 O GLN B 364 N ILE B 334
SHEET 1 F 3 CYS B 87 ARG B 98 0
SHEET 2 F 3 PHE B 101 TYR B 109 -1 O GLN B 103 N ILE B 96
SHEET 3 F 3 ILE B 176 GLN B 179 -1 O ILE B 177 N LEU B 102
SHEET 1 G 3 LYS B 135 ASP B 142 0
SHEET 2 G 3 LEU B 122 ALA B 132 -1 N PHE B 130 O GLU B 137
SHEET 3 G 3 VAL B 206 ASP B 216 -1 O SER B 213 N ALA B 125
SHEET 1 H 5 ALA B 221 VAL B 223 0
SHEET 2 H 5 PHE B 229 GLY B 232 -1 O ALA B 231 N ALA B 221
SHEET 3 H 5 GLU B 405 GLY B 408 -1 O ALA B 407 N ILE B 230
SHEET 4 H 5 PRO B 396 PHE B 398 -1 N PHE B 398 O LEU B 406
SHEET 5 H 5 ALA B 309 HIS B 310 1 N ALA B 309 O THR B 397
SHEET 1 I 9 ARG C 36 ARG C 37 0
SHEET 2 I 9 ARG C 51 ARG C 56 1 O ARG C 51 N ARG C 36
SHEET 3 I 9 SER C 60 ARG C 65 -1 O ILE C 64 N TYR C 52
SHEET 4 I 9 CYS C 257 THR C 262 -1 O CYS C 261 N LEU C 61
SHEET 5 I 9 ARG C 77 ALA C 82 1 N VAL C 79 O VAL C 260
SHEET 6 I 9 LEU C 302 ALA C 306 1 O VAL C 304 N LEU C 78
SHEET 7 I 9 ARG C 389 GLY C 394 1 O ARG C 389 N LEU C 303
SHEET 8 I 9 VAL C 333 LYS C 335 -1 N LYS C 335 O ASP C 392
SHEET 9 I 9 GLN C 364 PHE C 366 1 O GLN C 364 N ILE C 334
SHEET 1 J 3 CYS C 87 ARG C 98 0
SHEET 2 J 3 PHE C 101 TYR C 109 -1 O TYR C 109 N CYS C 87
SHEET 3 J 3 ILE C 176 GLN C 179 -1 O ILE C 177 N LEU C 102
SHEET 1 K 3 LYS C 135 ASP C 142 0
SHEET 2 K 3 LEU C 122 ALA C 132 -1 N VAL C 128 O ARG C 139
SHEET 3 K 3 VAL C 206 ASP C 216 -1 O ASP C 209 N THR C 129
SHEET 1 L 5 ALA C 221 VAL C 223 0
SHEET 2 L 5 PHE C 229 GLY C 232 -1 O PHE C 229 N VAL C 223
SHEET 3 L 5 GLU C 405 GLY C 408 -1 O ALA C 407 N ILE C 230
SHEET 4 L 5 PRO C 396 PHE C 398 -1 N PHE C 398 O LEU C 406
SHEET 5 L 5 ALA C 309 HIS C 310 1 N ALA C 309 O THR C 397
SHEET 1 M 9 ARG D 36 ARG D 37 0
SHEET 2 M 9 ARG D 51 ARG D 56 1 O ARG D 51 N ARG D 36
SHEET 3 M 9 SER D 60 ARG D 65 -1 O ILE D 64 N TYR D 52
SHEET 4 M 9 CYS D 257 THR D 262 -1 O CYS D 261 N LEU D 61
SHEET 5 M 9 ARG D 77 ALA D 82 1 N ARG D 77 O ILE D 258
SHEET 6 M 9 LEU D 302 ALA D 306 1 O ALA D 306 N GLY D 80
SHEET 7 M 9 THR D 390 GLY D 394 1 O ILE D 393 N SER D 305
SHEET 8 M 9 VAL D 333 LYS D 335 -1 N LYS D 335 O ASP D 392
SHEET 9 M 9 GLN D 364 PHE D 366 1 O GLN D 364 N ILE D 334
SHEET 1 N 6 LYS D 135 ASP D 142 0
SHEET 2 N 6 LEU D 122 ALA D 132 -1 N PHE D 130 O GLU D 137
SHEET 3 N 6 VAL D 206 ASP D 216 -1 O ASP D 209 N THR D 129
SHEET 4 N 6 CYS D 87 ARG D 98 -1 N LEU D 88 O PHE D 214
SHEET 5 N 6 PHE D 101 TYR D 109 -1 O TYR D 109 N CYS D 87
SHEET 6 N 6 ILE D 176 GLN D 179 -1 O ILE D 177 N LEU D 102
SHEET 1 O 5 ALA D 221 VAL D 223 0
SHEET 2 O 5 PHE D 229 GLY D 232 -1 O ALA D 231 N ALA D 221
SHEET 3 O 5 GLU D 405 GLY D 408 -1 O ALA D 407 N ILE D 230
SHEET 4 O 5 PRO D 396 PHE D 398 -1 N PHE D 398 O LEU D 406
SHEET 5 O 5 ALA D 309 HIS D 310 1 N ALA D 309 O THR D 397
SHEET 1 P 9 ARG E 36 ARG E 37 0
SHEET 2 P 9 ARG E 51 ARG E 56 1 O ARG E 51 N ARG E 36
SHEET 3 P 9 SER E 60 ARG E 65 -1 O ILE E 64 N TYR E 52
SHEET 4 P 9 CYS E 257 THR E 262 -1 O CYS E 261 N LEU E 61
SHEET 5 P 9 ARG E 77 ALA E 82 1 N ARG E 77 O ILE E 258
SHEET 6 P 9 LEU E 302 ALA E 306 1 O ALA E 306 N GLY E 80
SHEET 7 P 9 THR E 390 GLY E 394 1 O ILE E 393 N SER E 305
SHEET 8 P 9 VAL E 333 LYS E 335 -1 N VAL E 333 O GLY E 394
SHEET 9 P 9 GLN E 364 PHE E 366 1 O GLN E 364 N ILE E 334
SHEET 1 Q 3 CYS E 87 ARG E 98 0
SHEET 2 Q 3 PHE E 101 TYR E 109 -1 O TYR E 109 N CYS E 87
SHEET 3 Q 3 ILE E 176 GLN E 179 -1 O ALA E 178 N LEU E 102
SHEET 1 R 3 LYS E 135 ASP E 142 0
SHEET 2 R 3 LEU E 122 ALA E 132 -1 N PHE E 130 O GLU E 137
SHEET 3 R 3 VAL E 206 ASP E 216 -1 O SER E 213 N ALA E 125
SHEET 1 S 5 ALA E 221 VAL E 223 0
SHEET 2 S 5 PHE E 229 GLY E 232 -1 O ALA E 231 N ALA E 221
SHEET 3 S 5 GLU E 405 GLY E 408 -1 O ALA E 407 N ILE E 230
SHEET 4 S 5 PRO E 396 PHE E 398 -1 N PHE E 398 O LEU E 406
SHEET 5 S 5 ALA E 309 HIS E 310 1 N ALA E 309 O THR E 397
SHEET 1 T 9 ARG F 36 ARG F 37 0
SHEET 2 T 9 ARG F 51 ARG F 56 1 O ARG F 51 N ARG F 36
SHEET 3 T 9 SER F 60 ARG F 65 -1 O ILE F 62 N VAL F 54
SHEET 4 T 9 CYS F 257 THR F 262 -1 O CYS F 257 N ARG F 65
SHEET 5 T 9 ARG F 77 ALA F 82 1 N VAL F 79 O VAL F 260
SHEET 6 T 9 LEU F 302 ALA F 306 1 O VAL F 304 N LEU F 78
SHEET 7 T 9 THR F 390 GLY F 394 1 O VAL F 391 N SER F 305
SHEET 8 T 9 VAL F 333 LYS F 335 -1 N LYS F 335 O ASP F 392
SHEET 9 T 9 GLN F 364 PHE F 366 1 O GLN F 364 N ILE F 334
SHEET 1 U 3 CYS F 87 ARG F 98 0
SHEET 2 U 3 PHE F 101 TYR F 109 -1 O TYR F 109 N CYS F 87
SHEET 3 U 3 ILE F 176 GLN F 179 -1 O ILE F 177 N LEU F 102
SHEET 1 V 3 LYS F 135 ASP F 142 0
SHEET 2 V 3 LEU F 122 ALA F 132 -1 N PHE F 130 O GLU F 137
SHEET 3 V 3 VAL F 206 ASP F 216 -1 O ASP F 209 N THR F 129
SHEET 1 W 5 ALA F 221 VAL F 223 0
SHEET 2 W 5 PHE F 229 GLY F 232 -1 O ALA F 231 N ALA F 221
SHEET 3 W 5 GLU F 405 GLY F 408 -1 O ALA F 407 N ILE F 230
SHEET 4 W 5 PRO F 396 PHE F 398 -1 N PHE F 398 O LEU F 406
SHEET 5 W 5 ALA F 309 HIS F 310 1 N ALA F 309 O THR F 397
LINK OD2 ASP A 236 ZN ZN A 501 1555 1555 1.96
LINK OE2 GLU A 266 ZN ZN A 501 1555 1555 1.93
LINK NE2 HIS A 401 ZN ZN A 501 1555 1555 2.28
LINK ZN ZN A 501 O HOH A 601 1555 1555 2.48
LINK ZN ZN A 501 O HOH A 643 1555 1555 2.14
LINK OD2 ASP B 236 ZN ZN B 501 1555 1555 2.05
LINK OE2 GLU B 266 ZN ZN B 501 1555 1555 2.08
LINK NE2 HIS B 401 ZN ZN B 501 1555 1555 2.10
LINK ZN ZN B 501 O HOH B 601 1555 1555 2.69
LINK ZN ZN B 501 O HOH B 635 1555 1555 2.44
LINK OD2 ASP C 236 ZN ZN C 501 1555 1555 2.13
LINK OE2 GLU C 266 ZN ZN C 501 1555 1555 1.97
LINK NE2 HIS C 401 ZN ZN C 501 1555 1555 2.23
LINK ZN ZN C 501 O HOH C 618 1555 1555 2.43
LINK ZN ZN C 501 O HOH C 653 1555 1555 2.28
LINK OD2 ASP D 236 ZN ZN D 501 1555 1555 2.13
LINK OE2 GLU D 266 ZN ZN D 501 1555 1555 2.00
LINK NE2 HIS D 401 ZN ZN D 501 1555 1555 2.36
LINK ZN ZN D 501 O HOH D 629 1555 1555 2.29
LINK ZN ZN D 501 O HOH D 631 1555 1555 2.42
LINK OD2 ASP E 236 ZN ZN E 501 1555 1555 2.03
LINK OE2 GLU E 266 ZN ZN E 501 1555 1555 2.03
LINK NE2 HIS E 401 ZN ZN E 501 1555 1555 2.30
LINK ZN ZN E 501 O HOH E 632 1555 1555 2.59
LINK ZN ZN E 501 O HOH E 635 1555 1555 2.43
LINK OD2 ASP F 236 ZN ZN F 501 1555 1555 2.10
LINK OE2 GLU F 266 ZN ZN F 501 1555 1555 1.78
LINK NE2 HIS F 401 ZN ZN F 501 1555 1555 2.34
LINK ZN ZN F 501 O HOH F 637 1555 1555 2.39
CISPEP 1 ASP A 236 ASN A 237 0 -0.64
CISPEP 2 ARG B 2 ALA B 3 0 -0.52
CISPEP 3 ALA B 3 GLU B 4 0 3.72
CISPEP 4 GLU B 4 LEU B 5 0 -26.03
CISPEP 5 PRO B 182 GLY B 183 0 -30.00
CISPEP 6 ASP B 236 ASN B 237 0 1.21
CISPEP 7 PRO C 182 GLY C 183 0 -1.68
CISPEP 8 ASP C 236 ASN C 237 0 -2.13
CISPEP 9 GLY C 277 PRO C 278 0 -7.49
CISPEP 10 ASP D 236 ASN D 237 0 6.65
CISPEP 11 ASP E 236 ASN E 237 0 2.55
CISPEP 12 PRO F 182 GLY F 183 0 2.86
CISPEP 13 ASP F 236 ASN F 237 0 -0.39
SITE 1 AC1 5 ASP A 236 GLU A 266 HIS A 401 HOH A 601
SITE 2 AC1 5 HOH A 643
SITE 1 AC2 5 ASP B 236 GLU B 266 HIS B 401 HOH B 601
SITE 2 AC2 5 HOH B 635
SITE 1 AC3 5 ASP C 236 GLU C 266 HIS C 401 HOH C 618
SITE 2 AC3 5 HOH C 653
SITE 1 AC4 5 ASP D 236 GLU D 266 HIS D 401 HOH D 629
SITE 2 AC4 5 HOH D 631
SITE 1 AC5 5 ASP E 236 GLU E 266 HIS E 401 HOH E 632
SITE 2 AC5 5 HOH E 635
SITE 1 AC6 4 ASP F 236 GLU F 266 HIS F 401 HOH F 637
CRYST1 150.020 218.267 172.693 90.00 90.00 90.00 C 2 2 21 48
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 0.006666 0.000000 0.000000 0.00000
SCALE2 0.000000 0.004582 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005791 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
