HEADER OXIDOREDUCTASE 27-MAY-10 3N81
TITLE T244A MUTANT OF HUMAN MITOCHONDRIAL ALDEHYDE DEHYDROGENASE, APO FORM
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ALDEHYDE DEHYDROGENASE, MITOCHONDRIAL;
COMPND 3 CHAIN: A, B, C, D, E, F, G, H;
COMPND 4 FRAGMENT: MATURE SEQUENCE, RESIDUES 18-517;
COMPND 5 EC: 1.2.1.3;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: ALDH2, ALDM;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PT-7-7
KEYWDS OXIDOREDUCTASE, ALDH, ROSSMANN FOLD
EXPDTA X-RAY DIFFRACTION
AUTHOR L.GONZALEZ-SEGURA,T.D.HURLEY
REVDAT 5 06-SEP-23 3N81 1 REMARK SEQADV LINK
REVDAT 4 31-JAN-18 3N81 1 JRNL
REVDAT 3 08-NOV-17 3N81 1 REMARK
REVDAT 2 22-JUL-15 3N81 1 SOURCE VERSN
REVDAT 1 13-APR-11 3N81 0
JRNL AUTH K.-K.HO,L.GONZALEZ-SEGURA,S.PEREZ-MILLER,H.WEINER,T.D.HURLEY
JRNL TITL CONFORMATIONAL SELECTION DURING CATALYSIS: THE ROLE OF
JRNL TITL 2 THREONINE 244 IN ALDH2
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH K.-K.HO,T.D.HURLEY,H.WEINER
REMARK 1 TITL SELECTIVE ALTERATION OF THE RATE-LIMITING STEP IN CYTOSOLIC
REMARK 1 TITL 2 ALDEHYDE DEHYDROGENASE THROUGH RANDOM MUTAGENESIS
REMARK 1 REF BIOCHEMISTRY V. 45 9445 2006
REMARK 1 REFN ISSN 0006-2960
REMARK 1 REFERENCE 2
REMARK 1 AUTH H.N.LARSON,J.ZHOU,Z.CHEN,J.S.STAMLER,H.WEINER,T.D.HURLEY
REMARK 1 TITL STRUCTURAL AND FUNCTIONAL CONSEQUENCES OF COENZYME BINDING
REMARK 1 TITL 2 TO THE INACTIVE ASIAN VARIANT OF MITOCHONDRIAL ALDEHYDE
REMARK 1 TITL 3 DEHYDROGENASE (ROLES OF RESIDUES 475 AND 487)
REMARK 1 REF J. BIOL. CHEM. V. 282 12940 2007
REMARK 1 REFN ISSN 0021-9258
REMARK 2
REMARK 2 RESOLUTION. 1.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.3.0037
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) : 1.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 42.07
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.6
REMARK 3 NUMBER OF REFLECTIONS : 411531
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) : 0.182
REMARK 3 R VALUE (WORKING SET) : 0.181
REMARK 3 FREE R VALUE : 0.217
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 20606
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) : 1.70
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.74
REMARK 3 REFLECTION IN BIN (WORKING SET) : 28619
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.30
REMARK 3 BIN R VALUE (WORKING SET) : 0.2340
REMARK 3 BIN FREE R VALUE SET COUNT : 1499
REMARK 3 BIN FREE R VALUE : 0.2830
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 30363
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 200
REMARK 3 SOLVENT ATOMS : 3398
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 26.10
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 18.14
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.90000
REMARK 3 B22 (A**2) : -0.50000
REMARK 3 B33 (A**2) : -1.40000
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): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.112
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.076
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.288
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.962
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.946
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 31946 ; 0.012 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 43406 ; 1.266 ; 1.954
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 4145 ; 5.917 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 1453 ;35.194 ;24.652
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 5248 ;12.447 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 170 ;16.651 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 4736 ; 0.087 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 24731 ; 0.005 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 16539 ; 0.196 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 22212 ; 0.308 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 3113 ; 0.123 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): 25 ; 0.114 ; 0.200
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 82 ; 0.175 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 66 ; 0.145 ; 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): 20047 ; 0.614 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 32227 ; 1.068 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 12314 ; 2.019 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 11106 ; 3.215 ; 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: NULL
REMARK 4
REMARK 4 3N81 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 04-JUN-10.
REMARK 100 THE DEPOSITION ID IS D_1000059496.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 12-JUL-07
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.4
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 19-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.98
REMARK 200 MONOCHROMATOR : SAGITALLY FOCUSED SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO, HKL-3000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK, HKL-3000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 416273
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.700
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 200 DATA REDUNDANCY : 5.700
REMARK 200 R MERGE (I) : 0.09200
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 16.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.76
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.4
REMARK 200 DATA REDUNDANCY IN SHELL : 4.00
REMARK 200 R MERGE FOR SHELL (I) : 0.50300
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.400
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: DIRECT REFINEMENT
REMARK 200 SOFTWARE USED: REFMAC
REMARK 200 STARTING MODEL: PDB ENTRY 1O05
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 43.95
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.19
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM ACES (N-[2-ACETAMIDO]-2
REMARK 280 -AMINOETHANE SULFONIC ACID), 1-10MM MGCL2, 100-200 MM GUANIDINE
REMARK 280 HCL, 16-17% W/V PEG 6000, PH 6.4, VAPOR DIFFUSION, TEMPERATURE
REMARK 280 292K
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 70.87500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 88.64600
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 76.09700
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 88.64600
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 70.87500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 76.09700
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 26440 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 58090 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -77.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D
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
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 26200 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 58320 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -79.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F, G, H
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 SER A 1
REMARK 465 ALA A 2
REMARK 465 ALA A 3
REMARK 465 ALA A 4
REMARK 465 THR A 5
REMARK 465 GLN A 6
REMARK 465 SER B 1
REMARK 465 ALA B 2
REMARK 465 ALA B 3
REMARK 465 ALA B 4
REMARK 465 THR B 5
REMARK 465 GLN B 6
REMARK 465 SER C 1
REMARK 465 ALA C 2
REMARK 465 ALA C 3
REMARK 465 ALA C 4
REMARK 465 THR C 5
REMARK 465 GLN C 6
REMARK 465 SER D 1
REMARK 465 ALA D 2
REMARK 465 ALA D 3
REMARK 465 ALA D 4
REMARK 465 THR D 5
REMARK 465 GLN D 6
REMARK 465 SER E 1
REMARK 465 ALA E 2
REMARK 465 ALA E 3
REMARK 465 ALA E 4
REMARK 465 THR E 5
REMARK 465 GLN E 6
REMARK 465 SER F 1
REMARK 465 ALA F 2
REMARK 465 ALA F 3
REMARK 465 ALA F 4
REMARK 465 THR F 5
REMARK 465 GLN F 6
REMARK 465 SER G 1
REMARK 465 ALA G 2
REMARK 465 ALA G 3
REMARK 465 ALA G 4
REMARK 465 THR G 5
REMARK 465 GLN G 6
REMARK 465 ALA G 7
REMARK 465 SER H 1
REMARK 465 ALA H 2
REMARK 465 ALA H 3
REMARK 465 ALA H 4
REMARK 465 THR H 5
REMARK 465 GLN H 6
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 20 24.52 -147.88
REMARK 500 VAL A 120 -69.56 -106.60
REMARK 500 THR A 197 58.95 -148.25
REMARK 500 THR A 227 -76.49 -105.89
REMARK 500 SER A 260 -104.70 -104.10
REMARK 500 LEU A 269 -156.95 -120.31
REMARK 500 GLN A 300 59.04 -93.73
REMARK 500 GLN A 300 55.73 -93.73
REMARK 500 TYR A 379 56.30 -102.89
REMARK 500 LYS A 469 -131.62 56.19
REMARK 500 LEU A 477 167.64 67.61
REMARK 500 ASN B 20 31.24 -148.47
REMARK 500 VAL B 120 -73.13 -109.05
REMARK 500 THR B 197 59.30 -143.45
REMARK 500 THR B 227 -76.43 -105.73
REMARK 500 SER B 260 -101.52 -111.14
REMARK 500 LEU B 269 -159.04 -117.60
REMARK 500 GLN B 300 58.71 -96.47
REMARK 500 GLN B 300 58.19 -96.47
REMARK 500 TYR B 379 52.85 -91.59
REMARK 500 LYS B 469 -134.90 54.25
REMARK 500 LEU B 477 164.32 71.72
REMARK 500 ASN C 20 31.60 -151.45
REMARK 500 VAL C 120 -71.80 -109.56
REMARK 500 THR C 227 -78.10 -102.67
REMARK 500 SER C 260 -110.06 -111.42
REMARK 500 LEU C 269 -154.79 -119.09
REMARK 500 GLN C 300 59.28 -90.15
REMARK 500 LYS C 469 -133.46 54.48
REMARK 500 LEU C 477 163.99 74.20
REMARK 500 GLN C 497 109.63 -160.94
REMARK 500 ASN D 20 26.78 -149.26
REMARK 500 VAL D 120 -72.20 -109.16
REMARK 500 THR D 227 -76.18 -102.11
REMARK 500 SER D 260 -103.33 -98.72
REMARK 500 LEU D 269 -158.02 -117.55
REMARK 500 TYR D 379 58.91 -97.66
REMARK 500 LYS D 469 -133.30 57.65
REMARK 500 LEU D 477 165.37 70.03
REMARK 500 GLN D 497 111.58 -163.08
REMARK 500 ASN E 20 27.09 -152.15
REMARK 500 VAL E 120 -70.98 -110.88
REMARK 500 THR E 197 57.84 -146.61
REMARK 500 THR E 227 -79.97 -104.33
REMARK 500 SER E 260 -102.00 -106.46
REMARK 500 LEU E 269 -158.00 -115.37
REMARK 500 TYR E 379 58.30 -96.74
REMARK 500 LYS E 469 -134.64 54.73
REMARK 500 LEU E 477 165.18 72.02
REMARK 500 ASN F 20 30.28 -152.12
REMARK 500
REMARK 500 THIS ENTRY HAS 76 RAMACHANDRAN OUTLIERS.
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 NA A 601 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR A 39 OG1
REMARK 620 2 VAL A 40 O 98.9
REMARK 620 3 ASP A 109 OD1 55.8 98.6
REMARK 620 4 ASP A 109 O 134.1 96.6 79.4
REMARK 620 5 GLN A 196 O 74.6 169.3 84.9 94.0
REMARK 620 6 HOH A1923 O 72.1 79.8 127.0 153.5 90.0
REMARK 620 7 HOH A2100 O 143.6 91.9 156.1 78.1 88.7 75.9
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA B 602 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR B 39 OG1
REMARK 620 2 VAL B 40 O 103.2
REMARK 620 3 ASP B 109 OD1 57.7 102.1
REMARK 620 4 ASP B 109 O 135.0 97.8 79.2
REMARK 620 5 GLN B 196 O 72.0 167.6 85.1 93.4
REMARK 620 6 HOH B2152 O 133.2 87.6 163.7 86.5 87.8
REMARK 620 7 HOH B2756 O 67.5 83.7 124.9 155.2 83.9 68.7
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA C 603 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR C 39 OG1
REMARK 620 2 VAL C 40 O 99.8
REMARK 620 3 ASP C 109 O 134.9 100.3
REMARK 620 4 ASP C 109 OD1 56.3 102.7 80.0
REMARK 620 5 GLN C 196 O 72.3 166.2 93.2 82.5
REMARK 620 6 HOH C 688 O 65.9 85.1 155.8 122.1 81.3
REMARK 620 7 HOH C1967 O 133.6 91.8 85.5 161.0 86.2 70.7
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA D 604 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR D 39 OG1
REMARK 620 2 VAL D 40 O 101.6
REMARK 620 3 ASP D 109 O 135.9 100.2
REMARK 620 4 ASP D 109 OD1 56.6 103.1 81.3
REMARK 620 5 GLN D 196 O 71.4 166.3 92.7 83.1
REMARK 620 6 HOH D2487 O 67.9 84.5 152.4 124.4 82.0
REMARK 620 7 HOH D3277 O 128.0 91.7 88.9 163.5 84.1 63.7
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA E 605 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR E 39 OG1
REMARK 620 2 VAL E 40 O 101.1
REMARK 620 3 ASP E 109 O 134.2 98.8
REMARK 620 4 ASP E 109 OD1 57.9 101.7 77.9
REMARK 620 5 GLN E 196 O 70.6 168.4 92.7 81.1
REMARK 620 6 HOH E1968 O 129.0 97.4 88.0 157.7 82.5
REMARK 620 7 HOH E2044 O 68.3 84.1 155.0 126.0 85.2 67.0
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA F 606 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR F 39 OG1
REMARK 620 2 VAL F 40 O 101.2
REMARK 620 3 ASP F 109 OD1 57.0 109.3
REMARK 620 4 ASP F 109 O 137.0 101.2 81.0
REMARK 620 5 GLN F 196 O 74.4 162.7 82.7 92.8
REMARK 620 6 HOH F1738 O 137.9 89.4 154.5 78.3 83.5
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA G 607 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 VAL G 40 O
REMARK 620 2 ASP G 109 O 97.8
REMARK 620 3 ASP G 109 OD1 103.7 83.5
REMARK 620 4 GLN G 196 O 163.6 94.7 88.2
REMARK 620 5 HOH G1886 O 79.1 147.2 129.1 84.7
REMARK 620 6 HOH G3377 O 89.3 86.1 164.4 81.0 61.4
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA H 608 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR H 39 OG1
REMARK 620 2 VAL H 40 O 97.1
REMARK 620 3 ASP H 109 O 136.7 104.0
REMARK 620 4 ASP H 109 OD1 55.9 100.7 83.0
REMARK 620 5 GLN H 196 O 71.1 160.2 95.3 86.0
REMARK 620 6 HOH H2258 O 139.3 93.1 77.2 158.1 86.6
REMARK 620 7 HOH H3346 O 66.5 81.7 153.2 122.2 79.0 76.3
REMARK 620 N 1 2 3 4 5 6
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GAI A 801
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GAI A 811
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 901
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 911
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 921
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 941
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA B 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GAI B 802
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GAI B 812
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 902
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 912
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 942
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA C 603
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GAI C 803
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GAI C 813
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GAI C 823
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO C 903
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO C 913
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO C 923
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO C 943
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA D 604
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GAI D 804
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GAI D 814
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GAI D 833
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D 904
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D 944
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA E 605
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GAI E 805
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GAI E 815
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO E 905
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO E 915
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO E 925
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA F 606
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GAI F 806
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GAI F 816
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GAI F 826
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GAI F 845
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO F 906
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO F 916
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO F 926
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO F 946
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO F 966
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA G 607
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GAI G 807
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GAI G 817
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GAI G 838
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO G 907
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO G 917
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO G 927
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA H 608
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GAI H 808
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GAI H 818
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO H 908
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO H 928
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO H 948
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3N80 RELATED DB: PDB
REMARK 900 HUMAN MITOCHONDRIAL ALDEHYDE DEHYDROGENASE, APO FORM
REMARK 900 RELATED ID: 3N82 RELATED DB: PDB
REMARK 900 T244A MUTANT OF HUMAN MITOCHONDRIAL ALDEHYDE DEHYDROGENASE, NADH
REMARK 900 COMPLEX
REMARK 900 RELATED ID: 3N83 RELATED DB: PDB
REMARK 900 T244A MUTANT OF HUMAN MITOCHONDRIAL ALDEHYDE DEHYDROGENASE, NAD
REMARK 900 COMPLEX
DBREF 3N81 A 1 500 UNP P05091 ALDH2_HUMAN 18 517
DBREF 3N81 B 1 500 UNP P05091 ALDH2_HUMAN 18 517
DBREF 3N81 C 1 500 UNP P05091 ALDH2_HUMAN 18 517
DBREF 3N81 D 1 500 UNP P05091 ALDH2_HUMAN 18 517
DBREF 3N81 E 1 500 UNP P05091 ALDH2_HUMAN 18 517
DBREF 3N81 F 1 500 UNP P05091 ALDH2_HUMAN 18 517
DBREF 3N81 G 1 500 UNP P05091 ALDH2_HUMAN 18 517
DBREF 3N81 H 1 500 UNP P05091 ALDH2_HUMAN 18 517
SEQADV 3N81 ALA A 244 UNP P05091 THR 261 ENGINEERED MUTATION
SEQADV 3N81 ALA B 244 UNP P05091 THR 261 ENGINEERED MUTATION
SEQADV 3N81 ALA C 244 UNP P05091 THR 261 ENGINEERED MUTATION
SEQADV 3N81 ALA D 244 UNP P05091 THR 261 ENGINEERED MUTATION
SEQADV 3N81 ALA E 244 UNP P05091 THR 261 ENGINEERED MUTATION
SEQADV 3N81 ALA F 244 UNP P05091 THR 261 ENGINEERED MUTATION
SEQADV 3N81 ALA G 244 UNP P05091 THR 261 ENGINEERED MUTATION
SEQADV 3N81 ALA H 244 UNP P05091 THR 261 ENGINEERED MUTATION
SEQRES 1 A 500 SER ALA ALA ALA THR GLN ALA VAL PRO ALA PRO ASN GLN
SEQRES 2 A 500 GLN PRO GLU VAL PHE CYS ASN GLN ILE PHE ILE ASN ASN
SEQRES 3 A 500 GLU TRP HIS ASP ALA VAL SER ARG LYS THR PHE PRO THR
SEQRES 4 A 500 VAL ASN PRO SER THR GLY GLU VAL ILE CYS GLN VAL ALA
SEQRES 5 A 500 GLU GLY ASP LYS GLU ASP VAL ASP LYS ALA VAL LYS ALA
SEQRES 6 A 500 ALA ARG ALA ALA PHE GLN LEU GLY SER PRO TRP ARG ARG
SEQRES 7 A 500 MET ASP ALA SER HIS ARG GLY ARG LEU LEU ASN ARG LEU
SEQRES 8 A 500 ALA ASP LEU ILE GLU ARG ASP ARG THR TYR LEU ALA ALA
SEQRES 9 A 500 LEU GLU THR LEU ASP ASN GLY LYS PRO TYR VAL ILE SER
SEQRES 10 A 500 TYR LEU VAL ASP LEU ASP MET VAL LEU LYS CYS LEU ARG
SEQRES 11 A 500 TYR TYR ALA GLY TRP ALA ASP LYS TYR HIS GLY LYS THR
SEQRES 12 A 500 ILE PRO ILE ASP GLY ASP PHE PHE SER TYR THR ARG HIS
SEQRES 13 A 500 GLU PRO VAL GLY VAL CYS GLY GLN ILE ILE PRO TRP ASN
SEQRES 14 A 500 PHE PRO LEU LEU MET GLN ALA TRP LYS LEU GLY PRO ALA
SEQRES 15 A 500 LEU ALA THR GLY ASN VAL VAL VAL MET LYS VAL ALA GLU
SEQRES 16 A 500 GLN THR PRO LEU THR ALA LEU TYR VAL ALA ASN LEU ILE
SEQRES 17 A 500 LYS GLU ALA GLY PHE PRO PRO GLY VAL VAL ASN ILE VAL
SEQRES 18 A 500 PRO GLY PHE GLY PRO THR ALA GLY ALA ALA ILE ALA SER
SEQRES 19 A 500 HIS GLU ASP VAL ASP LYS VAL ALA PHE ALA GLY SER THR
SEQRES 20 A 500 GLU ILE GLY ARG VAL ILE GLN VAL ALA ALA GLY SER SER
SEQRES 21 A 500 ASN LEU LYS ARG VAL THR LEU GLU LEU GLY GLY LYS SER
SEQRES 22 A 500 PRO ASN ILE ILE MET SER ASP ALA ASP MET ASP TRP ALA
SEQRES 23 A 500 VAL GLU GLN ALA HIS PHE ALA LEU PHE PHE ASN GLN GLY
SEQRES 24 A 500 GLN CYS CYS CYS ALA GLY SER ARG THR PHE VAL GLN GLU
SEQRES 25 A 500 ASP ILE TYR ASP GLU PHE VAL GLU ARG SER VAL ALA ARG
SEQRES 26 A 500 ALA LYS SER ARG VAL VAL GLY ASN PRO PHE ASP SER LYS
SEQRES 27 A 500 THR GLU GLN GLY PRO GLN VAL ASP GLU THR GLN PHE LYS
SEQRES 28 A 500 LYS ILE LEU GLY TYR ILE ASN THR GLY LYS GLN GLU GLY
SEQRES 29 A 500 ALA LYS LEU LEU CYS GLY GLY GLY ILE ALA ALA ASP ARG
SEQRES 30 A 500 GLY TYR PHE ILE GLN PRO THR VAL PHE GLY ASP VAL GLN
SEQRES 31 A 500 ASP GLY MET THR ILE ALA LYS GLU GLU ILE PHE GLY PRO
SEQRES 32 A 500 VAL MET GLN ILE LEU LYS PHE LYS THR ILE GLU GLU VAL
SEQRES 33 A 500 VAL GLY ARG ALA ASN ASN SER THR TYR GLY LEU ALA ALA
SEQRES 34 A 500 ALA VAL PHE THR LYS ASP LEU ASP LYS ALA ASN TYR LEU
SEQRES 35 A 500 SER GLN ALA LEU GLN ALA GLY THR VAL TRP VAL ASN CYS
SEQRES 36 A 500 TYR ASP VAL PHE GLY ALA GLN SER PRO PHE GLY GLY TYR
SEQRES 37 A 500 LYS MET SER GLY SER GLY ARG GLU LEU GLY GLU TYR GLY
SEQRES 38 A 500 LEU GLN ALA TYR THR GLU VAL LYS THR VAL THR VAL LYS
SEQRES 39 A 500 VAL PRO GLN LYS ASN SER
SEQRES 1 B 500 SER ALA ALA ALA THR GLN ALA VAL PRO ALA PRO ASN GLN
SEQRES 2 B 500 GLN PRO GLU VAL PHE CYS ASN GLN ILE PHE ILE ASN ASN
SEQRES 3 B 500 GLU TRP HIS ASP ALA VAL SER ARG LYS THR PHE PRO THR
SEQRES 4 B 500 VAL ASN PRO SER THR GLY GLU VAL ILE CYS GLN VAL ALA
SEQRES 5 B 500 GLU GLY ASP LYS GLU ASP VAL ASP LYS ALA VAL LYS ALA
SEQRES 6 B 500 ALA ARG ALA ALA PHE GLN LEU GLY SER PRO TRP ARG ARG
SEQRES 7 B 500 MET ASP ALA SER HIS ARG GLY ARG LEU LEU ASN ARG LEU
SEQRES 8 B 500 ALA ASP LEU ILE GLU ARG ASP ARG THR TYR LEU ALA ALA
SEQRES 9 B 500 LEU GLU THR LEU ASP ASN GLY LYS PRO TYR VAL ILE SER
SEQRES 10 B 500 TYR LEU VAL ASP LEU ASP MET VAL LEU LYS CYS LEU ARG
SEQRES 11 B 500 TYR TYR ALA GLY TRP ALA ASP LYS TYR HIS GLY LYS THR
SEQRES 12 B 500 ILE PRO ILE ASP GLY ASP PHE PHE SER TYR THR ARG HIS
SEQRES 13 B 500 GLU PRO VAL GLY VAL CYS GLY GLN ILE ILE PRO TRP ASN
SEQRES 14 B 500 PHE PRO LEU LEU MET GLN ALA TRP LYS LEU GLY PRO ALA
SEQRES 15 B 500 LEU ALA THR GLY ASN VAL VAL VAL MET LYS VAL ALA GLU
SEQRES 16 B 500 GLN THR PRO LEU THR ALA LEU TYR VAL ALA ASN LEU ILE
SEQRES 17 B 500 LYS GLU ALA GLY PHE PRO PRO GLY VAL VAL ASN ILE VAL
SEQRES 18 B 500 PRO GLY PHE GLY PRO THR ALA GLY ALA ALA ILE ALA SER
SEQRES 19 B 500 HIS GLU ASP VAL ASP LYS VAL ALA PHE ALA GLY SER THR
SEQRES 20 B 500 GLU ILE GLY ARG VAL ILE GLN VAL ALA ALA GLY SER SER
SEQRES 21 B 500 ASN LEU LYS ARG VAL THR LEU GLU LEU GLY GLY LYS SER
SEQRES 22 B 500 PRO ASN ILE ILE MET SER ASP ALA ASP MET ASP TRP ALA
SEQRES 23 B 500 VAL GLU GLN ALA HIS PHE ALA LEU PHE PHE ASN GLN GLY
SEQRES 24 B 500 GLN CYS CYS CYS ALA GLY SER ARG THR PHE VAL GLN GLU
SEQRES 25 B 500 ASP ILE TYR ASP GLU PHE VAL GLU ARG SER VAL ALA ARG
SEQRES 26 B 500 ALA LYS SER ARG VAL VAL GLY ASN PRO PHE ASP SER LYS
SEQRES 27 B 500 THR GLU GLN GLY PRO GLN VAL ASP GLU THR GLN PHE LYS
SEQRES 28 B 500 LYS ILE LEU GLY TYR ILE ASN THR GLY LYS GLN GLU GLY
SEQRES 29 B 500 ALA LYS LEU LEU CYS GLY GLY GLY ILE ALA ALA ASP ARG
SEQRES 30 B 500 GLY TYR PHE ILE GLN PRO THR VAL PHE GLY ASP VAL GLN
SEQRES 31 B 500 ASP GLY MET THR ILE ALA LYS GLU GLU ILE PHE GLY PRO
SEQRES 32 B 500 VAL MET GLN ILE LEU LYS PHE LYS THR ILE GLU GLU VAL
SEQRES 33 B 500 VAL GLY ARG ALA ASN ASN SER THR TYR GLY LEU ALA ALA
SEQRES 34 B 500 ALA VAL PHE THR LYS ASP LEU ASP LYS ALA ASN TYR LEU
SEQRES 35 B 500 SER GLN ALA LEU GLN ALA GLY THR VAL TRP VAL ASN CYS
SEQRES 36 B 500 TYR ASP VAL PHE GLY ALA GLN SER PRO PHE GLY GLY TYR
SEQRES 37 B 500 LYS MET SER GLY SER GLY ARG GLU LEU GLY GLU TYR GLY
SEQRES 38 B 500 LEU GLN ALA TYR THR GLU VAL LYS THR VAL THR VAL LYS
SEQRES 39 B 500 VAL PRO GLN LYS ASN SER
SEQRES 1 C 500 SER ALA ALA ALA THR GLN ALA VAL PRO ALA PRO ASN GLN
SEQRES 2 C 500 GLN PRO GLU VAL PHE CYS ASN GLN ILE PHE ILE ASN ASN
SEQRES 3 C 500 GLU TRP HIS ASP ALA VAL SER ARG LYS THR PHE PRO THR
SEQRES 4 C 500 VAL ASN PRO SER THR GLY GLU VAL ILE CYS GLN VAL ALA
SEQRES 5 C 500 GLU GLY ASP LYS GLU ASP VAL ASP LYS ALA VAL LYS ALA
SEQRES 6 C 500 ALA ARG ALA ALA PHE GLN LEU GLY SER PRO TRP ARG ARG
SEQRES 7 C 500 MET ASP ALA SER HIS ARG GLY ARG LEU LEU ASN ARG LEU
SEQRES 8 C 500 ALA ASP LEU ILE GLU ARG ASP ARG THR TYR LEU ALA ALA
SEQRES 9 C 500 LEU GLU THR LEU ASP ASN GLY LYS PRO TYR VAL ILE SER
SEQRES 10 C 500 TYR LEU VAL ASP LEU ASP MET VAL LEU LYS CYS LEU ARG
SEQRES 11 C 500 TYR TYR ALA GLY TRP ALA ASP LYS TYR HIS GLY LYS THR
SEQRES 12 C 500 ILE PRO ILE ASP GLY ASP PHE PHE SER TYR THR ARG HIS
SEQRES 13 C 500 GLU PRO VAL GLY VAL CYS GLY GLN ILE ILE PRO TRP ASN
SEQRES 14 C 500 PHE PRO LEU LEU MET GLN ALA TRP LYS LEU GLY PRO ALA
SEQRES 15 C 500 LEU ALA THR GLY ASN VAL VAL VAL MET LYS VAL ALA GLU
SEQRES 16 C 500 GLN THR PRO LEU THR ALA LEU TYR VAL ALA ASN LEU ILE
SEQRES 17 C 500 LYS GLU ALA GLY PHE PRO PRO GLY VAL VAL ASN ILE VAL
SEQRES 18 C 500 PRO GLY PHE GLY PRO THR ALA GLY ALA ALA ILE ALA SER
SEQRES 19 C 500 HIS GLU ASP VAL ASP LYS VAL ALA PHE ALA GLY SER THR
SEQRES 20 C 500 GLU ILE GLY ARG VAL ILE GLN VAL ALA ALA GLY SER SER
SEQRES 21 C 500 ASN LEU LYS ARG VAL THR LEU GLU LEU GLY GLY LYS SER
SEQRES 22 C 500 PRO ASN ILE ILE MET SER ASP ALA ASP MET ASP TRP ALA
SEQRES 23 C 500 VAL GLU GLN ALA HIS PHE ALA LEU PHE PHE ASN GLN GLY
SEQRES 24 C 500 GLN CYS CYS CYS ALA GLY SER ARG THR PHE VAL GLN GLU
SEQRES 25 C 500 ASP ILE TYR ASP GLU PHE VAL GLU ARG SER VAL ALA ARG
SEQRES 26 C 500 ALA LYS SER ARG VAL VAL GLY ASN PRO PHE ASP SER LYS
SEQRES 27 C 500 THR GLU GLN GLY PRO GLN VAL ASP GLU THR GLN PHE LYS
SEQRES 28 C 500 LYS ILE LEU GLY TYR ILE ASN THR GLY LYS GLN GLU GLY
SEQRES 29 C 500 ALA LYS LEU LEU CYS GLY GLY GLY ILE ALA ALA ASP ARG
SEQRES 30 C 500 GLY TYR PHE ILE GLN PRO THR VAL PHE GLY ASP VAL GLN
SEQRES 31 C 500 ASP GLY MET THR ILE ALA LYS GLU GLU ILE PHE GLY PRO
SEQRES 32 C 500 VAL MET GLN ILE LEU LYS PHE LYS THR ILE GLU GLU VAL
SEQRES 33 C 500 VAL GLY ARG ALA ASN ASN SER THR TYR GLY LEU ALA ALA
SEQRES 34 C 500 ALA VAL PHE THR LYS ASP LEU ASP LYS ALA ASN TYR LEU
SEQRES 35 C 500 SER GLN ALA LEU GLN ALA GLY THR VAL TRP VAL ASN CYS
SEQRES 36 C 500 TYR ASP VAL PHE GLY ALA GLN SER PRO PHE GLY GLY TYR
SEQRES 37 C 500 LYS MET SER GLY SER GLY ARG GLU LEU GLY GLU TYR GLY
SEQRES 38 C 500 LEU GLN ALA TYR THR GLU VAL LYS THR VAL THR VAL LYS
SEQRES 39 C 500 VAL PRO GLN LYS ASN SER
SEQRES 1 D 500 SER ALA ALA ALA THR GLN ALA VAL PRO ALA PRO ASN GLN
SEQRES 2 D 500 GLN PRO GLU VAL PHE CYS ASN GLN ILE PHE ILE ASN ASN
SEQRES 3 D 500 GLU TRP HIS ASP ALA VAL SER ARG LYS THR PHE PRO THR
SEQRES 4 D 500 VAL ASN PRO SER THR GLY GLU VAL ILE CYS GLN VAL ALA
SEQRES 5 D 500 GLU GLY ASP LYS GLU ASP VAL ASP LYS ALA VAL LYS ALA
SEQRES 6 D 500 ALA ARG ALA ALA PHE GLN LEU GLY SER PRO TRP ARG ARG
SEQRES 7 D 500 MET ASP ALA SER HIS ARG GLY ARG LEU LEU ASN ARG LEU
SEQRES 8 D 500 ALA ASP LEU ILE GLU ARG ASP ARG THR TYR LEU ALA ALA
SEQRES 9 D 500 LEU GLU THR LEU ASP ASN GLY LYS PRO TYR VAL ILE SER
SEQRES 10 D 500 TYR LEU VAL ASP LEU ASP MET VAL LEU LYS CYS LEU ARG
SEQRES 11 D 500 TYR TYR ALA GLY TRP ALA ASP LYS TYR HIS GLY LYS THR
SEQRES 12 D 500 ILE PRO ILE ASP GLY ASP PHE PHE SER TYR THR ARG HIS
SEQRES 13 D 500 GLU PRO VAL GLY VAL CYS GLY GLN ILE ILE PRO TRP ASN
SEQRES 14 D 500 PHE PRO LEU LEU MET GLN ALA TRP LYS LEU GLY PRO ALA
SEQRES 15 D 500 LEU ALA THR GLY ASN VAL VAL VAL MET LYS VAL ALA GLU
SEQRES 16 D 500 GLN THR PRO LEU THR ALA LEU TYR VAL ALA ASN LEU ILE
SEQRES 17 D 500 LYS GLU ALA GLY PHE PRO PRO GLY VAL VAL ASN ILE VAL
SEQRES 18 D 500 PRO GLY PHE GLY PRO THR ALA GLY ALA ALA ILE ALA SER
SEQRES 19 D 500 HIS GLU ASP VAL ASP LYS VAL ALA PHE ALA GLY SER THR
SEQRES 20 D 500 GLU ILE GLY ARG VAL ILE GLN VAL ALA ALA GLY SER SER
SEQRES 21 D 500 ASN LEU LYS ARG VAL THR LEU GLU LEU GLY GLY LYS SER
SEQRES 22 D 500 PRO ASN ILE ILE MET SER ASP ALA ASP MET ASP TRP ALA
SEQRES 23 D 500 VAL GLU GLN ALA HIS PHE ALA LEU PHE PHE ASN GLN GLY
SEQRES 24 D 500 GLN CYS CYS CYS ALA GLY SER ARG THR PHE VAL GLN GLU
SEQRES 25 D 500 ASP ILE TYR ASP GLU PHE VAL GLU ARG SER VAL ALA ARG
SEQRES 26 D 500 ALA LYS SER ARG VAL VAL GLY ASN PRO PHE ASP SER LYS
SEQRES 27 D 500 THR GLU GLN GLY PRO GLN VAL ASP GLU THR GLN PHE LYS
SEQRES 28 D 500 LYS ILE LEU GLY TYR ILE ASN THR GLY LYS GLN GLU GLY
SEQRES 29 D 500 ALA LYS LEU LEU CYS GLY GLY GLY ILE ALA ALA ASP ARG
SEQRES 30 D 500 GLY TYR PHE ILE GLN PRO THR VAL PHE GLY ASP VAL GLN
SEQRES 31 D 500 ASP GLY MET THR ILE ALA LYS GLU GLU ILE PHE GLY PRO
SEQRES 32 D 500 VAL MET GLN ILE LEU LYS PHE LYS THR ILE GLU GLU VAL
SEQRES 33 D 500 VAL GLY ARG ALA ASN ASN SER THR TYR GLY LEU ALA ALA
SEQRES 34 D 500 ALA VAL PHE THR LYS ASP LEU ASP LYS ALA ASN TYR LEU
SEQRES 35 D 500 SER GLN ALA LEU GLN ALA GLY THR VAL TRP VAL ASN CYS
SEQRES 36 D 500 TYR ASP VAL PHE GLY ALA GLN SER PRO PHE GLY GLY TYR
SEQRES 37 D 500 LYS MET SER GLY SER GLY ARG GLU LEU GLY GLU TYR GLY
SEQRES 38 D 500 LEU GLN ALA TYR THR GLU VAL LYS THR VAL THR VAL LYS
SEQRES 39 D 500 VAL PRO GLN LYS ASN SER
SEQRES 1 E 500 SER ALA ALA ALA THR GLN ALA VAL PRO ALA PRO ASN GLN
SEQRES 2 E 500 GLN PRO GLU VAL PHE CYS ASN GLN ILE PHE ILE ASN ASN
SEQRES 3 E 500 GLU TRP HIS ASP ALA VAL SER ARG LYS THR PHE PRO THR
SEQRES 4 E 500 VAL ASN PRO SER THR GLY GLU VAL ILE CYS GLN VAL ALA
SEQRES 5 E 500 GLU GLY ASP LYS GLU ASP VAL ASP LYS ALA VAL LYS ALA
SEQRES 6 E 500 ALA ARG ALA ALA PHE GLN LEU GLY SER PRO TRP ARG ARG
SEQRES 7 E 500 MET ASP ALA SER HIS ARG GLY ARG LEU LEU ASN ARG LEU
SEQRES 8 E 500 ALA ASP LEU ILE GLU ARG ASP ARG THR TYR LEU ALA ALA
SEQRES 9 E 500 LEU GLU THR LEU ASP ASN GLY LYS PRO TYR VAL ILE SER
SEQRES 10 E 500 TYR LEU VAL ASP LEU ASP MET VAL LEU LYS CYS LEU ARG
SEQRES 11 E 500 TYR TYR ALA GLY TRP ALA ASP LYS TYR HIS GLY LYS THR
SEQRES 12 E 500 ILE PRO ILE ASP GLY ASP PHE PHE SER TYR THR ARG HIS
SEQRES 13 E 500 GLU PRO VAL GLY VAL CYS GLY GLN ILE ILE PRO TRP ASN
SEQRES 14 E 500 PHE PRO LEU LEU MET GLN ALA TRP LYS LEU GLY PRO ALA
SEQRES 15 E 500 LEU ALA THR GLY ASN VAL VAL VAL MET LYS VAL ALA GLU
SEQRES 16 E 500 GLN THR PRO LEU THR ALA LEU TYR VAL ALA ASN LEU ILE
SEQRES 17 E 500 LYS GLU ALA GLY PHE PRO PRO GLY VAL VAL ASN ILE VAL
SEQRES 18 E 500 PRO GLY PHE GLY PRO THR ALA GLY ALA ALA ILE ALA SER
SEQRES 19 E 500 HIS GLU ASP VAL ASP LYS VAL ALA PHE ALA GLY SER THR
SEQRES 20 E 500 GLU ILE GLY ARG VAL ILE GLN VAL ALA ALA GLY SER SER
SEQRES 21 E 500 ASN LEU LYS ARG VAL THR LEU GLU LEU GLY GLY LYS SER
SEQRES 22 E 500 PRO ASN ILE ILE MET SER ASP ALA ASP MET ASP TRP ALA
SEQRES 23 E 500 VAL GLU GLN ALA HIS PHE ALA LEU PHE PHE ASN GLN GLY
SEQRES 24 E 500 GLN CYS CYS CYS ALA GLY SER ARG THR PHE VAL GLN GLU
SEQRES 25 E 500 ASP ILE TYR ASP GLU PHE VAL GLU ARG SER VAL ALA ARG
SEQRES 26 E 500 ALA LYS SER ARG VAL VAL GLY ASN PRO PHE ASP SER LYS
SEQRES 27 E 500 THR GLU GLN GLY PRO GLN VAL ASP GLU THR GLN PHE LYS
SEQRES 28 E 500 LYS ILE LEU GLY TYR ILE ASN THR GLY LYS GLN GLU GLY
SEQRES 29 E 500 ALA LYS LEU LEU CYS GLY GLY GLY ILE ALA ALA ASP ARG
SEQRES 30 E 500 GLY TYR PHE ILE GLN PRO THR VAL PHE GLY ASP VAL GLN
SEQRES 31 E 500 ASP GLY MET THR ILE ALA LYS GLU GLU ILE PHE GLY PRO
SEQRES 32 E 500 VAL MET GLN ILE LEU LYS PHE LYS THR ILE GLU GLU VAL
SEQRES 33 E 500 VAL GLY ARG ALA ASN ASN SER THR TYR GLY LEU ALA ALA
SEQRES 34 E 500 ALA VAL PHE THR LYS ASP LEU ASP LYS ALA ASN TYR LEU
SEQRES 35 E 500 SER GLN ALA LEU GLN ALA GLY THR VAL TRP VAL ASN CYS
SEQRES 36 E 500 TYR ASP VAL PHE GLY ALA GLN SER PRO PHE GLY GLY TYR
SEQRES 37 E 500 LYS MET SER GLY SER GLY ARG GLU LEU GLY GLU TYR GLY
SEQRES 38 E 500 LEU GLN ALA TYR THR GLU VAL LYS THR VAL THR VAL LYS
SEQRES 39 E 500 VAL PRO GLN LYS ASN SER
SEQRES 1 F 500 SER ALA ALA ALA THR GLN ALA VAL PRO ALA PRO ASN GLN
SEQRES 2 F 500 GLN PRO GLU VAL PHE CYS ASN GLN ILE PHE ILE ASN ASN
SEQRES 3 F 500 GLU TRP HIS ASP ALA VAL SER ARG LYS THR PHE PRO THR
SEQRES 4 F 500 VAL ASN PRO SER THR GLY GLU VAL ILE CYS GLN VAL ALA
SEQRES 5 F 500 GLU GLY ASP LYS GLU ASP VAL ASP LYS ALA VAL LYS ALA
SEQRES 6 F 500 ALA ARG ALA ALA PHE GLN LEU GLY SER PRO TRP ARG ARG
SEQRES 7 F 500 MET ASP ALA SER HIS ARG GLY ARG LEU LEU ASN ARG LEU
SEQRES 8 F 500 ALA ASP LEU ILE GLU ARG ASP ARG THR TYR LEU ALA ALA
SEQRES 9 F 500 LEU GLU THR LEU ASP ASN GLY LYS PRO TYR VAL ILE SER
SEQRES 10 F 500 TYR LEU VAL ASP LEU ASP MET VAL LEU LYS CYS LEU ARG
SEQRES 11 F 500 TYR TYR ALA GLY TRP ALA ASP LYS TYR HIS GLY LYS THR
SEQRES 12 F 500 ILE PRO ILE ASP GLY ASP PHE PHE SER TYR THR ARG HIS
SEQRES 13 F 500 GLU PRO VAL GLY VAL CYS GLY GLN ILE ILE PRO TRP ASN
SEQRES 14 F 500 PHE PRO LEU LEU MET GLN ALA TRP LYS LEU GLY PRO ALA
SEQRES 15 F 500 LEU ALA THR GLY ASN VAL VAL VAL MET LYS VAL ALA GLU
SEQRES 16 F 500 GLN THR PRO LEU THR ALA LEU TYR VAL ALA ASN LEU ILE
SEQRES 17 F 500 LYS GLU ALA GLY PHE PRO PRO GLY VAL VAL ASN ILE VAL
SEQRES 18 F 500 PRO GLY PHE GLY PRO THR ALA GLY ALA ALA ILE ALA SER
SEQRES 19 F 500 HIS GLU ASP VAL ASP LYS VAL ALA PHE ALA GLY SER THR
SEQRES 20 F 500 GLU ILE GLY ARG VAL ILE GLN VAL ALA ALA GLY SER SER
SEQRES 21 F 500 ASN LEU LYS ARG VAL THR LEU GLU LEU GLY GLY LYS SER
SEQRES 22 F 500 PRO ASN ILE ILE MET SER ASP ALA ASP MET ASP TRP ALA
SEQRES 23 F 500 VAL GLU GLN ALA HIS PHE ALA LEU PHE PHE ASN GLN GLY
SEQRES 24 F 500 GLN CYS CYS CYS ALA GLY SER ARG THR PHE VAL GLN GLU
SEQRES 25 F 500 ASP ILE TYR ASP GLU PHE VAL GLU ARG SER VAL ALA ARG
SEQRES 26 F 500 ALA LYS SER ARG VAL VAL GLY ASN PRO PHE ASP SER LYS
SEQRES 27 F 500 THR GLU GLN GLY PRO GLN VAL ASP GLU THR GLN PHE LYS
SEQRES 28 F 500 LYS ILE LEU GLY TYR ILE ASN THR GLY LYS GLN GLU GLY
SEQRES 29 F 500 ALA LYS LEU LEU CYS GLY GLY GLY ILE ALA ALA ASP ARG
SEQRES 30 F 500 GLY TYR PHE ILE GLN PRO THR VAL PHE GLY ASP VAL GLN
SEQRES 31 F 500 ASP GLY MET THR ILE ALA LYS GLU GLU ILE PHE GLY PRO
SEQRES 32 F 500 VAL MET GLN ILE LEU LYS PHE LYS THR ILE GLU GLU VAL
SEQRES 33 F 500 VAL GLY ARG ALA ASN ASN SER THR TYR GLY LEU ALA ALA
SEQRES 34 F 500 ALA VAL PHE THR LYS ASP LEU ASP LYS ALA ASN TYR LEU
SEQRES 35 F 500 SER GLN ALA LEU GLN ALA GLY THR VAL TRP VAL ASN CYS
SEQRES 36 F 500 TYR ASP VAL PHE GLY ALA GLN SER PRO PHE GLY GLY TYR
SEQRES 37 F 500 LYS MET SER GLY SER GLY ARG GLU LEU GLY GLU TYR GLY
SEQRES 38 F 500 LEU GLN ALA TYR THR GLU VAL LYS THR VAL THR VAL LYS
SEQRES 39 F 500 VAL PRO GLN LYS ASN SER
SEQRES 1 G 500 SER ALA ALA ALA THR GLN ALA VAL PRO ALA PRO ASN GLN
SEQRES 2 G 500 GLN PRO GLU VAL PHE CYS ASN GLN ILE PHE ILE ASN ASN
SEQRES 3 G 500 GLU TRP HIS ASP ALA VAL SER ARG LYS THR PHE PRO THR
SEQRES 4 G 500 VAL ASN PRO SER THR GLY GLU VAL ILE CYS GLN VAL ALA
SEQRES 5 G 500 GLU GLY ASP LYS GLU ASP VAL ASP LYS ALA VAL LYS ALA
SEQRES 6 G 500 ALA ARG ALA ALA PHE GLN LEU GLY SER PRO TRP ARG ARG
SEQRES 7 G 500 MET ASP ALA SER HIS ARG GLY ARG LEU LEU ASN ARG LEU
SEQRES 8 G 500 ALA ASP LEU ILE GLU ARG ASP ARG THR TYR LEU ALA ALA
SEQRES 9 G 500 LEU GLU THR LEU ASP ASN GLY LYS PRO TYR VAL ILE SER
SEQRES 10 G 500 TYR LEU VAL ASP LEU ASP MET VAL LEU LYS CYS LEU ARG
SEQRES 11 G 500 TYR TYR ALA GLY TRP ALA ASP LYS TYR HIS GLY LYS THR
SEQRES 12 G 500 ILE PRO ILE ASP GLY ASP PHE PHE SER TYR THR ARG HIS
SEQRES 13 G 500 GLU PRO VAL GLY VAL CYS GLY GLN ILE ILE PRO TRP ASN
SEQRES 14 G 500 PHE PRO LEU LEU MET GLN ALA TRP LYS LEU GLY PRO ALA
SEQRES 15 G 500 LEU ALA THR GLY ASN VAL VAL VAL MET LYS VAL ALA GLU
SEQRES 16 G 500 GLN THR PRO LEU THR ALA LEU TYR VAL ALA ASN LEU ILE
SEQRES 17 G 500 LYS GLU ALA GLY PHE PRO PRO GLY VAL VAL ASN ILE VAL
SEQRES 18 G 500 PRO GLY PHE GLY PRO THR ALA GLY ALA ALA ILE ALA SER
SEQRES 19 G 500 HIS GLU ASP VAL ASP LYS VAL ALA PHE ALA GLY SER THR
SEQRES 20 G 500 GLU ILE GLY ARG VAL ILE GLN VAL ALA ALA GLY SER SER
SEQRES 21 G 500 ASN LEU LYS ARG VAL THR LEU GLU LEU GLY GLY LYS SER
SEQRES 22 G 500 PRO ASN ILE ILE MET SER ASP ALA ASP MET ASP TRP ALA
SEQRES 23 G 500 VAL GLU GLN ALA HIS PHE ALA LEU PHE PHE ASN GLN GLY
SEQRES 24 G 500 GLN CYS CYS CYS ALA GLY SER ARG THR PHE VAL GLN GLU
SEQRES 25 G 500 ASP ILE TYR ASP GLU PHE VAL GLU ARG SER VAL ALA ARG
SEQRES 26 G 500 ALA LYS SER ARG VAL VAL GLY ASN PRO PHE ASP SER LYS
SEQRES 27 G 500 THR GLU GLN GLY PRO GLN VAL ASP GLU THR GLN PHE LYS
SEQRES 28 G 500 LYS ILE LEU GLY TYR ILE ASN THR GLY LYS GLN GLU GLY
SEQRES 29 G 500 ALA LYS LEU LEU CYS GLY GLY GLY ILE ALA ALA ASP ARG
SEQRES 30 G 500 GLY TYR PHE ILE GLN PRO THR VAL PHE GLY ASP VAL GLN
SEQRES 31 G 500 ASP GLY MET THR ILE ALA LYS GLU GLU ILE PHE GLY PRO
SEQRES 32 G 500 VAL MET GLN ILE LEU LYS PHE LYS THR ILE GLU GLU VAL
SEQRES 33 G 500 VAL GLY ARG ALA ASN ASN SER THR TYR GLY LEU ALA ALA
SEQRES 34 G 500 ALA VAL PHE THR LYS ASP LEU ASP LYS ALA ASN TYR LEU
SEQRES 35 G 500 SER GLN ALA LEU GLN ALA GLY THR VAL TRP VAL ASN CYS
SEQRES 36 G 500 TYR ASP VAL PHE GLY ALA GLN SER PRO PHE GLY GLY TYR
SEQRES 37 G 500 LYS MET SER GLY SER GLY ARG GLU LEU GLY GLU TYR GLY
SEQRES 38 G 500 LEU GLN ALA TYR THR GLU VAL LYS THR VAL THR VAL LYS
SEQRES 39 G 500 VAL PRO GLN LYS ASN SER
SEQRES 1 H 500 SER ALA ALA ALA THR GLN ALA VAL PRO ALA PRO ASN GLN
SEQRES 2 H 500 GLN PRO GLU VAL PHE CYS ASN GLN ILE PHE ILE ASN ASN
SEQRES 3 H 500 GLU TRP HIS ASP ALA VAL SER ARG LYS THR PHE PRO THR
SEQRES 4 H 500 VAL ASN PRO SER THR GLY GLU VAL ILE CYS GLN VAL ALA
SEQRES 5 H 500 GLU GLY ASP LYS GLU ASP VAL ASP LYS ALA VAL LYS ALA
SEQRES 6 H 500 ALA ARG ALA ALA PHE GLN LEU GLY SER PRO TRP ARG ARG
SEQRES 7 H 500 MET ASP ALA SER HIS ARG GLY ARG LEU LEU ASN ARG LEU
SEQRES 8 H 500 ALA ASP LEU ILE GLU ARG ASP ARG THR TYR LEU ALA ALA
SEQRES 9 H 500 LEU GLU THR LEU ASP ASN GLY LYS PRO TYR VAL ILE SER
SEQRES 10 H 500 TYR LEU VAL ASP LEU ASP MET VAL LEU LYS CYS LEU ARG
SEQRES 11 H 500 TYR TYR ALA GLY TRP ALA ASP LYS TYR HIS GLY LYS THR
SEQRES 12 H 500 ILE PRO ILE ASP GLY ASP PHE PHE SER TYR THR ARG HIS
SEQRES 13 H 500 GLU PRO VAL GLY VAL CYS GLY GLN ILE ILE PRO TRP ASN
SEQRES 14 H 500 PHE PRO LEU LEU MET GLN ALA TRP LYS LEU GLY PRO ALA
SEQRES 15 H 500 LEU ALA THR GLY ASN VAL VAL VAL MET LYS VAL ALA GLU
SEQRES 16 H 500 GLN THR PRO LEU THR ALA LEU TYR VAL ALA ASN LEU ILE
SEQRES 17 H 500 LYS GLU ALA GLY PHE PRO PRO GLY VAL VAL ASN ILE VAL
SEQRES 18 H 500 PRO GLY PHE GLY PRO THR ALA GLY ALA ALA ILE ALA SER
SEQRES 19 H 500 HIS GLU ASP VAL ASP LYS VAL ALA PHE ALA GLY SER THR
SEQRES 20 H 500 GLU ILE GLY ARG VAL ILE GLN VAL ALA ALA GLY SER SER
SEQRES 21 H 500 ASN LEU LYS ARG VAL THR LEU GLU LEU GLY GLY LYS SER
SEQRES 22 H 500 PRO ASN ILE ILE MET SER ASP ALA ASP MET ASP TRP ALA
SEQRES 23 H 500 VAL GLU GLN ALA HIS PHE ALA LEU PHE PHE ASN GLN GLY
SEQRES 24 H 500 GLN CYS CYS CYS ALA GLY SER ARG THR PHE VAL GLN GLU
SEQRES 25 H 500 ASP ILE TYR ASP GLU PHE VAL GLU ARG SER VAL ALA ARG
SEQRES 26 H 500 ALA LYS SER ARG VAL VAL GLY ASN PRO PHE ASP SER LYS
SEQRES 27 H 500 THR GLU GLN GLY PRO GLN VAL ASP GLU THR GLN PHE LYS
SEQRES 28 H 500 LYS ILE LEU GLY TYR ILE ASN THR GLY LYS GLN GLU GLY
SEQRES 29 H 500 ALA LYS LEU LEU CYS GLY GLY GLY ILE ALA ALA ASP ARG
SEQRES 30 H 500 GLY TYR PHE ILE GLN PRO THR VAL PHE GLY ASP VAL GLN
SEQRES 31 H 500 ASP GLY MET THR ILE ALA LYS GLU GLU ILE PHE GLY PRO
SEQRES 32 H 500 VAL MET GLN ILE LEU LYS PHE LYS THR ILE GLU GLU VAL
SEQRES 33 H 500 VAL GLY ARG ALA ASN ASN SER THR TYR GLY LEU ALA ALA
SEQRES 34 H 500 ALA VAL PHE THR LYS ASP LEU ASP LYS ALA ASN TYR LEU
SEQRES 35 H 500 SER GLN ALA LEU GLN ALA GLY THR VAL TRP VAL ASN CYS
SEQRES 36 H 500 TYR ASP VAL PHE GLY ALA GLN SER PRO PHE GLY GLY TYR
SEQRES 37 H 500 LYS MET SER GLY SER GLY ARG GLU LEU GLY GLU TYR GLY
SEQRES 38 H 500 LEU GLN ALA TYR THR GLU VAL LYS THR VAL THR VAL LYS
SEQRES 39 H 500 VAL PRO GLN LYS ASN SER
HET NA A 601 1
HET GAI A 801 4
HET GAI A 811 4
HET EDO A 901 4
HET EDO A 911 4
HET EDO A 921 4
HET EDO A 941 4
HET NA B 602 1
HET GAI B 802 4
HET GAI B 812 4
HET EDO B 902 4
HET EDO B 912 4
HET EDO B 942 4
HET NA C 603 1
HET GAI C 803 4
HET GAI C 813 4
HET GAI C 823 4
HET EDO C 903 4
HET EDO C 913 4
HET EDO C 923 4
HET EDO C 943 4
HET NA D 604 1
HET GAI D 804 4
HET GAI D 814 4
HET GAI D 833 4
HET EDO D 904 4
HET EDO D 944 4
HET NA E 605 1
HET GAI E 805 4
HET GAI E 815 4
HET EDO E 905 4
HET EDO E 915 4
HET EDO E 925 4
HET NA F 606 1
HET GAI F 806 4
HET GAI F 816 4
HET GAI F 826 4
HET GAI F 845 4
HET EDO F 906 4
HET EDO F 916 4
HET EDO F 926 4
HET EDO F 946 4
HET EDO F 966 4
HET NA G 607 1
HET GAI G 807 4
HET GAI G 817 4
HET GAI G 838 4
HET EDO G 907 4
HET EDO G 917 4
HET EDO G 927 4
HET NA H 608 1
HET GAI H 808 4
HET GAI H 818 4
HET EDO H 908 4
HET EDO H 928 4
HET EDO H 948 4
HETNAM NA SODIUM ION
HETNAM GAI GUANIDINE
HETNAM EDO 1,2-ETHANEDIOL
HETSYN EDO ETHYLENE GLYCOL
FORMUL 9 NA 8(NA 1+)
FORMUL 10 GAI 21(C H5 N3)
FORMUL 12 EDO 27(C2 H6 O2)
FORMUL 65 HOH *3398(H2 O)
HELIX 1 1 ASP A 55 PHE A 70 1 16
HELIX 2 2 SER A 74 MET A 79 1 6
HELIX 3 3 ASP A 80 ASP A 98 1 19
HELIX 4 4 ASP A 98 GLY A 111 1 14
HELIX 5 5 PRO A 113 VAL A 120 1 8
HELIX 6 6 VAL A 120 ALA A 136 1 17
HELIX 7 7 PHE A 170 THR A 185 1 16
HELIX 8 8 PRO A 198 GLY A 212 1 15
HELIX 9 9 THR A 227 HIS A 235 1 9
HELIX 10 10 SER A 246 SER A 260 1 15
HELIX 11 11 ASP A 282 PHE A 296 1 15
HELIX 12 12 ASN A 297 GLN A 300 5 4
HELIX 13 13 GLU A 312 ARG A 329 1 18
HELIX 14 14 ASP A 346 GLU A 363 1 18
HELIX 15 15 MET A 393 GLU A 398 1 6
HELIX 16 16 THR A 412 ASN A 422 1 11
HELIX 17 17 ASP A 435 LEU A 446 1 12
HELIX 18 18 GLU A 479 ALA A 484 5 6
HELIX 19 19 ASP B 55 PHE B 70 1 16
HELIX 20 20 SER B 74 MET B 79 1 6
HELIX 21 21 ASP B 80 ASP B 98 1 19
HELIX 22 22 ASP B 98 GLY B 111 1 14
HELIX 23 23 PRO B 113 VAL B 120 1 8
HELIX 24 24 VAL B 120 ALA B 136 1 17
HELIX 25 25 PHE B 170 THR B 185 1 16
HELIX 26 26 PRO B 198 GLY B 212 1 15
HELIX 27 27 THR B 227 HIS B 235 1 9
HELIX 28 28 SER B 246 SER B 260 1 15
HELIX 29 29 ASP B 282 PHE B 296 1 15
HELIX 30 30 ASN B 297 GLN B 300 5 4
HELIX 31 31 GLU B 312 ARG B 329 1 18
HELIX 32 32 ASP B 346 GLU B 363 1 18
HELIX 33 33 MET B 393 GLU B 398 1 6
HELIX 34 34 THR B 412 ASN B 422 1 11
HELIX 35 35 ASP B 435 LEU B 446 1 12
HELIX 36 36 TYR B 468 MET B 470 5 3
HELIX 37 37 GLY B 478 ALA B 484 5 7
HELIX 38 38 ASP C 55 PHE C 70 1 16
HELIX 39 39 SER C 74 MET C 79 1 6
HELIX 40 40 ASP C 80 ASP C 98 1 19
HELIX 41 41 ASP C 98 GLY C 111 1 14
HELIX 42 42 PRO C 113 VAL C 120 1 8
HELIX 43 43 VAL C 120 ALA C 136 1 17
HELIX 44 44 PHE C 170 THR C 185 1 16
HELIX 45 45 PRO C 198 GLY C 212 1 15
HELIX 46 46 THR C 227 HIS C 235 1 9
HELIX 47 47 SER C 246 SER C 259 1 14
HELIX 48 48 ASP C 282 PHE C 296 1 15
HELIX 49 49 ASN C 297 GLN C 300 5 4
HELIX 50 50 GLU C 312 ARG C 329 1 18
HELIX 51 51 ASP C 346 GLY C 364 1 19
HELIX 52 52 MET C 393 GLU C 398 1 6
HELIX 53 53 THR C 412 ASN C 422 1 11
HELIX 54 54 ASP C 435 LEU C 446 1 12
HELIX 55 55 GLY C 478 ALA C 484 5 7
HELIX 56 56 ASP D 55 PHE D 70 1 16
HELIX 57 57 SER D 74 MET D 79 1 6
HELIX 58 58 ASP D 80 ASP D 98 1 19
HELIX 59 59 ASP D 98 GLY D 111 1 14
HELIX 60 60 PRO D 113 VAL D 120 1 8
HELIX 61 61 VAL D 120 ALA D 136 1 17
HELIX 62 62 PHE D 170 THR D 185 1 16
HELIX 63 63 PRO D 198 GLY D 212 1 15
HELIX 64 64 THR D 227 SER D 234 1 8
HELIX 65 65 SER D 246 SER D 260 1 15
HELIX 66 66 ASP D 282 PHE D 296 1 15
HELIX 67 67 ASN D 297 GLN D 300 5 4
HELIX 68 68 GLU D 312 ARG D 329 1 18
HELIX 69 69 ASP D 346 GLU D 363 1 18
HELIX 70 70 MET D 393 GLU D 398 1 6
HELIX 71 71 THR D 412 ASN D 422 1 11
HELIX 72 72 ASP D 435 LEU D 446 1 12
HELIX 73 73 GLY D 478 ALA D 484 5 7
HELIX 74 74 ASP E 55 PHE E 70 1 16
HELIX 75 75 SER E 74 MET E 79 1 6
HELIX 76 76 ASP E 80 ASP E 98 1 19
HELIX 77 77 ASP E 98 GLY E 111 1 14
HELIX 78 78 PRO E 113 VAL E 120 1 8
HELIX 79 79 VAL E 120 ALA E 136 1 17
HELIX 80 80 PHE E 170 THR E 185 1 16
HELIX 81 81 PRO E 198 GLY E 212 1 15
HELIX 82 82 THR E 227 HIS E 235 1 9
HELIX 83 83 SER E 246 SER E 260 1 15
HELIX 84 84 ASP E 282 PHE E 296 1 15
HELIX 85 85 ASN E 297 GLN E 300 5 4
HELIX 86 86 GLU E 312 ARG E 329 1 18
HELIX 87 87 ASP E 346 GLU E 363 1 18
HELIX 88 88 MET E 393 GLU E 398 1 6
HELIX 89 89 THR E 412 ASN E 422 1 11
HELIX 90 90 ASP E 435 LEU E 446 1 12
HELIX 91 91 GLY E 478 ALA E 484 5 7
HELIX 92 92 ASP F 55 PHE F 70 1 16
HELIX 93 93 SER F 74 MET F 79 1 6
HELIX 94 94 ASP F 80 ASP F 98 1 19
HELIX 95 95 ASP F 98 GLY F 111 1 14
HELIX 96 96 PRO F 113 VAL F 120 1 8
HELIX 97 97 VAL F 120 ALA F 136 1 17
HELIX 98 98 PHE F 170 THR F 185 1 16
HELIX 99 99 PRO F 198 GLY F 212 1 15
HELIX 100 100 THR F 227 SER F 234 1 8
HELIX 101 101 SER F 246 SER F 260 1 15
HELIX 102 102 ASP F 282 PHE F 296 1 15
HELIX 103 103 ASN F 297 GLN F 300 5 4
HELIX 104 104 GLU F 312 ARG F 329 1 18
HELIX 105 105 ASP F 346 GLU F 363 1 18
HELIX 106 106 MET F 393 GLU F 398 1 6
HELIX 107 107 THR F 412 ASN F 422 1 11
HELIX 108 108 ASP F 435 LEU F 446 1 12
HELIX 109 109 GLY F 478 ALA F 484 5 7
HELIX 110 110 ASP G 55 PHE G 70 1 16
HELIX 111 111 SER G 74 MET G 79 1 6
HELIX 112 112 ASP G 80 ASP G 98 1 19
HELIX 113 113 ASP G 98 GLY G 111 1 14
HELIX 114 114 PRO G 113 VAL G 120 1 8
HELIX 115 115 VAL G 120 ALA G 136 1 17
HELIX 116 116 PHE G 170 THR G 185 1 16
HELIX 117 117 PRO G 198 GLY G 212 1 15
HELIX 118 118 THR G 227 SER G 234 1 8
HELIX 119 119 SER G 246 SER G 260 1 15
HELIX 120 120 ASP G 282 PHE G 296 1 15
HELIX 121 121 ASN G 297 GLN G 300 5 4
HELIX 122 122 GLU G 312 ARG G 329 1 18
HELIX 123 123 ASP G 346 GLU G 363 1 18
HELIX 124 124 MET G 393 GLU G 398 1 6
HELIX 125 125 THR G 412 ASN G 422 1 11
HELIX 126 126 ASP G 435 LEU G 446 1 12
HELIX 127 127 TYR G 468 MET G 470 5 3
HELIX 128 128 GLY G 478 ALA G 484 5 7
HELIX 129 129 ASP H 55 PHE H 70 1 16
HELIX 130 130 SER H 74 MET H 79 1 6
HELIX 131 131 ASP H 80 ASP H 98 1 19
HELIX 132 132 ASP H 98 GLY H 111 1 14
HELIX 133 133 PRO H 113 VAL H 120 1 8
HELIX 134 134 VAL H 120 ALA H 136 1 17
HELIX 135 135 PHE H 170 THR H 185 1 16
HELIX 136 136 PRO H 198 GLY H 212 1 15
HELIX 137 137 THR H 227 SER H 234 1 8
HELIX 138 138 SER H 246 SER H 260 1 15
HELIX 139 139 ASP H 282 PHE H 296 1 15
HELIX 140 140 ASN H 297 GLN H 300 5 4
HELIX 141 141 GLU H 312 ARG H 329 1 18
HELIX 142 142 ASP H 346 GLU H 363 1 18
HELIX 143 143 MET H 393 GLU H 398 1 6
HELIX 144 144 THR H 412 ASN H 422 1 11
HELIX 145 145 ASP H 435 LEU H 446 1 12
HELIX 146 146 GLY H 478 ALA H 484 5 7
SHEET 1 A 2 ILE A 22 ILE A 24 0
SHEET 2 A 2 GLU A 27 HIS A 29 -1 O HIS A 29 N ILE A 22
SHEET 1 B 2 THR A 36 VAL A 40 0
SHEET 2 B 2 VAL A 47 ALA A 52 -1 O ILE A 48 N THR A 39
SHEET 1 C20 LYS B 366 CYS B 369 0
SHEET 2 C20 THR B 384 GLY B 387 -1 O VAL B 385 N LEU B 368
SHEET 3 C20 VAL B 404 PHE B 410 1 O MET B 405 N PHE B 386
SHEET 4 C20 ARG B 307 GLN B 311 1 N VAL B 310 O LEU B 408
SHEET 5 C20 PRO B 274 ILE B 277 1 N ILE B 277 O PHE B 309
SHEET 6 C20 ALA B 428 PHE B 432 1 O ALA B 430 N ILE B 276
SHEET 7 C20 THR B 450 VAL B 453 1 O TRP B 452 N ALA B 429
SHEET 8 C20 THR A 486 LYS A 494 1 N THR A 490 O VAL B 451
SHEET 9 C20 PHE A 150 PRO A 158 -1 N PHE A 151 O VAL A 493
SHEET 10 C20 GLY A 141 ILE A 144 -1 N ILE A 144 O SER A 152
SHEET 11 C20 GLY D 141 ILE D 144 -1 O THR D 143 N GLY A 141
SHEET 12 C20 PHE D 150 PRO D 158 -1 O SER D 152 N ILE D 144
SHEET 13 C20 THR D 486 LYS D 494 -1 O VAL D 493 N PHE D 151
SHEET 14 C20 THR C 450 VAL C 453 1 N VAL C 451 O THR D 490
SHEET 15 C20 ALA C 428 PHE C 432 1 N ALA C 429 O TRP C 452
SHEET 16 C20 SER C 273 ILE C 277 1 N ILE C 276 O ALA C 430
SHEET 17 C20 GLY C 305 GLN C 311 1 O PHE C 309 N ILE C 277
SHEET 18 C20 VAL C 404 PHE C 410 1 O LEU C 408 N VAL C 310
SHEET 19 C20 THR C 384 GLY C 387 1 N PHE C 386 O MET C 405
SHEET 20 C20 LYS C 366 CYS C 369 -1 N LYS C 366 O GLY C 387
SHEET 1 D 6 VAL A 218 PRO A 222 0
SHEET 2 D 6 VAL A 188 VAL A 193 1 N MET A 191 O VAL A 221
SHEET 3 D 6 VAL A 161 ILE A 165 1 N CYS A 162 O VAL A 188
SHEET 4 D 6 LYS A 240 ALA A 244 1 O LYS A 240 N GLY A 163
SHEET 5 D 6 ARG A 264 GLU A 268 1 O ARG A 264 N VAL A 241
SHEET 6 D 6 GLY A 472 SER A 473 -1 O SER A 473 N LEU A 267
SHEET 1 E20 LYS A 366 CYS A 369 0
SHEET 2 E20 THR A 384 GLY A 387 -1 O GLY A 387 N LYS A 366
SHEET 3 E20 VAL A 404 PHE A 410 1 O MET A 405 N PHE A 386
SHEET 4 E20 GLY A 305 GLN A 311 1 N VAL A 310 O LEU A 408
SHEET 5 E20 SER A 273 ILE A 277 1 N ILE A 277 O PHE A 309
SHEET 6 E20 ALA A 428 PHE A 432 1 O ALA A 430 N ILE A 276
SHEET 7 E20 THR A 450 VAL A 453 1 O TRP A 452 N ALA A 429
SHEET 8 E20 THR B 486 LYS B 494 1 O THR B 490 N VAL A 451
SHEET 9 E20 PHE B 150 PRO B 158 -1 N PHE B 151 O VAL B 493
SHEET 10 E20 GLY B 141 ILE B 144 -1 N ILE B 144 O SER B 152
SHEET 11 E20 GLY C 141 ILE C 144 -1 O GLY C 141 N THR B 143
SHEET 12 E20 PHE C 150 PRO C 158 -1 O SER C 152 N ILE C 144
SHEET 13 E20 THR C 486 LYS C 494 -1 O VAL C 493 N PHE C 151
SHEET 14 E20 THR D 450 VAL D 453 1 O VAL D 451 N THR C 490
SHEET 15 E20 ALA D 428 PHE D 432 1 N ALA D 429 O TRP D 452
SHEET 16 E20 SER D 273 ILE D 277 1 N ILE D 276 O ALA D 430
SHEET 17 E20 GLY D 305 GLN D 311 1 O PHE D 309 N ILE D 277
SHEET 18 E20 VAL D 404 PHE D 410 1 O LEU D 408 N VAL D 310
SHEET 19 E20 THR D 384 GLY D 387 1 N PHE D 386 O MET D 405
SHEET 20 E20 LYS D 366 CYS D 369 -1 N LEU D 368 O VAL D 385
SHEET 1 F 2 TYR A 425 GLY A 426 0
SHEET 2 F 2 TYR A 468 LYS A 469 -1 N TYR A 468 O GLY A 426
SHEET 1 G 2 ILE B 22 ILE B 24 0
SHEET 2 G 2 GLU B 27 HIS B 29 -1 O HIS B 29 N ILE B 22
SHEET 1 H 2 THR B 36 VAL B 40 0
SHEET 2 H 2 VAL B 47 ALA B 52 -1 O ILE B 48 N THR B 39
SHEET 1 I 6 VAL B 218 ILE B 220 0
SHEET 2 I 6 VAL B 188 LYS B 192 1 N MET B 191 O ASN B 219
SHEET 3 I 6 VAL B 161 ILE B 165 1 N CYS B 162 O VAL B 188
SHEET 4 I 6 LYS B 240 ALA B 244 1 O LYS B 240 N GLY B 163
SHEET 5 I 6 ARG B 264 GLU B 268 1 O ARG B 264 N VAL B 241
SHEET 6 I 6 GLY B 472 SER B 473 -1 O SER B 473 N LEU B 267
SHEET 1 J 2 ILE C 22 ILE C 24 0
SHEET 2 J 2 GLU C 27 HIS C 29 -1 O HIS C 29 N ILE C 22
SHEET 1 K 2 THR C 36 VAL C 40 0
SHEET 2 K 2 VAL C 47 ALA C 52 -1 O ILE C 48 N THR C 39
SHEET 1 L 6 VAL C 218 ILE C 220 0
SHEET 2 L 6 VAL C 188 LYS C 192 1 N MET C 191 O ASN C 219
SHEET 3 L 6 VAL C 161 ILE C 165 1 N CYS C 162 O VAL C 188
SHEET 4 L 6 LYS C 240 ALA C 244 1 O LYS C 240 N GLY C 163
SHEET 5 L 6 ARG C 264 GLU C 268 1 O ARG C 264 N VAL C 241
SHEET 6 L 6 GLY C 472 SER C 473 -1 O SER C 473 N LEU C 267
SHEET 1 M 2 TYR C 425 GLY C 426 0
SHEET 2 M 2 TYR C 468 LYS C 469 -1 O TYR C 468 N GLY C 426
SHEET 1 N 2 ILE D 22 ILE D 24 0
SHEET 2 N 2 GLU D 27 HIS D 29 -1 O HIS D 29 N ILE D 22
SHEET 1 O 2 THR D 36 VAL D 40 0
SHEET 2 O 2 VAL D 47 ALA D 52 -1 O ILE D 48 N THR D 39
SHEET 1 P 6 VAL D 218 ILE D 220 0
SHEET 2 P 6 VAL D 188 LYS D 192 1 N MET D 191 O ASN D 219
SHEET 3 P 6 VAL D 161 ILE D 165 1 N CYS D 162 O VAL D 188
SHEET 4 P 6 LYS D 240 ALA D 244 1 O LYS D 240 N GLY D 163
SHEET 5 P 6 ARG D 264 GLU D 268 1 O ARG D 264 N VAL D 241
SHEET 6 P 6 GLY D 472 SER D 473 -1 O SER D 473 N LEU D 267
SHEET 1 Q 2 TYR D 425 GLY D 426 0
SHEET 2 Q 2 TYR D 468 LYS D 469 -1 O TYR D 468 N GLY D 426
SHEET 1 R 2 ILE E 22 ILE E 24 0
SHEET 2 R 2 GLU E 27 HIS E 29 -1 O HIS E 29 N ILE E 22
SHEET 1 S 2 THR E 36 VAL E 40 0
SHEET 2 S 2 VAL E 47 ALA E 52 -1 O ILE E 48 N THR E 39
SHEET 1 T20 LYS F 366 CYS F 369 0
SHEET 2 T20 THR F 384 GLY F 387 -1 O VAL F 385 N LEU F 368
SHEET 3 T20 VAL F 404 PHE F 410 1 O MET F 405 N PHE F 386
SHEET 4 T20 ARG F 307 GLN F 311 1 N VAL F 310 O LEU F 408
SHEET 5 T20 PRO F 274 ILE F 277 1 N ILE F 277 O PHE F 309
SHEET 6 T20 ALA F 428 PHE F 432 1 O ALA F 430 N ILE F 276
SHEET 7 T20 THR F 450 VAL F 453 1 O TRP F 452 N ALA F 429
SHEET 8 T20 THR E 486 LYS E 494 1 N THR E 490 O VAL F 451
SHEET 9 T20 PHE E 150 PRO E 158 -1 N PHE E 151 O VAL E 493
SHEET 10 T20 GLY E 141 ILE E 144 -1 N ILE E 144 O SER E 152
SHEET 11 T20 GLY H 141 ILE H 144 -1 O GLY H 141 N THR E 143
SHEET 12 T20 PHE H 150 PRO H 158 -1 O SER H 152 N ILE H 144
SHEET 13 T20 THR H 486 LYS H 494 -1 O VAL H 493 N PHE H 151
SHEET 14 T20 THR G 450 VAL G 453 1 N VAL G 451 O THR H 490
SHEET 15 T20 ALA G 428 PHE G 432 1 N ALA G 429 O TRP G 452
SHEET 16 T20 SER G 273 ILE G 277 1 N ILE G 276 O ALA G 430
SHEET 17 T20 GLY G 305 GLN G 311 1 O PHE G 309 N ILE G 277
SHEET 18 T20 VAL G 404 PHE G 410 1 O LEU G 408 N VAL G 310
SHEET 19 T20 THR G 384 GLY G 387 1 N PHE G 386 O MET G 405
SHEET 20 T20 LYS G 366 CYS G 369 -1 N LEU G 368 O VAL G 385
SHEET 1 U 6 VAL E 218 ILE E 220 0
SHEET 2 U 6 VAL E 188 LYS E 192 1 N MET E 191 O ASN E 219
SHEET 3 U 6 VAL E 161 ILE E 165 1 N CYS E 162 O VAL E 188
SHEET 4 U 6 LYS E 240 ALA E 244 1 O LYS E 240 N GLY E 163
SHEET 5 U 6 ARG E 264 GLU E 268 1 O ARG E 264 N VAL E 241
SHEET 6 U 6 GLY E 472 SER E 473 -1 O SER E 473 N LEU E 267
SHEET 1 V20 LYS E 366 CYS E 369 0
SHEET 2 V20 THR E 384 GLY E 387 -1 O VAL E 385 N LEU E 368
SHEET 3 V20 VAL E 404 PHE E 410 1 O MET E 405 N THR E 384
SHEET 4 V20 ARG E 307 GLN E 311 1 N VAL E 310 O LEU E 408
SHEET 5 V20 PRO E 274 ILE E 277 1 N ILE E 277 O PHE E 309
SHEET 6 V20 ALA E 428 PHE E 432 1 O ALA E 430 N ILE E 276
SHEET 7 V20 THR E 450 VAL E 453 1 O TRP E 452 N ALA E 429
SHEET 8 V20 THR F 486 LYS F 494 1 O THR F 490 N VAL E 451
SHEET 9 V20 PHE F 150 PRO F 158 -1 N PHE F 151 O VAL F 493
SHEET 10 V20 GLY F 141 ILE F 144 -1 N ILE F 144 O SER F 152
SHEET 11 V20 GLY G 141 ILE G 144 -1 O GLY G 141 N THR F 143
SHEET 12 V20 PHE G 150 PRO G 158 -1 O SER G 152 N ILE G 144
SHEET 13 V20 THR G 486 LYS G 494 -1 O VAL G 493 N PHE G 151
SHEET 14 V20 THR H 450 VAL H 453 1 O VAL H 451 N THR G 490
SHEET 15 V20 ALA H 428 PHE H 432 1 N ALA H 429 O TRP H 452
SHEET 16 V20 PRO H 274 ILE H 277 1 N ILE H 276 O ALA H 430
SHEET 17 V20 ARG H 307 GLN H 311 1 O PHE H 309 N ILE H 277
SHEET 18 V20 VAL H 404 PHE H 410 1 O LEU H 408 N VAL H 310
SHEET 19 V20 THR H 384 GLY H 387 1 N PHE H 386 O MET H 405
SHEET 20 V20 LYS H 366 CYS H 369 -1 N LEU H 368 O VAL H 385
SHEET 1 W 2 TYR E 425 GLY E 426 0
SHEET 2 W 2 TYR E 468 LYS E 469 -1 O TYR E 468 N GLY E 426
SHEET 1 X 2 ILE F 22 ILE F 24 0
SHEET 2 X 2 GLU F 27 HIS F 29 -1 O HIS F 29 N ILE F 22
SHEET 1 Y 2 THR F 36 VAL F 40 0
SHEET 2 Y 2 VAL F 47 ALA F 52 -1 O ILE F 48 N THR F 39
SHEET 1 Z 6 VAL F 218 ILE F 220 0
SHEET 2 Z 6 VAL F 188 LYS F 192 1 N MET F 191 O ASN F 219
SHEET 3 Z 6 VAL F 161 ILE F 165 1 N CYS F 162 O VAL F 188
SHEET 4 Z 6 LYS F 240 ALA F 244 1 O LYS F 240 N GLY F 163
SHEET 5 Z 6 ARG F 264 GLU F 268 1 O ARG F 264 N VAL F 241
SHEET 6 Z 6 GLY F 472 SER F 473 -1 O SER F 473 N LEU F 267
SHEET 1 AA 2 TYR F 425 GLY F 426 0
SHEET 2 AA 2 TYR F 468 LYS F 469 -1 O TYR F 468 N GLY F 426
SHEET 1 AB 2 ILE G 22 ILE G 24 0
SHEET 2 AB 2 GLU G 27 HIS G 29 -1 O HIS G 29 N ILE G 22
SHEET 1 AC 2 THR G 36 VAL G 40 0
SHEET 2 AC 2 VAL G 47 ALA G 52 -1 O ILE G 48 N THR G 39
SHEET 1 AD 6 VAL G 218 ILE G 220 0
SHEET 2 AD 6 VAL G 188 LYS G 192 1 N MET G 191 O ASN G 219
SHEET 3 AD 6 VAL G 161 ILE G 165 1 N GLN G 164 O LYS G 192
SHEET 4 AD 6 LYS G 240 ALA G 244 1 O LYS G 240 N GLY G 163
SHEET 5 AD 6 ARG G 264 GLU G 268 1 O ARG G 264 N VAL G 241
SHEET 6 AD 6 GLY G 472 SER G 473 -1 O SER G 473 N LEU G 267
SHEET 1 AE 2 ILE H 22 ILE H 24 0
SHEET 2 AE 2 GLU H 27 HIS H 29 -1 O HIS H 29 N ILE H 22
SHEET 1 AF 2 THR H 36 VAL H 40 0
SHEET 2 AF 2 VAL H 47 ALA H 52 -1 O ILE H 48 N THR H 39
SHEET 1 AG 6 VAL H 218 ILE H 220 0
SHEET 2 AG 6 VAL H 188 LYS H 192 1 N MET H 191 O ASN H 219
SHEET 3 AG 6 VAL H 161 ILE H 165 1 N CYS H 162 O VAL H 188
SHEET 4 AG 6 LYS H 240 ALA H 244 1 O LYS H 240 N GLY H 163
SHEET 5 AG 6 ARG H 264 GLU H 268 1 O ARG H 264 N VAL H 241
SHEET 6 AG 6 GLY H 472 SER H 473 -1 O SER H 473 N LEU H 267
SHEET 1 AH 2 TYR H 425 GLY H 426 0
SHEET 2 AH 2 TYR H 468 LYS H 469 -1 O TYR H 468 N GLY H 426
LINK OG1 THR A 39 NA NA A 601 1555 1555 3.01
LINK O VAL A 40 NA NA A 601 1555 1555 2.35
LINK OD1 ASP A 109 NA NA A 601 1555 1555 2.47
LINK O ASP A 109 NA NA A 601 1555 1555 2.55
LINK O GLN A 196 NA NA A 601 1555 1555 2.23
LINK NA NA A 601 O HOH A1923 1555 1555 2.75
LINK NA NA A 601 O HOH A2100 1555 1555 2.31
LINK OG1 THR B 39 NA NA B 602 1555 1555 3.06
LINK O VAL B 40 NA NA B 602 1555 1555 2.45
LINK OD1 ASP B 109 NA NA B 602 1555 1555 2.40
LINK O ASP B 109 NA NA B 602 1555 1555 2.44
LINK O GLN B 196 NA NA B 602 1555 1555 2.28
LINK NA NA B 602 O HOH B2152 1555 1555 2.24
LINK NA NA B 602 O HOH B2756 1555 1555 2.72
LINK OG1 THR C 39 NA NA C 603 1555 1555 3.05
LINK O VAL C 40 NA NA C 603 1555 1555 2.35
LINK O ASP C 109 NA NA C 603 1555 1555 2.45
LINK OD1 ASP C 109 NA NA C 603 1555 1555 2.50
LINK O GLN C 196 NA NA C 603 1555 1555 2.34
LINK NA NA C 603 O HOH C 688 1555 1555 3.10
LINK NA NA C 603 O HOH C1967 1555 1555 2.23
LINK OG1 THR D 39 NA NA D 604 1555 1555 3.13
LINK O VAL D 40 NA NA D 604 1555 1555 2.35
LINK O ASP D 109 NA NA D 604 1555 1555 2.44
LINK OD1 ASP D 109 NA NA D 604 1555 1555 2.50
LINK O GLN D 196 NA NA D 604 1555 1555 2.34
LINK NA NA D 604 O HOH D2487 1555 1555 3.19
LINK NA NA D 604 O HOH D3277 1555 1555 2.28
LINK OG1 THR E 39 NA NA E 605 1555 1555 3.09
LINK O VAL E 40 NA NA E 605 1555 1555 2.34
LINK O ASP E 109 NA NA E 605 1555 1555 2.47
LINK OD1 ASP E 109 NA NA E 605 1555 1555 2.51
LINK O GLN E 196 NA NA E 605 1555 1555 2.30
LINK NA NA E 605 O HOH E1968 1555 1555 2.37
LINK NA NA E 605 O HOH E2044 1555 1555 2.98
LINK OG1 THR F 39 NA NA F 606 1555 1555 2.99
LINK O VAL F 40 NA NA F 606 1555 1555 2.31
LINK OD1 ASP F 109 NA NA F 606 1555 1555 2.40
LINK O ASP F 109 NA NA F 606 1555 1555 2.49
LINK O GLN F 196 NA NA F 606 1555 1555 2.34
LINK NA NA F 606 O HOH F1738 1555 1555 2.35
LINK O VAL G 40 NA NA G 607 1555 1555 2.47
LINK O ASP G 109 NA NA G 607 1555 1555 2.41
LINK OD1 ASP G 109 NA NA G 607 1555 1555 2.45
LINK O GLN G 196 NA NA G 607 1555 1555 2.32
LINK NA NA G 607 O HOH G1886 1555 1555 2.96
LINK NA NA G 607 O HOH G3377 1555 1555 2.20
LINK OG1 THR H 39 NA NA H 608 1555 1555 3.18
LINK O VAL H 40 NA NA H 608 1555 1555 2.42
LINK O ASP H 109 NA NA H 608 1555 1555 2.33
LINK OD1 ASP H 109 NA NA H 608 1555 1555 2.44
LINK O GLN H 196 NA NA H 608 1555 1555 2.36
LINK NA NA H 608 O HOH H2258 1555 1555 2.39
LINK NA NA H 608 O HOH H3346 1555 1555 3.04
SITE 1 AC1 6 THR A 39 VAL A 40 ASP A 109 GLN A 196
SITE 2 AC1 6 HOH A1923 HOH A2100
SITE 1 AC2 6 PHE A 70 GLU A 157 PRO A 158 VAL A 159
SITE 2 AC2 6 HOH A1588 TYR B 468
SITE 1 AC3 8 ILE A 146 ASP A 147 PHE A 150 HOH A1334
SITE 2 AC3 8 HOH A2251 HOH A2614 VAL B 458 PHE B 459
SITE 1 AC4 4 TYR A 153 ARG A 155 SER B 443 PHE D 151
SITE 1 AC5 4 GLN A 14 ASN A 41 THR A 44 LEU A 108
SITE 1 AC6 5 PHE A 18 TYR A 101 TYR A 203 HOH A1300
SITE 2 AC6 5 HOH A3317
SITE 1 AC7 6 TYR A 441 GLN A 444 ALA A 445 HOH A 533
SITE 2 AC7 6 LEU B 72 GLN C 497
SITE 1 AC8 6 THR B 39 VAL B 40 ASP B 109 GLN B 196
SITE 2 AC8 6 HOH B2152 HOH B2756
SITE 1 AC9 5 TYR A 468 PHE B 70 GLU B 157 PRO B 158
SITE 2 AC9 5 VAL B 159
SITE 1 BC1 5 PHE A 459 HOH A1107 ILE B 146 ASP B 147
SITE 2 BC1 5 PHE B 150
SITE 1 BC2 4 SER A 443 TYR B 153 ARG B 155 PHE C 151
SITE 1 BC3 5 GLN B 14 ASN B 41 THR B 44 GLU B 46
SITE 2 BC3 5 HOH B2850
SITE 1 BC4 7 LEU A 72 TYR B 441 GLN B 444 ALA B 445
SITE 2 BC4 7 HOH B 601 HOH B1909 GLN D 497
SITE 1 BC5 6 THR C 39 VAL C 40 ASP C 109 GLN C 196
SITE 2 BC5 6 HOH C 688 HOH C1967
SITE 1 BC6 7 PHE C 70 GLU C 157 PRO C 158 VAL C 159
SITE 2 BC6 7 HOH C 672 HOH C1098 TYR D 468
SITE 1 BC7 5 ILE C 146 ASP C 147 PHE C 150 HOH C2861
SITE 2 BC7 5 PHE D 459
SITE 1 BC8 4 PHE C 350 ALA C 375 ASP C 376 GLY C 378
SITE 1 BC9 4 PHE B 151 TYR C 153 ARG C 155 SER D 443
SITE 1 CC1 5 GLN C 14 ASN C 41 THR C 44 GLU C 46
SITE 2 CC1 5 LEU C 108
SITE 1 CC2 5 PHE C 18 TYR C 101 TYR C 203 HOH C 545
SITE 2 CC2 5 HOH C1875
SITE 1 CC3 6 GLN A 497 HOH A 534 TYR C 441 GLN C 444
SITE 2 CC3 6 ALA C 445 LEU D 72
SITE 1 CC4 5 THR D 39 VAL D 40 ASP D 109 GLN D 196
SITE 2 CC4 5 HOH D3277
SITE 1 CC5 5 TYR C 468 GLU D 157 PRO D 158 VAL D 159
SITE 2 CC5 5 HOH D1435
SITE 1 CC6 6 PHE C 459 ILE D 146 ASP D 147 PHE D 150
SITE 2 CC6 6 HOH D1785 HOH D3364
SITE 1 CC7 5 GLN D 14 PRO D 15 LEU D 108 HOH D2409
SITE 2 CC7 5 HOH H1803
SITE 1 CC8 4 PHE A 151 SER C 443 TYR D 153 ARG D 155
SITE 1 CC9 5 GLU D 414 TYR D 441 HOH D2622 LYS G 361
SITE 2 CC9 5 HOH G1321
SITE 1 DC1 6 THR E 39 VAL E 40 ASP E 109 GLN E 196
SITE 2 DC1 6 HOH E1968 HOH E2044
SITE 1 DC2 5 PHE E 70 GLU E 157 PRO E 158 VAL E 159
SITE 2 DC2 5 TYR F 468
SITE 1 DC3 5 ILE E 146 ASP E 147 PHE E 150 PHE F 459
SITE 2 DC3 5 HOH F1689
SITE 1 DC4 4 TYR E 153 ARG E 155 SER F 443 PHE H 151
SITE 1 DC5 4 GLN E 14 ASN E 41 THR E 44 GLU E 46
SITE 1 DC6 3 TYR E 101 TYR E 203 HOH E2068
SITE 1 DC7 5 THR F 39 VAL F 40 ASP F 109 GLN F 196
SITE 2 DC7 5 HOH F1738
SITE 1 DC8 5 TYR E 468 GLU F 157 PRO F 158 VAL F 159
SITE 2 DC8 5 HOH F 903
SITE 1 DC9 8 VAL E 458 PHE E 459 ILE F 146 ASP F 147
SITE 2 DC9 8 PHE F 150 HOH F 897 HOH F2432 HOH F2524
SITE 1 EC1 6 PHE F 350 ILE F 373 ALA F 375 ASP F 376
SITE 2 EC1 6 GLY F 378 EDO F 966
SITE 1 EC2 7 ALA F 326 LYS F 327 ARG F 329 VAL F 331
SITE 2 EC2 7 PRO F 383 HOH F 840 HOH F1711
SITE 1 EC3 4 SER E 443 TYR F 153 ARG F 155 PHE G 151
SITE 1 EC4 5 GLN F 14 ASN F 41 THR F 44 GLU F 46
SITE 2 EC4 5 LEU F 108
SITE 1 EC5 7 ARG E 321 HOH E 555 PHE F 18 TYR F 101
SITE 2 EC5 7 TYR F 203 HOH F1281 HOH F3315
SITE 1 EC6 6 LEU E 72 TYR F 441 GLN F 444 ALA F 445
SITE 2 EC6 6 HOH F1039 GLN H 497
SITE 1 EC7 5 GLY C 45 HOH C1684 GLU F 347 PHE F 350
SITE 2 EC7 5 GAI F 826
SITE 1 EC8 6 THR G 39 VAL G 40 ASP G 109 GLN G 196
SITE 2 EC8 6 HOH G1886 HOH G3377
SITE 1 EC9 7 PHE G 70 GLU G 157 PRO G 158 VAL G 159
SITE 2 EC9 7 HOH G 614 HOH G1596 TYR H 468
SITE 1 FC1 7 ILE G 146 ASP G 147 PHE G 150 HOH G1511
SITE 2 FC1 7 HOH G2035 VAL H 458 PHE H 459
SITE 1 FC2 6 ALA G 326 LYS G 327 ARG G 329 PRO G 383
SITE 2 FC2 6 HOH G 675 HOH G2722
SITE 1 FC3 4 PHE F 151 TYR G 153 ARG G 155 SER H 443
SITE 1 FC4 3 ASN G 41 THR G 44 GLU G 46
SITE 1 FC5 4 PHE G 18 TYR G 101 TYR G 203 HOH G1853
SITE 1 FC6 6 THR H 39 VAL H 40 ASP H 109 GLN H 196
SITE 2 FC6 6 HOH H2258 HOH H3346
SITE 1 FC7 3 GLU H 157 PRO H 158 VAL H 159
SITE 1 FC8 5 PHE G 459 HOH G 997 ILE H 146 ASP H 147
SITE 2 FC8 5 PHE H 150
SITE 1 FC9 4 PHE E 151 SER G 443 TYR H 153 ARG H 155
SITE 1 GC1 4 LYS E 361 PHE H 18 TYR H 101 TYR H 203
SITE 1 GC2 7 GLN F 497 LEU G 72 TYR H 441 GLN H 444
SITE 2 GC2 7 ALA H 445 HOH H 972 HOH H 981
CRYST1 141.750 152.194 177.292 90.00 90.00 90.00 P 21 21 21 32
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 0.007055 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006571 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005640 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
