7yc4-pdb | HEADER HYDROLASE 30-JUN-22 7YC4
TITLE ACETYLESTERASE (LGESTI) F207A
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ALPHA/BETA HYDROLASE;
COMPND 3 CHAIN: A, B, C, D, E, F, G, H;
COMPND 4 ENGINEERED: YES;
COMPND 5 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: LACTOCOCCUS GARVIEAE SUBSP. GARVIEAE;
SOURCE 3 ORGANISM_TAXID: 1890280;
SOURCE 4 GENE: F4V47_03290;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS ESTERASE, LIPASE, HYDROLASE, PATHOGEN BACTERIA
EXPDTA X-RAY DIFFRACTION
AUTHOR H.DO,J.H.LEE
REVDAT 1 07-JUN-23 7YC4 0
JRNL AUTH H.DO,W.YOO,Y.WANG,Y.NAM,S.C.SHIN,H.W.KIM,K.K.KIM,J.H.LEE
JRNL TITL CRYSTAL STRUCTURE AND BIOCHEMICAL ANALYSIS OF ACETYLESTERASE
JRNL TITL 2 (LGESTI) FROM LACTOCOCCUS GARVIEAE.
JRNL REF PLOS ONE V. 18 80988 2023
JRNL REFN ESSN 1932-6203
JRNL PMID 36745644
JRNL DOI 10.1371/JOURNAL.PONE.0280988
REMARK 2
REMARK 2 RESOLUTION. 2.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0267
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.37
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 151386
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : FREE R-VALUE
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING + TEST SET) : NULL
REMARK 3 R VALUE (WORKING SET) : 0.192
REMARK 3 FREE R VALUE : 0.245
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.008
REMARK 3 FREE R VALUE TEST SET COUNT : 7581
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.10
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.16
REMARK 3 REFLECTION IN BIN (WORKING SET) : 10604
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 BIN R VALUE (WORKING SET) : 0.2570
REMARK 3 BIN FREE R VALUE SET COUNT : 566
REMARK 3 BIN FREE R VALUE : 0.3130
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 20140
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 577
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 36.44
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.01500
REMARK 3 B22 (A**2) : 0.01000
REMARK 3 B33 (A**2) : 0.00500
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00100
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.239
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.199
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.156
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.972
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.954
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.923
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 20556 ; 0.008 ; 0.013
REMARK 3 BOND LENGTHS OTHERS (A): 19145 ; 0.001 ; 0.017
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 27917 ; 1.538 ; 1.642
REMARK 3 BOND ANGLES OTHERS (DEGREES): 44008 ; 1.281 ; 1.579
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 2511 ; 7.410 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 1198 ;34.714 ;23.255
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 3488 ;15.884 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 128 ;18.890 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 2703 ; 0.073 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 23593 ; 0.007 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 4775 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 4435 ; 0.199 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 96 ; 0.253 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 9846 ; 0.160 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 883 ; 0.159 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 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): 10068 ; 2.657 ; 3.724
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 10067 ; 2.657 ; 3.723
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 12571 ; 3.605 ; 5.573
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 12572 ; 3.606 ; 5.573
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 10488 ; 3.050 ; 4.044
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 10489 ; 3.051 ; 4.044
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 15346 ; 4.584 ; 5.955
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 15347 ; 4.584 ; 5.955
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 BULK SOLVENT
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 THEIR
REMARK 3 RIDING POSITIONS
REMARK 4
REMARK 4 7YC4 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 12-JUL-22.
REMARK 100 THE DEPOSITION ID IS D_1300030631.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 08-APR-21
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PAL/PLS
REMARK 200 BEAMLINE : 5C (4A)
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 9M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 151387
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100
REMARK 200 RESOLUTION RANGE LOW (A) : 29.365
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 6.700
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 10.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.14
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.71200
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 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: MOLREP
REMARK 200 STARTING MODEL: 7YC0
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 46.89
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.32
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M POTASSIUM FORMATE, PH 7.3, 20%
REMARK 280 (W/V) PEG 3350, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 63.69500
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, G
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: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, 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 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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: 4
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 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 -2
REMARK 465 SER A -1
REMARK 465 HIS A 0
REMARK 465 MET A 1
REMARK 465 LYS A 317
REMARK 465 GLY B -2
REMARK 465 SER B -1
REMARK 465 HIS B 0
REMARK 465 MET B 1
REMARK 465 GLY C -2
REMARK 465 SER C -1
REMARK 465 HIS C 0
REMARK 465 MET C 1
REMARK 465 VAL C 2
REMARK 465 GLU C 3
REMARK 465 GLY D -2
REMARK 465 SER D -1
REMARK 465 HIS D 0
REMARK 465 MET D 1
REMARK 465 VAL D 2
REMARK 465 GLU D 3
REMARK 465 LYS D 317
REMARK 465 GLY E -2
REMARK 465 SER E -1
REMARK 465 HIS E 0
REMARK 465 LYS E 317
REMARK 465 GLY F -2
REMARK 465 SER F -1
REMARK 465 HIS F 0
REMARK 465 MET F 1
REMARK 465 LYS F 317
REMARK 465 GLY G -2
REMARK 465 SER G -1
REMARK 465 HIS G 0
REMARK 465 MET G 1
REMARK 465 GLY H -2
REMARK 465 SER H -1
REMARK 465 HIS H 0
REMARK 465 MET H 1
REMARK 465 VAL H 2
REMARK 465 LYS H 317
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 OG1 THR A 221 OE1 GLU A 226 2.11
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 ALA A 87 36.28 92.07
REMARK 500 TRP A 89 -9.65 80.34
REMARK 500 ASN A 93 -178.85 -179.95
REMARK 500 HIS A 152 75.78 -114.18
REMARK 500 SER A 159 -119.59 59.75
REMARK 500 TYR A 187 61.32 39.68
REMARK 500 ALA A 192 44.60 -100.23
REMARK 500 ASN A 205 8.40 87.07
REMARK 500 ALA A 207 -78.49 69.80
REMARK 500 ALA A 232 -51.95 -122.50
REMARK 500 ALA A 255 65.46 -100.08
REMARK 500 LYS B 76 150.99 -47.96
REMARK 500 ALA B 87 34.12 96.61
REMARK 500 TRP B 89 -9.92 76.28
REMARK 500 ASN B 93 -176.37 -174.94
REMARK 500 ASN B 109 61.32 39.52
REMARK 500 HIS B 152 63.88 -111.43
REMARK 500 SER B 159 -120.07 62.35
REMARK 500 GLN B 178 131.99 -38.84
REMARK 500 TYR B 187 62.59 35.30
REMARK 500 ALA B 192 47.88 -78.97
REMARK 500 ASN B 205 1.27 86.85
REMARK 500 ALA B 207 -84.18 71.93
REMARK 500 THR B 221 122.42 -178.59
REMARK 500 SER B 223 99.17 -61.26
REMARK 500 ALA B 255 63.09 -103.30
REMARK 500 ARG B 316 -69.66 -95.60
REMARK 500 ALA C 87 35.32 87.87
REMARK 500 TRP C 89 -16.39 76.92
REMARK 500 PRO C 126 44.15 -100.48
REMARK 500 HIS C 152 65.41 -119.64
REMARK 500 SER C 159 -112.07 64.76
REMARK 500 TYR C 187 63.53 38.70
REMARK 500 ALA C 192 45.35 -84.58
REMARK 500 ASN C 205 -0.65 91.63
REMARK 500 ALA C 207 -74.98 45.63
REMARK 500 THR C 221 132.53 -173.62
REMARK 500 ALA C 247 136.78 -39.32
REMARK 500 HIS D 73 61.52 38.50
REMARK 500 ALA D 87 44.16 90.20
REMARK 500 TRP D 89 -8.72 78.06
REMARK 500 TYR D 125 133.09 -29.75
REMARK 500 SER D 159 -118.75 67.85
REMARK 500 TYR D 187 68.40 35.60
REMARK 500 ALA D 192 37.53 -83.35
REMARK 500 ASN D 205 19.12 84.29
REMARK 500 ALA D 207 -78.56 53.24
REMARK 500 SER D 223 98.63 -65.62
REMARK 500 ALA D 247 133.30 -34.97
REMARK 500 ALA D 255 68.01 -100.74
REMARK 500
REMARK 500 THIS ENTRY HAS 90 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 7YC0 RELATED DB: PDB
REMARK 900 7YC0 IS THE WILD TYPE
DBREF1 7YC4 A 1 317 UNP A0A5M9R5N4_9LACT
DBREF2 7YC4 A A0A5M9R5N4 1 317
DBREF1 7YC4 B 1 317 UNP A0A5M9R5N4_9LACT
DBREF2 7YC4 B A0A5M9R5N4 1 317
DBREF1 7YC4 C 1 317 UNP A0A5M9R5N4_9LACT
DBREF2 7YC4 C A0A5M9R5N4 1 317
DBREF1 7YC4 D 1 317 UNP A0A5M9R5N4_9LACT
DBREF2 7YC4 D A0A5M9R5N4 1 317
DBREF1 7YC4 E 1 317 UNP A0A5M9R5N4_9LACT
DBREF2 7YC4 E A0A5M9R5N4 1 317
DBREF1 7YC4 F 1 317 UNP A0A5M9R5N4_9LACT
DBREF2 7YC4 F A0A5M9R5N4 1 317
DBREF1 7YC4 G 1 317 UNP A0A5M9R5N4_9LACT
DBREF2 7YC4 G A0A5M9R5N4 1 317
DBREF1 7YC4 H 1 317 UNP A0A5M9R5N4_9LACT
DBREF2 7YC4 H A0A5M9R5N4 1 317
SEQADV 7YC4 GLY A -2 UNP A0A5M9R5N EXPRESSION TAG
SEQADV 7YC4 SER A -1 UNP A0A5M9R5N EXPRESSION TAG
SEQADV 7YC4 HIS A 0 UNP A0A5M9R5N EXPRESSION TAG
SEQADV 7YC4 ALA A 207 UNP A0A5M9R5N PHE 207 ENGINEERED MUTATION
SEQADV 7YC4 GLY B -2 UNP A0A5M9R5N EXPRESSION TAG
SEQADV 7YC4 SER B -1 UNP A0A5M9R5N EXPRESSION TAG
SEQADV 7YC4 HIS B 0 UNP A0A5M9R5N EXPRESSION TAG
SEQADV 7YC4 ALA B 207 UNP A0A5M9R5N PHE 207 ENGINEERED MUTATION
SEQADV 7YC4 GLY C -2 UNP A0A5M9R5N EXPRESSION TAG
SEQADV 7YC4 SER C -1 UNP A0A5M9R5N EXPRESSION TAG
SEQADV 7YC4 HIS C 0 UNP A0A5M9R5N EXPRESSION TAG
SEQADV 7YC4 ALA C 207 UNP A0A5M9R5N PHE 207 ENGINEERED MUTATION
SEQADV 7YC4 GLY D -2 UNP A0A5M9R5N EXPRESSION TAG
SEQADV 7YC4 SER D -1 UNP A0A5M9R5N EXPRESSION TAG
SEQADV 7YC4 HIS D 0 UNP A0A5M9R5N EXPRESSION TAG
SEQADV 7YC4 ALA D 207 UNP A0A5M9R5N PHE 207 ENGINEERED MUTATION
SEQADV 7YC4 GLY E -2 UNP A0A5M9R5N EXPRESSION TAG
SEQADV 7YC4 SER E -1 UNP A0A5M9R5N EXPRESSION TAG
SEQADV 7YC4 HIS E 0 UNP A0A5M9R5N EXPRESSION TAG
SEQADV 7YC4 ALA E 207 UNP A0A5M9R5N PHE 207 ENGINEERED MUTATION
SEQADV 7YC4 GLY F -2 UNP A0A5M9R5N EXPRESSION TAG
SEQADV 7YC4 SER F -1 UNP A0A5M9R5N EXPRESSION TAG
SEQADV 7YC4 HIS F 0 UNP A0A5M9R5N EXPRESSION TAG
SEQADV 7YC4 ALA F 207 UNP A0A5M9R5N PHE 207 ENGINEERED MUTATION
SEQADV 7YC4 GLY G -2 UNP A0A5M9R5N EXPRESSION TAG
SEQADV 7YC4 SER G -1 UNP A0A5M9R5N EXPRESSION TAG
SEQADV 7YC4 HIS G 0 UNP A0A5M9R5N EXPRESSION TAG
SEQADV 7YC4 ALA G 207 UNP A0A5M9R5N PHE 207 ENGINEERED MUTATION
SEQADV 7YC4 GLY H -2 UNP A0A5M9R5N EXPRESSION TAG
SEQADV 7YC4 SER H -1 UNP A0A5M9R5N EXPRESSION TAG
SEQADV 7YC4 HIS H 0 UNP A0A5M9R5N EXPRESSION TAG
SEQADV 7YC4 ALA H 207 UNP A0A5M9R5N PHE 207 ENGINEERED MUTATION
SEQRES 1 A 320 GLY SER HIS MET VAL GLU ARG ILE SER LEU GLU LYS ALA
SEQRES 2 A 320 ALA LEU GLU PHE SER GLU ALA ASN ALA PRO HIS PRO ARG
SEQRES 3 A 320 ILE TYR GLU LEU PRO VAL GLU GLU GLY ARG SER LEU LEU
SEQRES 4 A 320 ASN GLU VAL GLN ASP SER PRO VAL VAL LYS GLU ASP VAL
SEQRES 5 A 320 ASP ILE GLU ASP ILE ALA VAL ASP THR GLY GLU TRP GLY
SEQRES 6 A 320 GLU ILE ASN VAL ARG PHE ILE ARG PRO LEU HIS GLN GLU
SEQRES 7 A 320 LYS LYS LEU PRO VAL ILE PHE TYR ILE HIS GLY ALA GLY
SEQRES 8 A 320 TRP VAL PHE GLY ASN ALA HIS THR HIS ASP LYS LEU ILE
SEQRES 9 A 320 ARG GLU LEU ALA VAL ARG THR ASN SER VAL VAL VAL PHE
SEQRES 10 A 320 SER GLU TYR SER LEU SER PRO GLU ALA LYS TYR PRO THR
SEQRES 11 A 320 ALA ILE GLU GLN ASN TYR ALA VAL LEU GLN GLN LEU LYS
SEQRES 12 A 320 ASP PHE ALA ASN ASP LYS LYS PHE ASP VAL ASN HIS LEU
SEQRES 13 A 320 THR VAL ALA GLY ASP SER VAL GLY GLY ASN MET ALA THR
SEQRES 14 A 320 VAL MET THR LEU LEU THR LYS GLN ARG GLY GLY GLN LYS
SEQRES 15 A 320 ILE GLY GLN GLN VAL LEU TYR TYR PRO VAL THR ASP ALA
SEQRES 16 A 320 ASN PHE ASP THR ASP SER TYR ASN GLU PHE ALA GLU ASN
SEQRES 17 A 320 TYR ALA LEU THR LYS GLU GLY MET ILE TRP PHE TRP ASP
SEQRES 18 A 320 GLN TYR THR THR SER GLN GLU GLU ARG HIS GLN ILE THR
SEQRES 19 A 320 ALA SER PRO LEU ARG ALA THR LYS GLU ASP LEU ALA ASP
SEQRES 20 A 320 LEU PRO ALA ALA LEU ILE ILE THR GLY GLU ALA ASP VAL
SEQRES 21 A 320 LEU ARG ASP GLU GLY GLU ALA TYR ALA ARG LYS LEU ARG
SEQRES 22 A 320 GLU ALA ASP VAL GLU VAL THR GLN VAL ARG PHE GLN ALA
SEQRES 23 A 320 ILE ILE HIS ASP PHE VAL MET VAL ASN SER MET ASN GLU
SEQRES 24 A 320 THR HIS ALA THR ARG ALA ALA MET SER LEU SER THR GLN
SEQRES 25 A 320 TRP ILE ASN GLU LYS ASN ARG LYS
SEQRES 1 B 320 GLY SER HIS MET VAL GLU ARG ILE SER LEU GLU LYS ALA
SEQRES 2 B 320 ALA LEU GLU PHE SER GLU ALA ASN ALA PRO HIS PRO ARG
SEQRES 3 B 320 ILE TYR GLU LEU PRO VAL GLU GLU GLY ARG SER LEU LEU
SEQRES 4 B 320 ASN GLU VAL GLN ASP SER PRO VAL VAL LYS GLU ASP VAL
SEQRES 5 B 320 ASP ILE GLU ASP ILE ALA VAL ASP THR GLY GLU TRP GLY
SEQRES 6 B 320 GLU ILE ASN VAL ARG PHE ILE ARG PRO LEU HIS GLN GLU
SEQRES 7 B 320 LYS LYS LEU PRO VAL ILE PHE TYR ILE HIS GLY ALA GLY
SEQRES 8 B 320 TRP VAL PHE GLY ASN ALA HIS THR HIS ASP LYS LEU ILE
SEQRES 9 B 320 ARG GLU LEU ALA VAL ARG THR ASN SER VAL VAL VAL PHE
SEQRES 10 B 320 SER GLU TYR SER LEU SER PRO GLU ALA LYS TYR PRO THR
SEQRES 11 B 320 ALA ILE GLU GLN ASN TYR ALA VAL LEU GLN GLN LEU LYS
SEQRES 12 B 320 ASP PHE ALA ASN ASP LYS LYS PHE ASP VAL ASN HIS LEU
SEQRES 13 B 320 THR VAL ALA GLY ASP SER VAL GLY GLY ASN MET ALA THR
SEQRES 14 B 320 VAL MET THR LEU LEU THR LYS GLN ARG GLY GLY GLN LYS
SEQRES 15 B 320 ILE GLY GLN GLN VAL LEU TYR TYR PRO VAL THR ASP ALA
SEQRES 16 B 320 ASN PHE ASP THR ASP SER TYR ASN GLU PHE ALA GLU ASN
SEQRES 17 B 320 TYR ALA LEU THR LYS GLU GLY MET ILE TRP PHE TRP ASP
SEQRES 18 B 320 GLN TYR THR THR SER GLN GLU GLU ARG HIS GLN ILE THR
SEQRES 19 B 320 ALA SER PRO LEU ARG ALA THR LYS GLU ASP LEU ALA ASP
SEQRES 20 B 320 LEU PRO ALA ALA LEU ILE ILE THR GLY GLU ALA ASP VAL
SEQRES 21 B 320 LEU ARG ASP GLU GLY GLU ALA TYR ALA ARG LYS LEU ARG
SEQRES 22 B 320 GLU ALA ASP VAL GLU VAL THR GLN VAL ARG PHE GLN ALA
SEQRES 23 B 320 ILE ILE HIS ASP PHE VAL MET VAL ASN SER MET ASN GLU
SEQRES 24 B 320 THR HIS ALA THR ARG ALA ALA MET SER LEU SER THR GLN
SEQRES 25 B 320 TRP ILE ASN GLU LYS ASN ARG LYS
SEQRES 1 C 320 GLY SER HIS MET VAL GLU ARG ILE SER LEU GLU LYS ALA
SEQRES 2 C 320 ALA LEU GLU PHE SER GLU ALA ASN ALA PRO HIS PRO ARG
SEQRES 3 C 320 ILE TYR GLU LEU PRO VAL GLU GLU GLY ARG SER LEU LEU
SEQRES 4 C 320 ASN GLU VAL GLN ASP SER PRO VAL VAL LYS GLU ASP VAL
SEQRES 5 C 320 ASP ILE GLU ASP ILE ALA VAL ASP THR GLY GLU TRP GLY
SEQRES 6 C 320 GLU ILE ASN VAL ARG PHE ILE ARG PRO LEU HIS GLN GLU
SEQRES 7 C 320 LYS LYS LEU PRO VAL ILE PHE TYR ILE HIS GLY ALA GLY
SEQRES 8 C 320 TRP VAL PHE GLY ASN ALA HIS THR HIS ASP LYS LEU ILE
SEQRES 9 C 320 ARG GLU LEU ALA VAL ARG THR ASN SER VAL VAL VAL PHE
SEQRES 10 C 320 SER GLU TYR SER LEU SER PRO GLU ALA LYS TYR PRO THR
SEQRES 11 C 320 ALA ILE GLU GLN ASN TYR ALA VAL LEU GLN GLN LEU LYS
SEQRES 12 C 320 ASP PHE ALA ASN ASP LYS LYS PHE ASP VAL ASN HIS LEU
SEQRES 13 C 320 THR VAL ALA GLY ASP SER VAL GLY GLY ASN MET ALA THR
SEQRES 14 C 320 VAL MET THR LEU LEU THR LYS GLN ARG GLY GLY GLN LYS
SEQRES 15 C 320 ILE GLY GLN GLN VAL LEU TYR TYR PRO VAL THR ASP ALA
SEQRES 16 C 320 ASN PHE ASP THR ASP SER TYR ASN GLU PHE ALA GLU ASN
SEQRES 17 C 320 TYR ALA LEU THR LYS GLU GLY MET ILE TRP PHE TRP ASP
SEQRES 18 C 320 GLN TYR THR THR SER GLN GLU GLU ARG HIS GLN ILE THR
SEQRES 19 C 320 ALA SER PRO LEU ARG ALA THR LYS GLU ASP LEU ALA ASP
SEQRES 20 C 320 LEU PRO ALA ALA LEU ILE ILE THR GLY GLU ALA ASP VAL
SEQRES 21 C 320 LEU ARG ASP GLU GLY GLU ALA TYR ALA ARG LYS LEU ARG
SEQRES 22 C 320 GLU ALA ASP VAL GLU VAL THR GLN VAL ARG PHE GLN ALA
SEQRES 23 C 320 ILE ILE HIS ASP PHE VAL MET VAL ASN SER MET ASN GLU
SEQRES 24 C 320 THR HIS ALA THR ARG ALA ALA MET SER LEU SER THR GLN
SEQRES 25 C 320 TRP ILE ASN GLU LYS ASN ARG LYS
SEQRES 1 D 320 GLY SER HIS MET VAL GLU ARG ILE SER LEU GLU LYS ALA
SEQRES 2 D 320 ALA LEU GLU PHE SER GLU ALA ASN ALA PRO HIS PRO ARG
SEQRES 3 D 320 ILE TYR GLU LEU PRO VAL GLU GLU GLY ARG SER LEU LEU
SEQRES 4 D 320 ASN GLU VAL GLN ASP SER PRO VAL VAL LYS GLU ASP VAL
SEQRES 5 D 320 ASP ILE GLU ASP ILE ALA VAL ASP THR GLY GLU TRP GLY
SEQRES 6 D 320 GLU ILE ASN VAL ARG PHE ILE ARG PRO LEU HIS GLN GLU
SEQRES 7 D 320 LYS LYS LEU PRO VAL ILE PHE TYR ILE HIS GLY ALA GLY
SEQRES 8 D 320 TRP VAL PHE GLY ASN ALA HIS THR HIS ASP LYS LEU ILE
SEQRES 9 D 320 ARG GLU LEU ALA VAL ARG THR ASN SER VAL VAL VAL PHE
SEQRES 10 D 320 SER GLU TYR SER LEU SER PRO GLU ALA LYS TYR PRO THR
SEQRES 11 D 320 ALA ILE GLU GLN ASN TYR ALA VAL LEU GLN GLN LEU LYS
SEQRES 12 D 320 ASP PHE ALA ASN ASP LYS LYS PHE ASP VAL ASN HIS LEU
SEQRES 13 D 320 THR VAL ALA GLY ASP SER VAL GLY GLY ASN MET ALA THR
SEQRES 14 D 320 VAL MET THR LEU LEU THR LYS GLN ARG GLY GLY GLN LYS
SEQRES 15 D 320 ILE GLY GLN GLN VAL LEU TYR TYR PRO VAL THR ASP ALA
SEQRES 16 D 320 ASN PHE ASP THR ASP SER TYR ASN GLU PHE ALA GLU ASN
SEQRES 17 D 320 TYR ALA LEU THR LYS GLU GLY MET ILE TRP PHE TRP ASP
SEQRES 18 D 320 GLN TYR THR THR SER GLN GLU GLU ARG HIS GLN ILE THR
SEQRES 19 D 320 ALA SER PRO LEU ARG ALA THR LYS GLU ASP LEU ALA ASP
SEQRES 20 D 320 LEU PRO ALA ALA LEU ILE ILE THR GLY GLU ALA ASP VAL
SEQRES 21 D 320 LEU ARG ASP GLU GLY GLU ALA TYR ALA ARG LYS LEU ARG
SEQRES 22 D 320 GLU ALA ASP VAL GLU VAL THR GLN VAL ARG PHE GLN ALA
SEQRES 23 D 320 ILE ILE HIS ASP PHE VAL MET VAL ASN SER MET ASN GLU
SEQRES 24 D 320 THR HIS ALA THR ARG ALA ALA MET SER LEU SER THR GLN
SEQRES 25 D 320 TRP ILE ASN GLU LYS ASN ARG LYS
SEQRES 1 E 320 GLY SER HIS MET VAL GLU ARG ILE SER LEU GLU LYS ALA
SEQRES 2 E 320 ALA LEU GLU PHE SER GLU ALA ASN ALA PRO HIS PRO ARG
SEQRES 3 E 320 ILE TYR GLU LEU PRO VAL GLU GLU GLY ARG SER LEU LEU
SEQRES 4 E 320 ASN GLU VAL GLN ASP SER PRO VAL VAL LYS GLU ASP VAL
SEQRES 5 E 320 ASP ILE GLU ASP ILE ALA VAL ASP THR GLY GLU TRP GLY
SEQRES 6 E 320 GLU ILE ASN VAL ARG PHE ILE ARG PRO LEU HIS GLN GLU
SEQRES 7 E 320 LYS LYS LEU PRO VAL ILE PHE TYR ILE HIS GLY ALA GLY
SEQRES 8 E 320 TRP VAL PHE GLY ASN ALA HIS THR HIS ASP LYS LEU ILE
SEQRES 9 E 320 ARG GLU LEU ALA VAL ARG THR ASN SER VAL VAL VAL PHE
SEQRES 10 E 320 SER GLU TYR SER LEU SER PRO GLU ALA LYS TYR PRO THR
SEQRES 11 E 320 ALA ILE GLU GLN ASN TYR ALA VAL LEU GLN GLN LEU LYS
SEQRES 12 E 320 ASP PHE ALA ASN ASP LYS LYS PHE ASP VAL ASN HIS LEU
SEQRES 13 E 320 THR VAL ALA GLY ASP SER VAL GLY GLY ASN MET ALA THR
SEQRES 14 E 320 VAL MET THR LEU LEU THR LYS GLN ARG GLY GLY GLN LYS
SEQRES 15 E 320 ILE GLY GLN GLN VAL LEU TYR TYR PRO VAL THR ASP ALA
SEQRES 16 E 320 ASN PHE ASP THR ASP SER TYR ASN GLU PHE ALA GLU ASN
SEQRES 17 E 320 TYR ALA LEU THR LYS GLU GLY MET ILE TRP PHE TRP ASP
SEQRES 18 E 320 GLN TYR THR THR SER GLN GLU GLU ARG HIS GLN ILE THR
SEQRES 19 E 320 ALA SER PRO LEU ARG ALA THR LYS GLU ASP LEU ALA ASP
SEQRES 20 E 320 LEU PRO ALA ALA LEU ILE ILE THR GLY GLU ALA ASP VAL
SEQRES 21 E 320 LEU ARG ASP GLU GLY GLU ALA TYR ALA ARG LYS LEU ARG
SEQRES 22 E 320 GLU ALA ASP VAL GLU VAL THR GLN VAL ARG PHE GLN ALA
SEQRES 23 E 320 ILE ILE HIS ASP PHE VAL MET VAL ASN SER MET ASN GLU
SEQRES 24 E 320 THR HIS ALA THR ARG ALA ALA MET SER LEU SER THR GLN
SEQRES 25 E 320 TRP ILE ASN GLU LYS ASN ARG LYS
SEQRES 1 F 320 GLY SER HIS MET VAL GLU ARG ILE SER LEU GLU LYS ALA
SEQRES 2 F 320 ALA LEU GLU PHE SER GLU ALA ASN ALA PRO HIS PRO ARG
SEQRES 3 F 320 ILE TYR GLU LEU PRO VAL GLU GLU GLY ARG SER LEU LEU
SEQRES 4 F 320 ASN GLU VAL GLN ASP SER PRO VAL VAL LYS GLU ASP VAL
SEQRES 5 F 320 ASP ILE GLU ASP ILE ALA VAL ASP THR GLY GLU TRP GLY
SEQRES 6 F 320 GLU ILE ASN VAL ARG PHE ILE ARG PRO LEU HIS GLN GLU
SEQRES 7 F 320 LYS LYS LEU PRO VAL ILE PHE TYR ILE HIS GLY ALA GLY
SEQRES 8 F 320 TRP VAL PHE GLY ASN ALA HIS THR HIS ASP LYS LEU ILE
SEQRES 9 F 320 ARG GLU LEU ALA VAL ARG THR ASN SER VAL VAL VAL PHE
SEQRES 10 F 320 SER GLU TYR SER LEU SER PRO GLU ALA LYS TYR PRO THR
SEQRES 11 F 320 ALA ILE GLU GLN ASN TYR ALA VAL LEU GLN GLN LEU LYS
SEQRES 12 F 320 ASP PHE ALA ASN ASP LYS LYS PHE ASP VAL ASN HIS LEU
SEQRES 13 F 320 THR VAL ALA GLY ASP SER VAL GLY GLY ASN MET ALA THR
SEQRES 14 F 320 VAL MET THR LEU LEU THR LYS GLN ARG GLY GLY GLN LYS
SEQRES 15 F 320 ILE GLY GLN GLN VAL LEU TYR TYR PRO VAL THR ASP ALA
SEQRES 16 F 320 ASN PHE ASP THR ASP SER TYR ASN GLU PHE ALA GLU ASN
SEQRES 17 F 320 TYR ALA LEU THR LYS GLU GLY MET ILE TRP PHE TRP ASP
SEQRES 18 F 320 GLN TYR THR THR SER GLN GLU GLU ARG HIS GLN ILE THR
SEQRES 19 F 320 ALA SER PRO LEU ARG ALA THR LYS GLU ASP LEU ALA ASP
SEQRES 20 F 320 LEU PRO ALA ALA LEU ILE ILE THR GLY GLU ALA ASP VAL
SEQRES 21 F 320 LEU ARG ASP GLU GLY GLU ALA TYR ALA ARG LYS LEU ARG
SEQRES 22 F 320 GLU ALA ASP VAL GLU VAL THR GLN VAL ARG PHE GLN ALA
SEQRES 23 F 320 ILE ILE HIS ASP PHE VAL MET VAL ASN SER MET ASN GLU
SEQRES 24 F 320 THR HIS ALA THR ARG ALA ALA MET SER LEU SER THR GLN
SEQRES 25 F 320 TRP ILE ASN GLU LYS ASN ARG LYS
SEQRES 1 G 320 GLY SER HIS MET VAL GLU ARG ILE SER LEU GLU LYS ALA
SEQRES 2 G 320 ALA LEU GLU PHE SER GLU ALA ASN ALA PRO HIS PRO ARG
SEQRES 3 G 320 ILE TYR GLU LEU PRO VAL GLU GLU GLY ARG SER LEU LEU
SEQRES 4 G 320 ASN GLU VAL GLN ASP SER PRO VAL VAL LYS GLU ASP VAL
SEQRES 5 G 320 ASP ILE GLU ASP ILE ALA VAL ASP THR GLY GLU TRP GLY
SEQRES 6 G 320 GLU ILE ASN VAL ARG PHE ILE ARG PRO LEU HIS GLN GLU
SEQRES 7 G 320 LYS LYS LEU PRO VAL ILE PHE TYR ILE HIS GLY ALA GLY
SEQRES 8 G 320 TRP VAL PHE GLY ASN ALA HIS THR HIS ASP LYS LEU ILE
SEQRES 9 G 320 ARG GLU LEU ALA VAL ARG THR ASN SER VAL VAL VAL PHE
SEQRES 10 G 320 SER GLU TYR SER LEU SER PRO GLU ALA LYS TYR PRO THR
SEQRES 11 G 320 ALA ILE GLU GLN ASN TYR ALA VAL LEU GLN GLN LEU LYS
SEQRES 12 G 320 ASP PHE ALA ASN ASP LYS LYS PHE ASP VAL ASN HIS LEU
SEQRES 13 G 320 THR VAL ALA GLY ASP SER VAL GLY GLY ASN MET ALA THR
SEQRES 14 G 320 VAL MET THR LEU LEU THR LYS GLN ARG GLY GLY GLN LYS
SEQRES 15 G 320 ILE GLY GLN GLN VAL LEU TYR TYR PRO VAL THR ASP ALA
SEQRES 16 G 320 ASN PHE ASP THR ASP SER TYR ASN GLU PHE ALA GLU ASN
SEQRES 17 G 320 TYR ALA LEU THR LYS GLU GLY MET ILE TRP PHE TRP ASP
SEQRES 18 G 320 GLN TYR THR THR SER GLN GLU GLU ARG HIS GLN ILE THR
SEQRES 19 G 320 ALA SER PRO LEU ARG ALA THR LYS GLU ASP LEU ALA ASP
SEQRES 20 G 320 LEU PRO ALA ALA LEU ILE ILE THR GLY GLU ALA ASP VAL
SEQRES 21 G 320 LEU ARG ASP GLU GLY GLU ALA TYR ALA ARG LYS LEU ARG
SEQRES 22 G 320 GLU ALA ASP VAL GLU VAL THR GLN VAL ARG PHE GLN ALA
SEQRES 23 G 320 ILE ILE HIS ASP PHE VAL MET VAL ASN SER MET ASN GLU
SEQRES 24 G 320 THR HIS ALA THR ARG ALA ALA MET SER LEU SER THR GLN
SEQRES 25 G 320 TRP ILE ASN GLU LYS ASN ARG LYS
SEQRES 1 H 320 GLY SER HIS MET VAL GLU ARG ILE SER LEU GLU LYS ALA
SEQRES 2 H 320 ALA LEU GLU PHE SER GLU ALA ASN ALA PRO HIS PRO ARG
SEQRES 3 H 320 ILE TYR GLU LEU PRO VAL GLU GLU GLY ARG SER LEU LEU
SEQRES 4 H 320 ASN GLU VAL GLN ASP SER PRO VAL VAL LYS GLU ASP VAL
SEQRES 5 H 320 ASP ILE GLU ASP ILE ALA VAL ASP THR GLY GLU TRP GLY
SEQRES 6 H 320 GLU ILE ASN VAL ARG PHE ILE ARG PRO LEU HIS GLN GLU
SEQRES 7 H 320 LYS LYS LEU PRO VAL ILE PHE TYR ILE HIS GLY ALA GLY
SEQRES 8 H 320 TRP VAL PHE GLY ASN ALA HIS THR HIS ASP LYS LEU ILE
SEQRES 9 H 320 ARG GLU LEU ALA VAL ARG THR ASN SER VAL VAL VAL PHE
SEQRES 10 H 320 SER GLU TYR SER LEU SER PRO GLU ALA LYS TYR PRO THR
SEQRES 11 H 320 ALA ILE GLU GLN ASN TYR ALA VAL LEU GLN GLN LEU LYS
SEQRES 12 H 320 ASP PHE ALA ASN ASP LYS LYS PHE ASP VAL ASN HIS LEU
SEQRES 13 H 320 THR VAL ALA GLY ASP SER VAL GLY GLY ASN MET ALA THR
SEQRES 14 H 320 VAL MET THR LEU LEU THR LYS GLN ARG GLY GLY GLN LYS
SEQRES 15 H 320 ILE GLY GLN GLN VAL LEU TYR TYR PRO VAL THR ASP ALA
SEQRES 16 H 320 ASN PHE ASP THR ASP SER TYR ASN GLU PHE ALA GLU ASN
SEQRES 17 H 320 TYR ALA LEU THR LYS GLU GLY MET ILE TRP PHE TRP ASP
SEQRES 18 H 320 GLN TYR THR THR SER GLN GLU GLU ARG HIS GLN ILE THR
SEQRES 19 H 320 ALA SER PRO LEU ARG ALA THR LYS GLU ASP LEU ALA ASP
SEQRES 20 H 320 LEU PRO ALA ALA LEU ILE ILE THR GLY GLU ALA ASP VAL
SEQRES 21 H 320 LEU ARG ASP GLU GLY GLU ALA TYR ALA ARG LYS LEU ARG
SEQRES 22 H 320 GLU ALA ASP VAL GLU VAL THR GLN VAL ARG PHE GLN ALA
SEQRES 23 H 320 ILE ILE HIS ASP PHE VAL MET VAL ASN SER MET ASN GLU
SEQRES 24 H 320 THR HIS ALA THR ARG ALA ALA MET SER LEU SER THR GLN
SEQRES 25 H 320 TRP ILE ASN GLU LYS ASN ARG LYS
FORMUL 9 HOH *577(H2 O)
HELIX 1 AA1 GLU A 8 ASN A 18 1 11
HELIX 2 AA2 ARG A 23 LEU A 27 5 5
HELIX 3 AA3 PRO A 28 GLN A 40 1 13
HELIX 4 AA4 GLY A 59 TRP A 61 5 3
HELIX 5 AA5 HIS A 97 THR A 108 1 12
HELIX 6 AA6 PRO A 126 GLN A 138 1 13
HELIX 7 AA7 GLN A 138 ALA A 143 1 6
HELIX 8 AA8 SER A 159 GLY A 176 1 18
HELIX 9 AA9 THR A 196 PHE A 202 1 7
HELIX 10 AB1 THR A 209 THR A 221 1 13
HELIX 11 AB2 SER A 223 HIS A 228 1 6
HELIX 12 AB3 SER A 233 ALA A 237 5 5
HELIX 13 AB4 THR A 238 ALA A 243 1 6
HELIX 14 AB5 LEU A 258 ALA A 272 1 15
HELIX 15 AB6 VAL A 291 ASN A 295 5 5
HELIX 16 AB7 THR A 297 ASN A 315 1 19
HELIX 17 AB8 GLU B 8 ASN B 18 1 11
HELIX 18 AB9 ARG B 23 LEU B 27 5 5
HELIX 19 AC1 PRO B 28 GLN B 40 1 13
HELIX 20 AC2 GLY B 59 TRP B 61 5 3
HELIX 21 AC3 HIS B 97 THR B 108 1 12
HELIX 22 AC4 PRO B 126 GLN B 137 1 12
HELIX 23 AC5 GLN B 138 LYS B 147 1 10
HELIX 24 AC6 SER B 159 GLY B 176 1 18
HELIX 25 AC7 THR B 196 PHE B 202 1 7
HELIX 26 AC8 THR B 209 THR B 221 1 13
HELIX 27 AC9 SER B 223 GLN B 229 1 7
HELIX 28 AD1 SER B 233 ALA B 237 5 5
HELIX 29 AD2 THR B 238 ALA B 243 1 6
HELIX 30 AD3 LEU B 258 ALA B 272 1 15
HELIX 31 AD4 VAL B 291 ASN B 295 5 5
HELIX 32 AD5 THR B 297 LYS B 317 1 21
HELIX 33 AD6 GLU C 8 ASN C 18 1 11
HELIX 34 AD7 PRO C 28 GLN C 40 1 13
HELIX 35 AD8 GLY C 59 TRP C 61 5 3
HELIX 36 AD9 HIS C 97 ASN C 109 1 13
HELIX 37 AE1 PRO C 126 GLN C 138 1 13
HELIX 38 AE2 LEU C 139 PHE C 142 5 4
HELIX 39 AE3 SER C 159 GLY C 176 1 18
HELIX 40 AE4 THR C 196 PHE C 202 1 7
HELIX 41 AE5 THR C 209 THR C 221 1 13
HELIX 42 AE6 SER C 223 HIS C 228 1 6
HELIX 43 AE7 SER C 233 ALA C 237 5 5
HELIX 44 AE8 THR C 238 ALA C 243 1 6
HELIX 45 AE9 LEU C 258 ALA C 272 1 15
HELIX 46 AF1 VAL C 291 ASN C 295 5 5
HELIX 47 AF2 THR C 297 LYS C 317 1 21
HELIX 48 AF3 GLU D 8 ASN D 18 1 11
HELIX 49 AF4 ARG D 23 LEU D 27 5 5
HELIX 50 AF5 PRO D 28 GLN D 40 1 13
HELIX 51 AF6 GLY D 59 TRP D 61 5 3
HELIX 52 AF7 HIS D 97 THR D 108 1 12
HELIX 53 AF8 PRO D 126 LEU D 139 1 14
HELIX 54 AF9 LYS D 140 PHE D 142 5 3
HELIX 55 AG1 SER D 159 GLY D 176 1 18
HELIX 56 AG2 THR D 196 PHE D 202 1 7
HELIX 57 AG3 THR D 209 THR D 221 1 13
HELIX 58 AG4 GLU D 225 GLN D 229 5 5
HELIX 59 AG5 SER D 233 ALA D 237 5 5
HELIX 60 AG6 THR D 238 ALA D 243 1 6
HELIX 61 AG7 LEU D 258 ALA D 272 1 15
HELIX 62 AG8 VAL D 291 ASN D 295 5 5
HELIX 63 AG9 THR D 297 ASN D 315 1 19
HELIX 64 AH1 GLU E 8 ASN E 18 1 11
HELIX 65 AH2 ARG E 23 LEU E 27 5 5
HELIX 66 AH3 PRO E 28 GLN E 40 1 13
HELIX 67 AH4 HIS E 97 ASN E 109 1 13
HELIX 68 AH5 PRO E 126 LYS E 147 1 22
HELIX 69 AH6 SER E 159 GLY E 176 1 18
HELIX 70 AH7 THR E 196 PHE E 202 1 7
HELIX 71 AH8 THR E 209 THR E 221 1 13
HELIX 72 AH9 SER E 223 HIS E 228 1 6
HELIX 73 AI1 SER E 233 ALA E 237 5 5
HELIX 74 AI2 THR E 238 ALA E 243 1 6
HELIX 75 AI3 LEU E 258 ALA E 272 1 15
HELIX 76 AI4 VAL E 291 ASN E 295 5 5
HELIX 77 AI5 THR E 297 ARG E 316 1 20
HELIX 78 AI6 GLU F 8 ASN F 18 1 11
HELIX 79 AI7 ARG F 23 LEU F 27 5 5
HELIX 80 AI8 PRO F 28 GLN F 40 1 13
HELIX 81 AI9 HIS F 97 ASN F 109 1 13
HELIX 82 AJ1 PRO F 126 GLN F 138 1 13
HELIX 83 AJ2 GLN F 138 ASN F 144 1 7
HELIX 84 AJ3 SER F 159 GLY F 176 1 18
HELIX 85 AJ4 THR F 196 PHE F 202 1 7
HELIX 86 AJ5 THR F 209 THR F 221 1 13
HELIX 87 AJ6 SER F 223 HIS F 228 1 6
HELIX 88 AJ7 SER F 233 ALA F 237 5 5
HELIX 89 AJ8 THR F 238 ALA F 243 1 6
HELIX 90 AJ9 LEU F 258 ALA F 272 1 15
HELIX 91 AK1 VAL F 291 ASN F 295 5 5
HELIX 92 AK2 THR F 297 ARG F 316 1 20
HELIX 93 AK3 GLU G 8 ASN G 18 1 11
HELIX 94 AK4 ARG G 23 LEU G 27 5 5
HELIX 95 AK5 PRO G 28 GLN G 40 1 13
HELIX 96 AK6 HIS G 97 ASN G 109 1 13
HELIX 97 AK7 PRO G 126 GLN G 137 1 12
HELIX 98 AK8 GLN G 138 ALA G 143 1 6
HELIX 99 AK9 SER G 159 GLY G 176 1 18
HELIX 100 AL1 THR G 196 PHE G 202 1 7
HELIX 101 AL2 THR G 209 THR G 221 1 13
HELIX 102 AL3 SER G 233 ALA G 237 5 5
HELIX 103 AL4 THR G 238 ALA G 243 1 6
HELIX 104 AL5 LEU G 258 ALA G 272 1 15
HELIX 105 AL6 VAL G 291 ASN G 295 5 5
HELIX 106 AL7 THR G 297 LYS G 317 1 21
HELIX 107 AL8 GLU H 8 ASN H 18 1 11
HELIX 108 AL9 ARG H 23 LEU H 27 5 5
HELIX 109 AM1 PRO H 28 GLN H 40 1 13
HELIX 110 AM2 HIS H 97 THR H 108 1 12
HELIX 111 AM3 PRO H 126 ALA H 143 1 18
HELIX 112 AM4 SER H 159 GLY H 176 1 18
HELIX 113 AM5 THR H 196 PHE H 202 1 7
HELIX 114 AM6 THR H 209 THR H 221 1 13
HELIX 115 AM7 SER H 223 HIS H 228 1 6
HELIX 116 AM8 SER H 233 ALA H 237 5 5
HELIX 117 AM9 THR H 238 ALA H 243 1 6
HELIX 118 AN1 LEU H 258 ALA H 272 1 15
HELIX 119 AN2 VAL H 291 ASN H 295 5 5
HELIX 120 AN3 THR H 297 ASN H 315 1 19
SHEET 1 AA116 ASP A 50 ASP A 57 0
SHEET 2 AA116 GLU A 63 ARG A 70 -1 O PHE A 68 N GLU A 52
SHEET 3 AA116 VAL A 111 GLU A 116 -1 O PHE A 114 N ARG A 67
SHEET 4 AA116 LEU A 78 ILE A 84 1 N ILE A 81 O VAL A 113
SHEET 5 AA116 PHE A 148 ASP A 158 1 O HIS A 152 N VAL A 80
SHEET 6 AA116 GLN A 182 TYR A 186 1 O GLN A 182 N VAL A 155
SHEET 7 AA116 ALA A 247 ALA A 255 1 O LEU A 249 N LEU A 185
SHEET 8 AA116 VAL A 276 ILE A 285 1 O PHE A 281 N THR A 252
SHEET 9 AA116 VAL G 276 ILE G 285 -1 O ARG G 280 N ARG A 280
SHEET 10 AA116 ALA G 247 ALA G 255 1 N ILE G 250 O THR G 277
SHEET 11 AA116 GLN G 182 TYR G 186 1 N LEU G 185 O LEU G 249
SHEET 12 AA116 PHE G 148 ASP G 158 1 N GLY G 157 O TYR G 186
SHEET 13 AA116 LEU G 78 ILE G 84 1 N PHE G 82 O THR G 154
SHEET 14 AA116 VAL G 111 SER G 115 1 O VAL G 113 N TYR G 83
SHEET 15 AA116 GLU G 63 PRO G 71 -1 N ARG G 67 O PHE G 114
SHEET 16 AA116 VAL G 49 ASP G 57 -1 N GLU G 52 O PHE G 68
SHEET 1 AA216 ASP B 50 ASP B 57 0
SHEET 2 AA216 GLU B 63 ARG B 70 -1 O PHE B 68 N GLU B 52
SHEET 3 AA216 VAL B 111 SER B 115 -1 O PHE B 114 N ARG B 67
SHEET 4 AA216 LEU B 78 ILE B 84 1 N TYR B 83 O VAL B 113
SHEET 5 AA216 PHE B 148 ASP B 158 1 O THR B 154 N PHE B 82
SHEET 6 AA216 GLN B 182 TYR B 186 1 O TYR B 186 N GLY B 157
SHEET 7 AA216 ALA B 247 ALA B 255 1 O LEU B 249 N LEU B 185
SHEET 8 AA216 VAL B 276 ILE B 285 1 O THR B 277 N ALA B 248
SHEET 9 AA216 VAL H 276 ILE H 285 -1 O ARG H 280 N ARG B 280
SHEET 10 AA216 ALA H 247 ALA H 255 1 N ILE H 250 O THR H 277
SHEET 11 AA216 GLN H 182 TYR H 186 1 N LEU H 185 O LEU H 249
SHEET 12 AA216 PHE H 148 ASP H 158 1 N GLY H 157 O TYR H 186
SHEET 13 AA216 LEU H 78 ILE H 84 1 N PHE H 82 O THR H 154
SHEET 14 AA216 VAL H 111 SER H 115 1 O VAL H 111 N ILE H 81
SHEET 15 AA216 GLU H 63 ARG H 70 -1 N ARG H 67 O PHE H 114
SHEET 16 AA216 ASP H 50 ASP H 57 -1 N ASP H 50 O ARG H 70
SHEET 1 AA316 ASP C 50 ASP C 57 0
SHEET 2 AA316 GLU C 63 ARG C 70 -1 O VAL C 66 N ILE C 54
SHEET 3 AA316 VAL C 111 SER C 115 -1 O PHE C 114 N ARG C 67
SHEET 4 AA316 LEU C 78 ILE C 84 1 N TYR C 83 O VAL C 113
SHEET 5 AA316 PHE C 148 ASP C 158 1 O THR C 154 N PHE C 82
SHEET 6 AA316 GLN C 182 TYR C 186 1 O TYR C 186 N GLY C 157
SHEET 7 AA316 ALA C 247 GLY C 253 1 O ALA C 247 N GLN C 183
SHEET 8 AA316 VAL C 276 PHE C 281 1 O THR C 277 N ILE C 250
SHEET 9 AA316 VAL D 276 ILE D 285 -1 O ARG D 280 N ARG C 280
SHEET 10 AA316 ALA D 247 ALA D 255 1 N ILE D 250 O THR D 277
SHEET 11 AA316 GLN D 182 TYR D 186 1 N LEU D 185 O LEU D 249
SHEET 12 AA316 PHE D 148 ASP D 158 1 N GLY D 157 O TYR D 186
SHEET 13 AA316 LEU D 78 ILE D 84 1 N PHE D 82 O THR D 154
SHEET 14 AA316 VAL D 111 SER D 115 1 O VAL D 113 N ILE D 81
SHEET 15 AA316 GLU D 63 ARG D 70 -1 N ARG D 67 O PHE D 114
SHEET 16 AA316 ASP D 50 ASP D 57 -1 N GLU D 52 O PHE D 68
SHEET 1 AA416 VAL E 49 ASP E 57 0
SHEET 2 AA416 GLU E 63 PRO E 71 -1 O PHE E 68 N GLU E 52
SHEET 3 AA416 VAL E 111 SER E 115 -1 O PHE E 114 N ARG E 67
SHEET 4 AA416 LEU E 78 ILE E 84 1 N ILE E 81 O VAL E 111
SHEET 5 AA416 PHE E 148 ASP E 158 1 O THR E 154 N PHE E 82
SHEET 6 AA416 GLN E 182 TYR E 186 1 O TYR E 186 N GLY E 157
SHEET 7 AA416 ALA E 247 ALA E 255 1 O LEU E 249 N LEU E 185
SHEET 8 AA416 VAL E 276 ILE E 285 1 O THR E 277 N ILE E 250
SHEET 9 AA416 VAL F 276 ILE F 285 -1 O ARG F 280 N ARG E 280
SHEET 10 AA416 ALA F 247 ALA F 255 1 N ILE F 250 O THR F 277
SHEET 11 AA416 GLN F 182 TYR F 186 1 N LEU F 185 O LEU F 249
SHEET 12 AA416 PHE F 148 ASP F 158 1 N GLY F 157 O TYR F 186
SHEET 13 AA416 LEU F 78 ILE F 84 1 N PHE F 82 O THR F 154
SHEET 14 AA416 VAL F 111 SER F 115 1 O VAL F 111 N ILE F 81
SHEET 15 AA416 GLU F 63 PRO F 71 -1 N ARG F 67 O PHE F 114
SHEET 16 AA416 VAL F 49 ASP F 57 -1 N GLU F 52 O PHE F 68
CISPEP 1 HIS A 21 PRO A 22 0 2.65
CISPEP 2 SER A 120 PRO A 121 0 -2.73
CISPEP 3 TYR A 125 PRO A 126 0 3.21
CISPEP 4 HIS B 21 PRO B 22 0 -8.05
CISPEP 5 SER B 120 PRO B 121 0 0.11
CISPEP 6 TYR B 125 PRO B 126 0 -2.80
CISPEP 7 HIS C 21 PRO C 22 0 -4.68
CISPEP 8 SER C 120 PRO C 121 0 -1.35
CISPEP 9 TYR C 125 PRO C 126 0 -4.99
CISPEP 10 HIS D 21 PRO D 22 0 -3.98
CISPEP 11 SER D 120 PRO D 121 0 16.86
CISPEP 12 TYR D 125 PRO D 126 0 -1.66
CISPEP 13 HIS E 21 PRO E 22 0 6.23
CISPEP 14 SER E 120 PRO E 121 0 -2.86
CISPEP 15 TYR E 125 PRO E 126 0 -2.35
CISPEP 16 HIS F 21 PRO F 22 0 -5.08
CISPEP 17 SER F 120 PRO F 121 0 -5.27
CISPEP 18 TYR F 125 PRO F 126 0 -4.61
CISPEP 19 HIS G 21 PRO G 22 0 -5.58
CISPEP 20 SER G 120 PRO G 121 0 -0.38
CISPEP 21 TYR G 125 PRO G 126 0 -0.27
CISPEP 22 HIS H 21 PRO H 22 0 2.28
CISPEP 23 SER H 120 PRO H 121 0 -3.13
CISPEP 24 TYR H 125 PRO H 126 0 -5.26
CRYST1 99.200 127.390 104.760 90.00 90.17 90.00 P 1 21 1 16
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.010081 0.000000 0.000030 0.00000
SCALE2 0.000000 0.007850 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009546 0.00000
TER 2519 ARG A 316
TER 5047 LYS B 317
TER 7559 LYS C 317
TER 10062 ARG D 316
TER 12589 ARG E 316
TER 15108 ARG F 316
TER 17636 LYS G 317
TER 20148 ARG H 316
MASTER 378 0 0 120 64 0 0 620717 8 0 200
END
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