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HEADER HYDROLASE 28-DEC-19 6VE6
TITLE A STRUCTURAL CHARACTERIZATION OF POLY(ASPARTIC ACID) HYDROLASE-1 FROM
TITLE 2 SPHINGOMONAS SP. KT-1.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: POLY(ASPARTIC ACID) HYDROLASE-1;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SPHINGOMONAS SP. KT-1;
SOURCE 3 ORGANISM_TAXID: 88363;
SOURCE 4 GENE: PAHZ;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 88363
KEYWDS HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.L.BOLAY,H.SALVO,C.A.BRAMBLEY,T.J.YARED,J.M.MILLER,J.R.WALLEN,
AUTHOR 2 M.H.WEILAND
REVDAT 1 09-DEC-20 6VE6 0
JRNL AUTH C.A.BRAMBLEY,A.L.BOLAY,H.SALVO,A.L.JANSCH,T.J.YARED,
JRNL AUTH 2 J.M.MILLER,J.R.WALLEN,M.H.WEILAND
JRNL TITL STRUCTURAL CHARACTERIZATION OF SPHINGOMONAS SP. KT-1
JRNL TITL 2 PAHZ1-CATALYZED BIODEGRADATION OF THERMALLY SYNTHESIZED
JRNL TITL 3 POLY(ASPARTIC ACID)
JRNL REF ACS SUSTAIN CHEM ENG 2020
JRNL REFN ESSN 2168-0485
JRNL DOI 10.1021/ACSSUSCHEMENG.0C01158
REMARK 2
REMARK 2 RESOLUTION. 2.45 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.14_3260
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.45
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 47.69
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.0
REMARK 3 NUMBER OF REFLECTIONS : 44451
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.238
REMARK 3 R VALUE (WORKING SET) : 0.236
REMARK 3 FREE R VALUE : 0.290
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.940
REMARK 3 FREE R VALUE TEST SET COUNT : 2197
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 47.6910 - 6.1604 0.98 2878 142 0.1629 0.1760
REMARK 3 2 6.1604 - 4.8913 0.99 2777 129 0.1643 0.1640
REMARK 3 3 4.8913 - 4.2734 1.00 2766 111 0.1578 0.2022
REMARK 3 4 4.2734 - 3.8829 0.85 2315 128 0.2927 0.4098
REMARK 3 5 3.8829 - 3.6047 0.93 2538 131 0.2970 0.3622
REMARK 3 6 3.6047 - 3.3922 0.85 2305 134 0.3125 0.3611
REMARK 3 7 3.3922 - 3.2224 0.97 2606 161 0.2615 0.3204
REMARK 3 8 3.2224 - 3.0821 1.00 2701 144 0.2450 0.2775
REMARK 3 9 3.0821 - 2.9635 1.00 2664 151 0.2559 0.3552
REMARK 3 10 2.9635 - 2.8612 1.00 2706 129 0.2494 0.3168
REMARK 3 11 2.8612 - 2.7718 1.00 2671 160 0.2512 0.2751
REMARK 3 12 2.7718 - 2.6926 1.00 2713 132 0.2572 0.3218
REMARK 3 13 2.6926 - 2.6217 1.00 2673 140 0.2644 0.3359
REMARK 3 14 2.6217 - 2.5577 1.00 2661 135 0.2659 0.3175
REMARK 3 15 2.5577 - 2.4996 1.00 2685 142 0.2737 0.3268
REMARK 3 16 2.4996 - 2.4464 0.96 2595 128 0.2683 0.3266
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.310
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 27.860
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 34.66
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : NULL NULL
REMARK 3 ANGLE : NULL NULL
REMARK 3 CHIRALITY : NULL NULL
REMARK 3 PLANARITY : NULL NULL
REMARK 3 DIHEDRAL : NULL NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : 1
REMARK 3 NCS GROUP : 1
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: (CHAIN A AND RESID 32 THROUGH 295)
REMARK 3 SELECTION : (CHAIN B AND RESID 32 THROUGH 295)
REMARK 3 ATOM PAIRS NUMBER : 3208
REMARK 3 RMSD : NULL
REMARK 3 NCS OPERATOR : 2
REMARK 3 REFERENCE SELECTION: (CHAIN A AND RESID 32 THROUGH 295)
REMARK 3 SELECTION : CHAIN C
REMARK 3 ATOM PAIRS NUMBER : 3208
REMARK 3 RMSD : NULL
REMARK 3 NCS OPERATOR : 3
REMARK 3 REFERENCE SELECTION: (CHAIN A AND RESID 32 THROUGH 295)
REMARK 3 SELECTION : (CHAIN D AND RESID 32 THROUGH 295)
REMARK 3 ATOM PAIRS NUMBER : 3208
REMARK 3 RMSD : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 6VE6 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-JAN-20.
REMARK 100 THE DEPOSITION ID IS D_1000246240.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 18-OCT-18
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU MICROMAX-007
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 R CDTE 300K
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-3000
REMARK 200 DATA SCALING SOFTWARE : HKL-3000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 45675
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.446
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 (%) : 99.7
REMARK 200 DATA REDUNDANCY : 5.000
REMARK 200 R MERGE (I) : 0.16000
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 5.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.45
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.49
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 5.20
REMARK 200 R MERGE FOR SHELL (I) : 0.75600
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: PHASER
REMARK 200 STARTING MODEL: 3D0K
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 46.99
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.32
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 15% PEG 3350, 2% 1,4-DIOXANE, AND 0.1M
REMARK 280 TRIS PH 8.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K
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 40.87450
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 85.53000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 43.50300
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 85.53000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 40.87450
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 43.50300
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, 3
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: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
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: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
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 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A 1
REMARK 465 GLY A 2
REMARK 465 SER A 3
REMARK 465 SER A 4
REMARK 465 HIS A 5
REMARK 465 HIS A 6
REMARK 465 HIS A 7
REMARK 465 HIS A 8
REMARK 465 HIS A 9
REMARK 465 HIS A 10
REMARK 465 SER A 11
REMARK 465 SER A 12
REMARK 465 GLY A 13
REMARK 465 LEU A 14
REMARK 465 VAL A 15
REMARK 465 PRO A 16
REMARK 465 ARG A 17
REMARK 465 GLY A 18
REMARK 465 SER A 19
REMARK 465 HIS A 20
REMARK 465 MET A 21
REMARK 465 SER A 22
REMARK 465 LYS A 23
REMARK 465 GLY A 24
REMARK 465 LYS A 25
REMARK 465 ALA A 26
REMARK 465 ALA A 27
REMARK 465 ALA A 28
REMARK 465 LEU A 29
REMARK 465 MET B 1
REMARK 465 GLY B 2
REMARK 465 SER B 3
REMARK 465 SER B 4
REMARK 465 HIS B 5
REMARK 465 HIS B 6
REMARK 465 HIS B 7
REMARK 465 HIS B 8
REMARK 465 HIS B 9
REMARK 465 HIS B 10
REMARK 465 SER B 11
REMARK 465 SER B 12
REMARK 465 GLY B 13
REMARK 465 LEU B 14
REMARK 465 VAL B 15
REMARK 465 PRO B 16
REMARK 465 ARG B 17
REMARK 465 GLY B 18
REMARK 465 SER B 19
REMARK 465 HIS B 20
REMARK 465 MET B 21
REMARK 465 SER B 22
REMARK 465 LYS B 23
REMARK 465 GLY B 24
REMARK 465 LYS B 25
REMARK 465 ALA B 26
REMARK 465 ALA B 27
REMARK 465 ALA B 28
REMARK 465 LEU B 29
REMARK 465 MET C 1
REMARK 465 GLY C 2
REMARK 465 SER C 3
REMARK 465 SER C 4
REMARK 465 HIS C 5
REMARK 465 HIS C 6
REMARK 465 HIS C 7
REMARK 465 HIS C 8
REMARK 465 HIS C 9
REMARK 465 HIS C 10
REMARK 465 SER C 11
REMARK 465 SER C 12
REMARK 465 GLY C 13
REMARK 465 LEU C 14
REMARK 465 VAL C 15
REMARK 465 PRO C 16
REMARK 465 ARG C 17
REMARK 465 GLY C 18
REMARK 465 SER C 19
REMARK 465 HIS C 20
REMARK 465 MET C 21
REMARK 465 SER C 22
REMARK 465 LYS C 23
REMARK 465 GLY C 24
REMARK 465 LYS C 25
REMARK 465 ALA C 26
REMARK 465 ALA C 27
REMARK 465 ALA C 28
REMARK 465 LEU C 29
REMARK 465 PRO C 30
REMARK 465 ASP C 31
REMARK 465 MET D 1
REMARK 465 GLY D 2
REMARK 465 SER D 3
REMARK 465 SER D 4
REMARK 465 HIS D 5
REMARK 465 HIS D 6
REMARK 465 HIS D 7
REMARK 465 HIS D 8
REMARK 465 HIS D 9
REMARK 465 HIS D 10
REMARK 465 SER D 11
REMARK 465 SER D 12
REMARK 465 GLY D 13
REMARK 465 LEU D 14
REMARK 465 VAL D 15
REMARK 465 PRO D 16
REMARK 465 ARG D 17
REMARK 465 GLY D 18
REMARK 465 SER D 19
REMARK 465 HIS D 20
REMARK 465 MET D 21
REMARK 465 SER D 22
REMARK 465 LYS D 23
REMARK 465 GLY D 24
REMARK 465 LYS D 25
REMARK 465 ALA D 26
REMARK 465 ALA D 27
REMARK 465 ALA D 28
REMARK 465 LEU D 29
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O GLY C 73 O HOH C 301 1.93
REMARK 500 OG SER D 157 O HOH D 301 2.00
REMARK 500 O MET A 136 O HOH A 301 2.00
REMARK 500 N VAL A 140 O HOH A 301 2.09
REMARK 500 O HOH A 304 O HOH A 411 2.09
REMARK 500 OG SER C 157 O HOH C 302 2.11
REMARK 500 O HOH B 322 O HOH B 367 2.15
REMARK 500 O TYR A 274 O HOH A 302 2.17
REMARK 500 O GLN D 290 O HOH D 302 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 GLN B 287 CA - CB - CG ANGL. DEV. = -19.4 DEGREES
REMARK 500 GLN C 91 CA - CB - CG ANGL. DEV. = -23.1 DEGREES
REMARK 500 LYS D 267 CB - CA - C ANGL. DEV. = 13.7 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 TYR A 110 -91.16 -114.47
REMARK 500 SER A 157 -116.96 55.78
REMARK 500 ARG A 174 46.55 -108.71
REMARK 500 PRO A 203 62.51 -67.50
REMARK 500 ALA A 279 -143.51 -111.94
REMARK 500 PRO B 34 -2.00 -49.52
REMARK 500 TYR B 110 -89.76 -112.47
REMARK 500 SER B 157 -117.44 57.09
REMARK 500 PRO B 203 62.69 -67.15
REMARK 500 ALA B 279 -147.46 -109.74
REMARK 500 ARG C 74 43.28 -61.92
REMARK 500 TYR C 110 -91.81 -115.69
REMARK 500 SER C 157 -117.10 56.03
REMARK 500 ARG C 174 45.80 -106.64
REMARK 500 PRO C 203 65.09 -66.36
REMARK 500 ALA C 279 -147.57 -109.49
REMARK 500 TYR D 110 -90.80 -111.49
REMARK 500 SER D 157 -116.92 56.84
REMARK 500 ARG D 174 45.39 -106.12
REMARK 500 PRO D 203 62.99 -67.66
REMARK 500 ALA D 279 -144.71 -109.63
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH B 405 DISTANCE = 6.86 ANGSTROMS
REMARK 525 HOH C 376 DISTANCE = 6.35 ANGSTROMS
REMARK 525 HOH C 377 DISTANCE = 6.92 ANGSTROMS
DBREF 6VE6 A 22 295 UNP Q7WSC1 Q7WSC1_9SPHN 41 314
DBREF 6VE6 B 22 295 UNP Q7WSC1 Q7WSC1_9SPHN 41 314
DBREF 6VE6 C 22 295 UNP Q7WSC1 Q7WSC1_9SPHN 41 314
DBREF 6VE6 D 22 295 UNP Q7WSC1 Q7WSC1_9SPHN 41 314
SEQADV 6VE6 MET A 1 UNP Q7WSC1 INITIATING METHIONINE
SEQADV 6VE6 GLY A 2 UNP Q7WSC1 EXPRESSION TAG
SEQADV 6VE6 SER A 3 UNP Q7WSC1 EXPRESSION TAG
SEQADV 6VE6 SER A 4 UNP Q7WSC1 EXPRESSION TAG
SEQADV 6VE6 HIS A 5 UNP Q7WSC1 EXPRESSION TAG
SEQADV 6VE6 HIS A 6 UNP Q7WSC1 EXPRESSION TAG
SEQADV 6VE6 HIS A 7 UNP Q7WSC1 EXPRESSION TAG
SEQADV 6VE6 HIS A 8 UNP Q7WSC1 EXPRESSION TAG
SEQADV 6VE6 HIS A 9 UNP Q7WSC1 EXPRESSION TAG
SEQADV 6VE6 HIS A 10 UNP Q7WSC1 EXPRESSION TAG
SEQADV 6VE6 SER A 11 UNP Q7WSC1 EXPRESSION TAG
SEQADV 6VE6 SER A 12 UNP Q7WSC1 EXPRESSION TAG
SEQADV 6VE6 GLY A 13 UNP Q7WSC1 EXPRESSION TAG
SEQADV 6VE6 LEU A 14 UNP Q7WSC1 EXPRESSION TAG
SEQADV 6VE6 VAL A 15 UNP Q7WSC1 EXPRESSION TAG
SEQADV 6VE6 PRO A 16 UNP Q7WSC1 EXPRESSION TAG
SEQADV 6VE6 ARG A 17 UNP Q7WSC1 EXPRESSION TAG
SEQADV 6VE6 GLY A 18 UNP Q7WSC1 EXPRESSION TAG
SEQADV 6VE6 SER A 19 UNP Q7WSC1 EXPRESSION TAG
SEQADV 6VE6 HIS A 20 UNP Q7WSC1 EXPRESSION TAG
SEQADV 6VE6 MET A 21 UNP Q7WSC1 EXPRESSION TAG
SEQADV 6VE6 MET B 1 UNP Q7WSC1 INITIATING METHIONINE
SEQADV 6VE6 GLY B 2 UNP Q7WSC1 EXPRESSION TAG
SEQADV 6VE6 SER B 3 UNP Q7WSC1 EXPRESSION TAG
SEQADV 6VE6 SER B 4 UNP Q7WSC1 EXPRESSION TAG
SEQADV 6VE6 HIS B 5 UNP Q7WSC1 EXPRESSION TAG
SEQADV 6VE6 HIS B 6 UNP Q7WSC1 EXPRESSION TAG
SEQADV 6VE6 HIS B 7 UNP Q7WSC1 EXPRESSION TAG
SEQADV 6VE6 HIS B 8 UNP Q7WSC1 EXPRESSION TAG
SEQADV 6VE6 HIS B 9 UNP Q7WSC1 EXPRESSION TAG
SEQADV 6VE6 HIS B 10 UNP Q7WSC1 EXPRESSION TAG
SEQADV 6VE6 SER B 11 UNP Q7WSC1 EXPRESSION TAG
SEQADV 6VE6 SER B 12 UNP Q7WSC1 EXPRESSION TAG
SEQADV 6VE6 GLY B 13 UNP Q7WSC1 EXPRESSION TAG
SEQADV 6VE6 LEU B 14 UNP Q7WSC1 EXPRESSION TAG
SEQADV 6VE6 VAL B 15 UNP Q7WSC1 EXPRESSION TAG
SEQADV 6VE6 PRO B 16 UNP Q7WSC1 EXPRESSION TAG
SEQADV 6VE6 ARG B 17 UNP Q7WSC1 EXPRESSION TAG
SEQADV 6VE6 GLY B 18 UNP Q7WSC1 EXPRESSION TAG
SEQADV 6VE6 SER B 19 UNP Q7WSC1 EXPRESSION TAG
SEQADV 6VE6 HIS B 20 UNP Q7WSC1 EXPRESSION TAG
SEQADV 6VE6 MET B 21 UNP Q7WSC1 EXPRESSION TAG
SEQADV 6VE6 MET C 1 UNP Q7WSC1 INITIATING METHIONINE
SEQADV 6VE6 GLY C 2 UNP Q7WSC1 EXPRESSION TAG
SEQADV 6VE6 SER C 3 UNP Q7WSC1 EXPRESSION TAG
SEQADV 6VE6 SER C 4 UNP Q7WSC1 EXPRESSION TAG
SEQADV 6VE6 HIS C 5 UNP Q7WSC1 EXPRESSION TAG
SEQADV 6VE6 HIS C 6 UNP Q7WSC1 EXPRESSION TAG
SEQADV 6VE6 HIS C 7 UNP Q7WSC1 EXPRESSION TAG
SEQADV 6VE6 HIS C 8 UNP Q7WSC1 EXPRESSION TAG
SEQADV 6VE6 HIS C 9 UNP Q7WSC1 EXPRESSION TAG
SEQADV 6VE6 HIS C 10 UNP Q7WSC1 EXPRESSION TAG
SEQADV 6VE6 SER C 11 UNP Q7WSC1 EXPRESSION TAG
SEQADV 6VE6 SER C 12 UNP Q7WSC1 EXPRESSION TAG
SEQADV 6VE6 GLY C 13 UNP Q7WSC1 EXPRESSION TAG
SEQADV 6VE6 LEU C 14 UNP Q7WSC1 EXPRESSION TAG
SEQADV 6VE6 VAL C 15 UNP Q7WSC1 EXPRESSION TAG
SEQADV 6VE6 PRO C 16 UNP Q7WSC1 EXPRESSION TAG
SEQADV 6VE6 ARG C 17 UNP Q7WSC1 EXPRESSION TAG
SEQADV 6VE6 GLY C 18 UNP Q7WSC1 EXPRESSION TAG
SEQADV 6VE6 SER C 19 UNP Q7WSC1 EXPRESSION TAG
SEQADV 6VE6 HIS C 20 UNP Q7WSC1 EXPRESSION TAG
SEQADV 6VE6 MET C 21 UNP Q7WSC1 EXPRESSION TAG
SEQADV 6VE6 MET D 1 UNP Q7WSC1 INITIATING METHIONINE
SEQADV 6VE6 GLY D 2 UNP Q7WSC1 EXPRESSION TAG
SEQADV 6VE6 SER D 3 UNP Q7WSC1 EXPRESSION TAG
SEQADV 6VE6 SER D 4 UNP Q7WSC1 EXPRESSION TAG
SEQADV 6VE6 HIS D 5 UNP Q7WSC1 EXPRESSION TAG
SEQADV 6VE6 HIS D 6 UNP Q7WSC1 EXPRESSION TAG
SEQADV 6VE6 HIS D 7 UNP Q7WSC1 EXPRESSION TAG
SEQADV 6VE6 HIS D 8 UNP Q7WSC1 EXPRESSION TAG
SEQADV 6VE6 HIS D 9 UNP Q7WSC1 EXPRESSION TAG
SEQADV 6VE6 HIS D 10 UNP Q7WSC1 EXPRESSION TAG
SEQADV 6VE6 SER D 11 UNP Q7WSC1 EXPRESSION TAG
SEQADV 6VE6 SER D 12 UNP Q7WSC1 EXPRESSION TAG
SEQADV 6VE6 GLY D 13 UNP Q7WSC1 EXPRESSION TAG
SEQADV 6VE6 LEU D 14 UNP Q7WSC1 EXPRESSION TAG
SEQADV 6VE6 VAL D 15 UNP Q7WSC1 EXPRESSION TAG
SEQADV 6VE6 PRO D 16 UNP Q7WSC1 EXPRESSION TAG
SEQADV 6VE6 ARG D 17 UNP Q7WSC1 EXPRESSION TAG
SEQADV 6VE6 GLY D 18 UNP Q7WSC1 EXPRESSION TAG
SEQADV 6VE6 SER D 19 UNP Q7WSC1 EXPRESSION TAG
SEQADV 6VE6 HIS D 20 UNP Q7WSC1 EXPRESSION TAG
SEQADV 6VE6 MET D 21 UNP Q7WSC1 EXPRESSION TAG
SEQRES 1 A 295 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 A 295 LEU VAL PRO ARG GLY SER HIS MET SER LYS GLY LYS ALA
SEQRES 3 A 295 ALA ALA LEU PRO ASP LEU LYS PRO GLY ALA GLY SER PHE
SEQRES 4 A 295 LEU PHE THR GLY TRP ALA GLY LYS PRO LEU LYS VAL HIS
SEQRES 5 A 295 TYR TYR ALA PRO ASP LYS ILE THR GLU THR THR ARG ILE
SEQRES 6 A 295 LEU PHE VAL ILE HIS GLY ALA GLY ARG ASN ALA ASP GLY
SEQRES 7 A 295 TYR ARG ASP ALA TRP ILE PRO TYR ALA LYS GLU GLY GLN
SEQRES 8 A 295 TYR ILE VAL LEU THR PRO GLU TYR SER MET ALA ASP PHE
SEQRES 9 A 295 PRO THR SER LEU THR TYR ASN VAL GLY HIS ILE VAL ASP
SEQRES 10 A 295 GLU ALA GLY ASN PRO ARG PRO ARG GLU GLU TRP SER PHE
SEQRES 11 A 295 ALA SER ILE GLU PRO MET PHE ASP GLN VAL ARG LYS ALA
SEQRES 12 A 295 THR GLY SER LYS VAL PRO THR TYR ALA ILE TYR GLY HIS
SEQRES 13 A 295 SER ALA GLY GLY GLN PHE VAL HIS ARG PHE VAL GLU LEU
SEQRES 14 A 295 TRP PRO ASP ALA ARG TYR SER ARG ALA VAL ALA ALA ASN
SEQRES 15 A 295 ALA GLY TRP TYR THR MET PRO ASP LEU ALA ILE LYS TYR
SEQRES 16 A 295 PRO TYR GLY LEU LYS ASP ALA PRO THR ASP ALA ALA GLY
SEQRES 17 A 295 LEU LYS ALA THR LEU GLU LYS PRO LEU THR ILE LEU LEU
SEQRES 18 A 295 GLY THR ALA ASP THR ASP VAL ASN HIS HIS GLN LEU SER
SEQRES 19 A 295 ARG THR PRO GLU ALA MET THR GLN GLY VAL HIS ARG LEU
SEQRES 20 A 295 ALA ARG GLY GLU PHE PHE TYR ALA TYR GLY ARG LYS VAL
SEQRES 21 A 295 ALA HIS GLU LEU ASN ALA LYS PHE ALA TRP LYS LEU ASP
SEQRES 22 A 295 TYR ALA PRO ASP ILE ALA HIS SER ASN THR GLY MET SER
SEQRES 23 A 295 GLN TYR ALA GLN LYS LEU VAL TRP GLU
SEQRES 1 B 295 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 B 295 LEU VAL PRO ARG GLY SER HIS MET SER LYS GLY LYS ALA
SEQRES 3 B 295 ALA ALA LEU PRO ASP LEU LYS PRO GLY ALA GLY SER PHE
SEQRES 4 B 295 LEU PHE THR GLY TRP ALA GLY LYS PRO LEU LYS VAL HIS
SEQRES 5 B 295 TYR TYR ALA PRO ASP LYS ILE THR GLU THR THR ARG ILE
SEQRES 6 B 295 LEU PHE VAL ILE HIS GLY ALA GLY ARG ASN ALA ASP GLY
SEQRES 7 B 295 TYR ARG ASP ALA TRP ILE PRO TYR ALA LYS GLU GLY GLN
SEQRES 8 B 295 TYR ILE VAL LEU THR PRO GLU TYR SER MET ALA ASP PHE
SEQRES 9 B 295 PRO THR SER LEU THR TYR ASN VAL GLY HIS ILE VAL ASP
SEQRES 10 B 295 GLU ALA GLY ASN PRO ARG PRO ARG GLU GLU TRP SER PHE
SEQRES 11 B 295 ALA SER ILE GLU PRO MET PHE ASP GLN VAL ARG LYS ALA
SEQRES 12 B 295 THR GLY SER LYS VAL PRO THR TYR ALA ILE TYR GLY HIS
SEQRES 13 B 295 SER ALA GLY GLY GLN PHE VAL HIS ARG PHE VAL GLU LEU
SEQRES 14 B 295 TRP PRO ASP ALA ARG TYR SER ARG ALA VAL ALA ALA ASN
SEQRES 15 B 295 ALA GLY TRP TYR THR MET PRO ASP LEU ALA ILE LYS TYR
SEQRES 16 B 295 PRO TYR GLY LEU LYS ASP ALA PRO THR ASP ALA ALA GLY
SEQRES 17 B 295 LEU LYS ALA THR LEU GLU LYS PRO LEU THR ILE LEU LEU
SEQRES 18 B 295 GLY THR ALA ASP THR ASP VAL ASN HIS HIS GLN LEU SER
SEQRES 19 B 295 ARG THR PRO GLU ALA MET THR GLN GLY VAL HIS ARG LEU
SEQRES 20 B 295 ALA ARG GLY GLU PHE PHE TYR ALA TYR GLY ARG LYS VAL
SEQRES 21 B 295 ALA HIS GLU LEU ASN ALA LYS PHE ALA TRP LYS LEU ASP
SEQRES 22 B 295 TYR ALA PRO ASP ILE ALA HIS SER ASN THR GLY MET SER
SEQRES 23 B 295 GLN TYR ALA GLN LYS LEU VAL TRP GLU
SEQRES 1 C 295 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 C 295 LEU VAL PRO ARG GLY SER HIS MET SER LYS GLY LYS ALA
SEQRES 3 C 295 ALA ALA LEU PRO ASP LEU LYS PRO GLY ALA GLY SER PHE
SEQRES 4 C 295 LEU PHE THR GLY TRP ALA GLY LYS PRO LEU LYS VAL HIS
SEQRES 5 C 295 TYR TYR ALA PRO ASP LYS ILE THR GLU THR THR ARG ILE
SEQRES 6 C 295 LEU PHE VAL ILE HIS GLY ALA GLY ARG ASN ALA ASP GLY
SEQRES 7 C 295 TYR ARG ASP ALA TRP ILE PRO TYR ALA LYS GLU GLY GLN
SEQRES 8 C 295 TYR ILE VAL LEU THR PRO GLU TYR SER MET ALA ASP PHE
SEQRES 9 C 295 PRO THR SER LEU THR TYR ASN VAL GLY HIS ILE VAL ASP
SEQRES 10 C 295 GLU ALA GLY ASN PRO ARG PRO ARG GLU GLU TRP SER PHE
SEQRES 11 C 295 ALA SER ILE GLU PRO MET PHE ASP GLN VAL ARG LYS ALA
SEQRES 12 C 295 THR GLY SER LYS VAL PRO THR TYR ALA ILE TYR GLY HIS
SEQRES 13 C 295 SER ALA GLY GLY GLN PHE VAL HIS ARG PHE VAL GLU LEU
SEQRES 14 C 295 TRP PRO ASP ALA ARG TYR SER ARG ALA VAL ALA ALA ASN
SEQRES 15 C 295 ALA GLY TRP TYR THR MET PRO ASP LEU ALA ILE LYS TYR
SEQRES 16 C 295 PRO TYR GLY LEU LYS ASP ALA PRO THR ASP ALA ALA GLY
SEQRES 17 C 295 LEU LYS ALA THR LEU GLU LYS PRO LEU THR ILE LEU LEU
SEQRES 18 C 295 GLY THR ALA ASP THR ASP VAL ASN HIS HIS GLN LEU SER
SEQRES 19 C 295 ARG THR PRO GLU ALA MET THR GLN GLY VAL HIS ARG LEU
SEQRES 20 C 295 ALA ARG GLY GLU PHE PHE TYR ALA TYR GLY ARG LYS VAL
SEQRES 21 C 295 ALA HIS GLU LEU ASN ALA LYS PHE ALA TRP LYS LEU ASP
SEQRES 22 C 295 TYR ALA PRO ASP ILE ALA HIS SER ASN THR GLY MET SER
SEQRES 23 C 295 GLN TYR ALA GLN LYS LEU VAL TRP GLU
SEQRES 1 D 295 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 D 295 LEU VAL PRO ARG GLY SER HIS MET SER LYS GLY LYS ALA
SEQRES 3 D 295 ALA ALA LEU PRO ASP LEU LYS PRO GLY ALA GLY SER PHE
SEQRES 4 D 295 LEU PHE THR GLY TRP ALA GLY LYS PRO LEU LYS VAL HIS
SEQRES 5 D 295 TYR TYR ALA PRO ASP LYS ILE THR GLU THR THR ARG ILE
SEQRES 6 D 295 LEU PHE VAL ILE HIS GLY ALA GLY ARG ASN ALA ASP GLY
SEQRES 7 D 295 TYR ARG ASP ALA TRP ILE PRO TYR ALA LYS GLU GLY GLN
SEQRES 8 D 295 TYR ILE VAL LEU THR PRO GLU TYR SER MET ALA ASP PHE
SEQRES 9 D 295 PRO THR SER LEU THR TYR ASN VAL GLY HIS ILE VAL ASP
SEQRES 10 D 295 GLU ALA GLY ASN PRO ARG PRO ARG GLU GLU TRP SER PHE
SEQRES 11 D 295 ALA SER ILE GLU PRO MET PHE ASP GLN VAL ARG LYS ALA
SEQRES 12 D 295 THR GLY SER LYS VAL PRO THR TYR ALA ILE TYR GLY HIS
SEQRES 13 D 295 SER ALA GLY GLY GLN PHE VAL HIS ARG PHE VAL GLU LEU
SEQRES 14 D 295 TRP PRO ASP ALA ARG TYR SER ARG ALA VAL ALA ALA ASN
SEQRES 15 D 295 ALA GLY TRP TYR THR MET PRO ASP LEU ALA ILE LYS TYR
SEQRES 16 D 295 PRO TYR GLY LEU LYS ASP ALA PRO THR ASP ALA ALA GLY
SEQRES 17 D 295 LEU LYS ALA THR LEU GLU LYS PRO LEU THR ILE LEU LEU
SEQRES 18 D 295 GLY THR ALA ASP THR ASP VAL ASN HIS HIS GLN LEU SER
SEQRES 19 D 295 ARG THR PRO GLU ALA MET THR GLN GLY VAL HIS ARG LEU
SEQRES 20 D 295 ALA ARG GLY GLU PHE PHE TYR ALA TYR GLY ARG LYS VAL
SEQRES 21 D 295 ALA HIS GLU LEU ASN ALA LYS PHE ALA TRP LYS LEU ASP
SEQRES 22 D 295 TYR ALA PRO ASP ILE ALA HIS SER ASN THR GLY MET SER
SEQRES 23 D 295 GLN TYR ALA GLN LYS LEU VAL TRP GLU
FORMUL 5 HOH *424(H2 O)
HELIX 1 AA1 ASN A 75 GLN A 91 1 17
HELIX 2 AA2 PRO A 124 ALA A 131 5 8
HELIX 3 AA3 SER A 132 GLY A 145 1 14
HELIX 4 AA4 SER A 157 TRP A 170 1 14
HELIX 5 AA5 ASP A 205 LEU A 213 1 9
HELIX 6 AA6 THR A 236 THR A 241 1 6
HELIX 7 AA7 HIS A 245 LEU A 264 1 20
HELIX 8 AA8 SER A 281 GLN A 290 1 10
HELIX 9 AA9 ASN B 75 GLN B 91 1 17
HELIX 10 AB1 PRO B 124 ALA B 131 5 8
HELIX 11 AB2 SER B 132 GLY B 145 1 14
HELIX 12 AB3 SER B 157 TRP B 170 1 14
HELIX 13 AB4 ASP B 205 GLU B 214 1 10
HELIX 14 AB5 THR B 236 THR B 241 1 6
HELIX 15 AB6 HIS B 245 LEU B 264 1 20
HELIX 16 AB7 SER B 281 GLN B 290 1 10
HELIX 17 AB8 ASN C 75 GLN C 91 1 17
HELIX 18 AB9 PRO C 124 ALA C 131 5 8
HELIX 19 AC1 SER C 132 GLY C 145 1 14
HELIX 20 AC2 SER C 157 TRP C 170 1 14
HELIX 21 AC3 ASP C 205 LEU C 213 1 9
HELIX 22 AC4 THR C 236 THR C 241 1 6
HELIX 23 AC5 HIS C 245 LEU C 264 1 20
HELIX 24 AC6 SER C 281 GLN C 290 1 10
HELIX 25 AC7 ASN D 75 GLN D 91 1 17
HELIX 26 AC8 THR D 106 TYR D 110 5 5
HELIX 27 AC9 PRO D 124 ALA D 131 5 8
HELIX 28 AD1 SER D 132 GLY D 145 1 14
HELIX 29 AD2 SER D 157 TRP D 170 1 14
HELIX 30 AD3 ASP D 205 LEU D 213 1 9
HELIX 31 AD4 THR D 236 THR D 241 1 6
HELIX 32 AD5 HIS D 245 ASN D 265 1 21
HELIX 33 AD6 SER D 281 GLN D 290 1 10
SHEET 1 AA1 8 GLY A 35 PHE A 41 0
SHEET 2 AA1 8 LEU A 49 ALA A 55 -1 O VAL A 51 N PHE A 39
SHEET 3 AA1 8 ILE A 93 GLU A 98 -1 O THR A 96 N HIS A 52
SHEET 4 AA1 8 ILE A 65 ILE A 69 1 N LEU A 66 O LEU A 95
SHEET 5 AA1 8 TYR A 151 HIS A 156 1 O TYR A 154 N PHE A 67
SHEET 6 AA1 8 TYR A 175 ALA A 181 1 O ALA A 181 N GLY A 155
SHEET 7 AA1 8 LEU A 217 GLY A 222 1 O THR A 218 N ALA A 178
SHEET 8 AA1 8 LYS A 271 ALA A 275 1 O LYS A 271 N ILE A 219
SHEET 1 AA2 8 ALA B 36 PHE B 41 0
SHEET 2 AA2 8 LEU B 49 TYR B 54 -1 O VAL B 51 N PHE B 39
SHEET 3 AA2 8 ILE B 93 GLU B 98 -1 O THR B 96 N HIS B 52
SHEET 4 AA2 8 ILE B 65 ILE B 69 1 N VAL B 68 O LEU B 95
SHEET 5 AA2 8 TYR B 151 HIS B 156 1 O TYR B 154 N PHE B 67
SHEET 6 AA2 8 TYR B 175 ALA B 181 1 O ALA B 181 N GLY B 155
SHEET 7 AA2 8 LEU B 217 GLY B 222 1 O THR B 218 N ALA B 178
SHEET 8 AA2 8 LYS B 271 ALA B 275 1 O ALA B 275 N LEU B 221
SHEET 1 AA3 8 GLY C 35 PHE C 41 0
SHEET 2 AA3 8 LEU C 49 ALA C 55 -1 O VAL C 51 N PHE C 39
SHEET 3 AA3 8 ILE C 93 GLU C 98 -1 O THR C 96 N HIS C 52
SHEET 4 AA3 8 ILE C 65 ILE C 69 1 N VAL C 68 O LEU C 95
SHEET 5 AA3 8 TYR C 151 HIS C 156 1 O TYR C 154 N PHE C 67
SHEET 6 AA3 8 TYR C 175 ALA C 181 1 O ALA C 181 N GLY C 155
SHEET 7 AA3 8 LEU C 217 GLY C 222 1 O THR C 218 N ALA C 180
SHEET 8 AA3 8 LYS C 271 ALA C 275 1 O ALA C 275 N LEU C 221
SHEET 1 AA4 8 GLY D 35 PHE D 41 0
SHEET 2 AA4 8 LEU D 49 ALA D 55 -1 O VAL D 51 N PHE D 39
SHEET 3 AA4 8 ILE D 93 GLU D 98 -1 O THR D 96 N HIS D 52
SHEET 4 AA4 8 ILE D 65 ILE D 69 1 N LEU D 66 O ILE D 93
SHEET 5 AA4 8 TYR D 151 HIS D 156 1 O TYR D 154 N PHE D 67
SHEET 6 AA4 8 TYR D 175 ALA D 181 1 O ALA D 181 N GLY D 155
SHEET 7 AA4 8 LEU D 217 GLY D 222 1 O THR D 218 N ALA D 180
SHEET 8 AA4 8 LYS D 271 ALA D 275 1 O LYS D 271 N ILE D 219
CISPEP 1 TYR A 195 PRO A 196 0 12.68
CISPEP 2 TYR B 195 PRO B 196 0 12.43
CISPEP 3 TYR C 195 PRO C 196 0 11.41
CISPEP 4 TYR D 195 PRO D 196 0 12.53
CRYST1 81.749 87.006 171.060 90.00 90.00 90.00 P 21 21 21 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 0.012233 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011493 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005846 0.00000
TER 2107 GLU A 295
TER 4214 GLU B 295
TER 6306 GLU C 295
TER 8413 GLU D 295
MASTER 449 0 0 33 32 0 0 6 8833 4 0 92
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