HEADER HYDROLASE 14-DEC-10 3PZV
TITLE C2 CRYSTAL FORM OF THE ENDO-1,4-BETA-GLUCANASE FROM BACILLUS SUBTILIS
TITLE 2 168
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ENDOGLUCANASE;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 FRAGMENT: CATALYTIC DOMAIN, UNP RESIDUES 27-332;
COMPND 5 SYNONYM: CARBOXYMETHYL-CELLULASE, CMCASE, CELLULASE, ENDO-1,4-BETA-
COMPND 6 GLUCANASE;
COMPND 7 EC: 3.2.1.4;
COMPND 8 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BACILLUS SUBTILIS SUBSP. SUBTILIS;
SOURCE 3 ORGANISM_TAXID: 224308;
SOURCE 4 STRAIN: 168;
SOURCE 5 GENE: EGLS, BGLC, GLD, BSU18130;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS ALPHA/BETA BARREL, GLYCOSYL HYDROLASE, CELLULOSE BINDING, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR C.R.SANTOS,J.H.PAIVA,P.K.AKAO,A.N.MEZA,J.C.SILVA,F.M.SQUINA,R.J.WARD,
AUTHOR 2 R.RULLER,M.T.MURAKAMI
REVDAT 3 21-FEB-24 3PZV 1 SEQADV
REVDAT 2 28-DEC-11 3PZV 1 JRNL
REVDAT 1 14-SEP-11 3PZV 0
JRNL AUTH C.R.SANTOS,J.H.PAIVA,M.L.SFORCA,J.L.NEVES,R.Z.NAVARRO,
JRNL AUTH 2 J.COTA,P.K.AKAO,Z.B.HOFFMAM,A.N.MEZA,J.H.SMETANA,
JRNL AUTH 3 M.L.NOGUEIRA,I.POLIKARPOV,J.XAVIER-NETO,F.M.SQUINA,R.J.WARD,
JRNL AUTH 4 R.RULLER,A.C.ZERI,M.T.MURAKAMI
JRNL TITL DISSECTING STRUCTURE-FUNCTION-STABILITY RELATIONSHIPS OF A
JRNL TITL 2 THERMOSTABLE GH5-CBM3 CELLULASE FROM BACILLUS SUBTILIS 168.
JRNL REF BIOCHEM.J. V. 441 95 2012
JRNL REFN ISSN 0264-6021
JRNL PMID 21880019
JRNL DOI 10.1042/BJ20110869
REMARK 2
REMARK 2 RESOLUTION. 2.87 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.6.4_486)
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 : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.87
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 41.46
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 89.8
REMARK 3 NUMBER OF REFLECTIONS : 28575
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.234
REMARK 3 R VALUE (WORKING SET) : 0.230
REMARK 3 FREE R VALUE : 0.296
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1456
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 41.4684 - 6.1704 0.97 2994 178 0.2027 0.2738
REMARK 3 2 6.1704 - 4.9001 0.97 2966 149 0.2347 0.2851
REMARK 3 3 4.9001 - 4.2814 0.97 2937 164 0.2001 0.2764
REMARK 3 4 4.2814 - 3.8903 0.96 2917 136 0.2077 0.2556
REMARK 3 5 3.8903 - 3.6116 0.96 2905 165 0.2370 0.3232
REMARK 3 6 3.6116 - 3.3988 0.94 2833 149 0.2647 0.2887
REMARK 3 7 3.3988 - 3.2286 0.93 2776 165 0.2716 0.3544
REMARK 3 8 3.2286 - 3.0881 0.89 2679 138 0.2858 0.3606
REMARK 3 9 3.0881 - 2.9693 0.80 2383 137 0.3200 0.3779
REMARK 3 10 2.9693 - 2.8670 0.57 1729 75 0.3203 0.4494
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.20
REMARK 3 SHRINKAGE RADIUS : 0.95
REMARK 3 K_SOL : 0.29
REMARK 3 B_SOL : 38.06
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.410
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : NULL
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 18.14860
REMARK 3 B22 (A**2) : -6.20130
REMARK 3 B33 (A**2) : -11.94730
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 10.05620
REMARK 3 B23 (A**2) : 0.00000
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 : 0.006 9584
REMARK 3 ANGLE : 1.261 12996
REMARK 3 CHIRALITY : 0.088 1376
REMARK 3 PLANARITY : 0.006 1684
REMARK 3 DIHEDRAL : 16.235 3452
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 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3PZV COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 21-DEC-10.
REMARK 100 THE DEPOSITION ID IS D_1000063017.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 09-SEP-10
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : LNLS
REMARK 200 BEAMLINE : W01B-MX2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.4586
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 30407
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.867
REMARK 200 RESOLUTION RANGE LOW (A) : 41.500
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.1
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.00
REMARK 200 COMPLETENESS FOR SHELL (%) : 83.7
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 49.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.41
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG3350 200 MM SODIUM NITRATE, PH
REMARK 280 6.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
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 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 77.67950
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 40.54000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 77.67950
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 40.54000
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, 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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C
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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 6
REMARK 465 GLY A 7
REMARK 465 SER A 8
REMARK 465 SER A 9
REMARK 465 HIS A 10
REMARK 465 HIS A 11
REMARK 465 HIS A 12
REMARK 465 HIS A 13
REMARK 465 HIS A 14
REMARK 465 HIS A 15
REMARK 465 SER A 16
REMARK 465 SER A 17
REMARK 465 GLY A 18
REMARK 465 LEU A 19
REMARK 465 VAL A 20
REMARK 465 PRO A 21
REMARK 465 ARG A 22
REMARK 465 GLY A 23
REMARK 465 SER A 24
REMARK 465 HIS A 25
REMARK 465 MET A 26
REMARK 465 ALA A 27
REMARK 465 SER A 28
REMARK 465 ALA A 29
REMARK 465 ALA A 30
REMARK 465 GLY A 31
REMARK 465 THR A 32
REMARK 465 LYS A 33
REMARK 465 THR A 332
REMARK 465 MET B 6
REMARK 465 GLY B 7
REMARK 465 SER B 8
REMARK 465 SER B 9
REMARK 465 HIS B 10
REMARK 465 HIS B 11
REMARK 465 HIS B 12
REMARK 465 HIS B 13
REMARK 465 HIS B 14
REMARK 465 HIS B 15
REMARK 465 SER B 16
REMARK 465 SER B 17
REMARK 465 GLY B 18
REMARK 465 LEU B 19
REMARK 465 VAL B 20
REMARK 465 PRO B 21
REMARK 465 ARG B 22
REMARK 465 GLY B 23
REMARK 465 SER B 24
REMARK 465 HIS B 25
REMARK 465 MET B 26
REMARK 465 ALA B 27
REMARK 465 SER B 28
REMARK 465 ALA B 29
REMARK 465 ALA B 30
REMARK 465 GLY B 31
REMARK 465 THR B 32
REMARK 465 LYS B 33
REMARK 465 THR B 332
REMARK 465 MET C 6
REMARK 465 GLY C 7
REMARK 465 SER C 8
REMARK 465 SER C 9
REMARK 465 HIS C 10
REMARK 465 HIS C 11
REMARK 465 HIS C 12
REMARK 465 HIS C 13
REMARK 465 HIS C 14
REMARK 465 HIS C 15
REMARK 465 SER C 16
REMARK 465 SER C 17
REMARK 465 GLY C 18
REMARK 465 LEU C 19
REMARK 465 VAL C 20
REMARK 465 PRO C 21
REMARK 465 ARG C 22
REMARK 465 GLY C 23
REMARK 465 SER C 24
REMARK 465 HIS C 25
REMARK 465 MET C 26
REMARK 465 ALA C 27
REMARK 465 SER C 28
REMARK 465 ALA C 29
REMARK 465 ALA C 30
REMARK 465 GLY C 31
REMARK 465 THR C 32
REMARK 465 LYS C 33
REMARK 465 THR C 332
REMARK 465 MET D 6
REMARK 465 GLY D 7
REMARK 465 SER D 8
REMARK 465 SER D 9
REMARK 465 HIS D 10
REMARK 465 HIS D 11
REMARK 465 HIS D 12
REMARK 465 HIS D 13
REMARK 465 HIS D 14
REMARK 465 HIS D 15
REMARK 465 SER D 16
REMARK 465 SER D 17
REMARK 465 GLY D 18
REMARK 465 LEU D 19
REMARK 465 VAL D 20
REMARK 465 PRO D 21
REMARK 465 ARG D 22
REMARK 465 GLY D 23
REMARK 465 SER D 24
REMARK 465 HIS D 25
REMARK 465 MET D 26
REMARK 465 ALA D 27
REMARK 465 SER D 28
REMARK 465 ALA D 29
REMARK 465 ALA D 30
REMARK 465 GLY D 31
REMARK 465 THR D 32
REMARK 465 LYS D 33
REMARK 465 THR D 332
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 PRO A 35 -171.40 -68.39
REMARK 500 VAL A 36 -48.57 52.06
REMARK 500 LEU A 133 -77.07 -157.21
REMARK 500 ALA A 167 89.89 -169.08
REMARK 500 ASP A 217 62.99 -105.20
REMARK 500 ASN A 266 -159.74 -142.04
REMARK 500 GLN A 297 30.26 -66.71
REMARK 500 ASP A 317 -16.70 -48.35
REMARK 500 LEU A 330 23.10 -57.34
REMARK 500 ASN B 51 -168.54 -110.33
REMARK 500 ASN B 105 80.54 -161.78
REMARK 500 LEU B 133 -76.29 -161.19
REMARK 500 ALA B 167 88.20 -163.76
REMARK 500 ASN B 168 -74.08 -36.03
REMARK 500 SER B 208 46.95 75.64
REMARK 500 ASP B 217 57.02 -154.74
REMARK 500 SER B 248 7.97 -59.45
REMARK 500 SER B 261 -166.45 -103.94
REMARK 500 ASN B 266 -149.22 -132.01
REMARK 500 PHE B 270 78.89 -119.49
REMARK 500 PRO C 35 -85.80 -96.59
REMARK 500 VAL C 36 10.34 -63.96
REMARK 500 ASN C 39 53.88 -109.84
REMARK 500 ASN C 51 -132.42 -75.19
REMARK 500 ILE C 88 143.15 -38.39
REMARK 500 PRO C 106 45.57 -77.00
REMARK 500 TRP C 130 84.15 -62.59
REMARK 500 LEU C 133 -77.89 -143.08
REMARK 500 ASP C 135 63.86 -64.02
REMARK 500 PRO C 138 -5.22 -59.73
REMARK 500 PHE C 148 -70.69 -77.09
REMARK 500 PHE C 149 -15.16 -41.19
REMARK 500 ASN C 194 -24.60 -160.66
REMARK 500 SER C 208 68.97 38.67
REMARK 500 ASP C 216 -18.13 -141.36
REMARK 500 GLN C 218 -161.78 -75.06
REMARK 500 VAL C 255 90.97 -59.43
REMARK 500 ASP C 262 -157.85 -73.91
REMARK 500 ASN C 266 -127.36 -140.45
REMARK 500 GLN C 297 72.83 -60.58
REMARK 500 LEU C 330 -74.72 -70.96
REMARK 500 ASN D 51 -152.12 -96.63
REMARK 500 HIS D 65 -157.15 -87.45
REMARK 500 ASN D 75 167.02 162.76
REMARK 500 ASP D 85 -73.72 -94.21
REMARK 500 VAL D 90 155.72 175.48
REMARK 500 THR D 97 -82.50 -70.76
REMARK 500 ALA D 98 -171.91 -68.06
REMARK 500 ASP D 99 61.21 62.05
REMARK 500 LEU D 133 -75.20 -172.27
REMARK 500
REMARK 500 THIS ENTRY HAS 68 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3PZT RELATED DB: PDB
REMARK 900 WITH MANGANESE(II) ION
REMARK 900 RELATED ID: 3PZU RELATED DB: PDB
REMARK 900 P212121 CRYSTAL FORM
DBREF 3PZV A 27 332 UNP P10475 GUN2_BACSU 27 332
DBREF 3PZV B 27 332 UNP P10475 GUN2_BACSU 27 332
DBREF 3PZV C 27 332 UNP P10475 GUN2_BACSU 27 332
DBREF 3PZV D 27 332 UNP P10475 GUN2_BACSU 27 332
SEQADV 3PZV MET A 6 UNP P10475 EXPRESSION TAG
SEQADV 3PZV GLY A 7 UNP P10475 EXPRESSION TAG
SEQADV 3PZV SER A 8 UNP P10475 EXPRESSION TAG
SEQADV 3PZV SER A 9 UNP P10475 EXPRESSION TAG
SEQADV 3PZV HIS A 10 UNP P10475 EXPRESSION TAG
SEQADV 3PZV HIS A 11 UNP P10475 EXPRESSION TAG
SEQADV 3PZV HIS A 12 UNP P10475 EXPRESSION TAG
SEQADV 3PZV HIS A 13 UNP P10475 EXPRESSION TAG
SEQADV 3PZV HIS A 14 UNP P10475 EXPRESSION TAG
SEQADV 3PZV HIS A 15 UNP P10475 EXPRESSION TAG
SEQADV 3PZV SER A 16 UNP P10475 EXPRESSION TAG
SEQADV 3PZV SER A 17 UNP P10475 EXPRESSION TAG
SEQADV 3PZV GLY A 18 UNP P10475 EXPRESSION TAG
SEQADV 3PZV LEU A 19 UNP P10475 EXPRESSION TAG
SEQADV 3PZV VAL A 20 UNP P10475 EXPRESSION TAG
SEQADV 3PZV PRO A 21 UNP P10475 EXPRESSION TAG
SEQADV 3PZV ARG A 22 UNP P10475 EXPRESSION TAG
SEQADV 3PZV GLY A 23 UNP P10475 EXPRESSION TAG
SEQADV 3PZV SER A 24 UNP P10475 EXPRESSION TAG
SEQADV 3PZV HIS A 25 UNP P10475 EXPRESSION TAG
SEQADV 3PZV MET A 26 UNP P10475 EXPRESSION TAG
SEQADV 3PZV MET B 6 UNP P10475 EXPRESSION TAG
SEQADV 3PZV GLY B 7 UNP P10475 EXPRESSION TAG
SEQADV 3PZV SER B 8 UNP P10475 EXPRESSION TAG
SEQADV 3PZV SER B 9 UNP P10475 EXPRESSION TAG
SEQADV 3PZV HIS B 10 UNP P10475 EXPRESSION TAG
SEQADV 3PZV HIS B 11 UNP P10475 EXPRESSION TAG
SEQADV 3PZV HIS B 12 UNP P10475 EXPRESSION TAG
SEQADV 3PZV HIS B 13 UNP P10475 EXPRESSION TAG
SEQADV 3PZV HIS B 14 UNP P10475 EXPRESSION TAG
SEQADV 3PZV HIS B 15 UNP P10475 EXPRESSION TAG
SEQADV 3PZV SER B 16 UNP P10475 EXPRESSION TAG
SEQADV 3PZV SER B 17 UNP P10475 EXPRESSION TAG
SEQADV 3PZV GLY B 18 UNP P10475 EXPRESSION TAG
SEQADV 3PZV LEU B 19 UNP P10475 EXPRESSION TAG
SEQADV 3PZV VAL B 20 UNP P10475 EXPRESSION TAG
SEQADV 3PZV PRO B 21 UNP P10475 EXPRESSION TAG
SEQADV 3PZV ARG B 22 UNP P10475 EXPRESSION TAG
SEQADV 3PZV GLY B 23 UNP P10475 EXPRESSION TAG
SEQADV 3PZV SER B 24 UNP P10475 EXPRESSION TAG
SEQADV 3PZV HIS B 25 UNP P10475 EXPRESSION TAG
SEQADV 3PZV MET B 26 UNP P10475 EXPRESSION TAG
SEQADV 3PZV MET C 6 UNP P10475 EXPRESSION TAG
SEQADV 3PZV GLY C 7 UNP P10475 EXPRESSION TAG
SEQADV 3PZV SER C 8 UNP P10475 EXPRESSION TAG
SEQADV 3PZV SER C 9 UNP P10475 EXPRESSION TAG
SEQADV 3PZV HIS C 10 UNP P10475 EXPRESSION TAG
SEQADV 3PZV HIS C 11 UNP P10475 EXPRESSION TAG
SEQADV 3PZV HIS C 12 UNP P10475 EXPRESSION TAG
SEQADV 3PZV HIS C 13 UNP P10475 EXPRESSION TAG
SEQADV 3PZV HIS C 14 UNP P10475 EXPRESSION TAG
SEQADV 3PZV HIS C 15 UNP P10475 EXPRESSION TAG
SEQADV 3PZV SER C 16 UNP P10475 EXPRESSION TAG
SEQADV 3PZV SER C 17 UNP P10475 EXPRESSION TAG
SEQADV 3PZV GLY C 18 UNP P10475 EXPRESSION TAG
SEQADV 3PZV LEU C 19 UNP P10475 EXPRESSION TAG
SEQADV 3PZV VAL C 20 UNP P10475 EXPRESSION TAG
SEQADV 3PZV PRO C 21 UNP P10475 EXPRESSION TAG
SEQADV 3PZV ARG C 22 UNP P10475 EXPRESSION TAG
SEQADV 3PZV GLY C 23 UNP P10475 EXPRESSION TAG
SEQADV 3PZV SER C 24 UNP P10475 EXPRESSION TAG
SEQADV 3PZV HIS C 25 UNP P10475 EXPRESSION TAG
SEQADV 3PZV MET C 26 UNP P10475 EXPRESSION TAG
SEQADV 3PZV MET D 6 UNP P10475 EXPRESSION TAG
SEQADV 3PZV GLY D 7 UNP P10475 EXPRESSION TAG
SEQADV 3PZV SER D 8 UNP P10475 EXPRESSION TAG
SEQADV 3PZV SER D 9 UNP P10475 EXPRESSION TAG
SEQADV 3PZV HIS D 10 UNP P10475 EXPRESSION TAG
SEQADV 3PZV HIS D 11 UNP P10475 EXPRESSION TAG
SEQADV 3PZV HIS D 12 UNP P10475 EXPRESSION TAG
SEQADV 3PZV HIS D 13 UNP P10475 EXPRESSION TAG
SEQADV 3PZV HIS D 14 UNP P10475 EXPRESSION TAG
SEQADV 3PZV HIS D 15 UNP P10475 EXPRESSION TAG
SEQADV 3PZV SER D 16 UNP P10475 EXPRESSION TAG
SEQADV 3PZV SER D 17 UNP P10475 EXPRESSION TAG
SEQADV 3PZV GLY D 18 UNP P10475 EXPRESSION TAG
SEQADV 3PZV LEU D 19 UNP P10475 EXPRESSION TAG
SEQADV 3PZV VAL D 20 UNP P10475 EXPRESSION TAG
SEQADV 3PZV PRO D 21 UNP P10475 EXPRESSION TAG
SEQADV 3PZV ARG D 22 UNP P10475 EXPRESSION TAG
SEQADV 3PZV GLY D 23 UNP P10475 EXPRESSION TAG
SEQADV 3PZV SER D 24 UNP P10475 EXPRESSION TAG
SEQADV 3PZV HIS D 25 UNP P10475 EXPRESSION TAG
SEQADV 3PZV MET D 26 UNP P10475 EXPRESSION TAG
SEQRES 1 A 327 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 A 327 LEU VAL PRO ARG GLY SER HIS MET ALA SER ALA ALA GLY
SEQRES 3 A 327 THR LYS THR PRO VAL ALA LYS ASN GLY GLN LEU SER ILE
SEQRES 4 A 327 LYS GLY THR GLN LEU VAL ASN ARG ASP GLY LYS ALA VAL
SEQRES 5 A 327 GLN LEU LYS GLY ILE SER SER HIS GLY LEU GLN TRP TYR
SEQRES 6 A 327 GLY GLU TYR VAL ASN LYS ASP SER LEU LYS TRP LEU ARG
SEQRES 7 A 327 ASP ASP TRP GLY ILE THR VAL PHE ARG ALA ALA MET TYR
SEQRES 8 A 327 THR ALA ASP GLY GLY TYR ILE ASP ASN PRO SER VAL LYS
SEQRES 9 A 327 ASN LYS VAL LYS GLU ALA VAL GLU ALA ALA LYS GLU LEU
SEQRES 10 A 327 GLY ILE TYR VAL ILE ILE ASP TRP HIS ILE LEU ASN ASP
SEQRES 11 A 327 GLY ASN PRO ASN GLN ASN LYS GLU LYS ALA LYS GLU PHE
SEQRES 12 A 327 PHE LYS GLU MET SER SER LEU TYR GLY ASN THR PRO ASN
SEQRES 13 A 327 VAL ILE TYR GLU ILE ALA ASN GLU PRO ASN GLY ASP VAL
SEQRES 14 A 327 ASN TRP LYS ARG ASP ILE LYS PRO TYR ALA GLU GLU VAL
SEQRES 15 A 327 ILE SER VAL ILE ARG LYS ASN ASP PRO ASP ASN ILE ILE
SEQRES 16 A 327 ILE VAL GLY THR GLY THR TRP SER GLN ASP VAL ASN ASP
SEQRES 17 A 327 ALA ALA ASP ASP GLN LEU LYS ASP ALA ASN VAL MET TYR
SEQRES 18 A 327 ALA LEU HIS PHE TYR ALA GLY THR HIS GLY GLN PHE LEU
SEQRES 19 A 327 ARG ASP LYS ALA ASN TYR ALA LEU SER LYS GLY ALA PRO
SEQRES 20 A 327 ILE PHE VAL THR GLU TRP GLY THR SER ASP ALA SER GLY
SEQRES 21 A 327 ASN GLY GLY VAL PHE LEU ASP GLN SER ARG GLU TRP LEU
SEQRES 22 A 327 LYS TYR LEU ASP SER LYS THR ILE SER TRP VAL ASN TRP
SEQRES 23 A 327 ASN LEU SER ASP LYS GLN GLU SER SER SER ALA LEU LYS
SEQRES 24 A 327 PRO GLY ALA SER LYS THR GLY GLY TRP ARG LEU SER ASP
SEQRES 25 A 327 LEU SER ALA SER GLY THR PHE VAL ARG GLU ASN ILE LEU
SEQRES 26 A 327 GLY THR
SEQRES 1 B 327 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 B 327 LEU VAL PRO ARG GLY SER HIS MET ALA SER ALA ALA GLY
SEQRES 3 B 327 THR LYS THR PRO VAL ALA LYS ASN GLY GLN LEU SER ILE
SEQRES 4 B 327 LYS GLY THR GLN LEU VAL ASN ARG ASP GLY LYS ALA VAL
SEQRES 5 B 327 GLN LEU LYS GLY ILE SER SER HIS GLY LEU GLN TRP TYR
SEQRES 6 B 327 GLY GLU TYR VAL ASN LYS ASP SER LEU LYS TRP LEU ARG
SEQRES 7 B 327 ASP ASP TRP GLY ILE THR VAL PHE ARG ALA ALA MET TYR
SEQRES 8 B 327 THR ALA ASP GLY GLY TYR ILE ASP ASN PRO SER VAL LYS
SEQRES 9 B 327 ASN LYS VAL LYS GLU ALA VAL GLU ALA ALA LYS GLU LEU
SEQRES 10 B 327 GLY ILE TYR VAL ILE ILE ASP TRP HIS ILE LEU ASN ASP
SEQRES 11 B 327 GLY ASN PRO ASN GLN ASN LYS GLU LYS ALA LYS GLU PHE
SEQRES 12 B 327 PHE LYS GLU MET SER SER LEU TYR GLY ASN THR PRO ASN
SEQRES 13 B 327 VAL ILE TYR GLU ILE ALA ASN GLU PRO ASN GLY ASP VAL
SEQRES 14 B 327 ASN TRP LYS ARG ASP ILE LYS PRO TYR ALA GLU GLU VAL
SEQRES 15 B 327 ILE SER VAL ILE ARG LYS ASN ASP PRO ASP ASN ILE ILE
SEQRES 16 B 327 ILE VAL GLY THR GLY THR TRP SER GLN ASP VAL ASN ASP
SEQRES 17 B 327 ALA ALA ASP ASP GLN LEU LYS ASP ALA ASN VAL MET TYR
SEQRES 18 B 327 ALA LEU HIS PHE TYR ALA GLY THR HIS GLY GLN PHE LEU
SEQRES 19 B 327 ARG ASP LYS ALA ASN TYR ALA LEU SER LYS GLY ALA PRO
SEQRES 20 B 327 ILE PHE VAL THR GLU TRP GLY THR SER ASP ALA SER GLY
SEQRES 21 B 327 ASN GLY GLY VAL PHE LEU ASP GLN SER ARG GLU TRP LEU
SEQRES 22 B 327 LYS TYR LEU ASP SER LYS THR ILE SER TRP VAL ASN TRP
SEQRES 23 B 327 ASN LEU SER ASP LYS GLN GLU SER SER SER ALA LEU LYS
SEQRES 24 B 327 PRO GLY ALA SER LYS THR GLY GLY TRP ARG LEU SER ASP
SEQRES 25 B 327 LEU SER ALA SER GLY THR PHE VAL ARG GLU ASN ILE LEU
SEQRES 26 B 327 GLY THR
SEQRES 1 C 327 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 C 327 LEU VAL PRO ARG GLY SER HIS MET ALA SER ALA ALA GLY
SEQRES 3 C 327 THR LYS THR PRO VAL ALA LYS ASN GLY GLN LEU SER ILE
SEQRES 4 C 327 LYS GLY THR GLN LEU VAL ASN ARG ASP GLY LYS ALA VAL
SEQRES 5 C 327 GLN LEU LYS GLY ILE SER SER HIS GLY LEU GLN TRP TYR
SEQRES 6 C 327 GLY GLU TYR VAL ASN LYS ASP SER LEU LYS TRP LEU ARG
SEQRES 7 C 327 ASP ASP TRP GLY ILE THR VAL PHE ARG ALA ALA MET TYR
SEQRES 8 C 327 THR ALA ASP GLY GLY TYR ILE ASP ASN PRO SER VAL LYS
SEQRES 9 C 327 ASN LYS VAL LYS GLU ALA VAL GLU ALA ALA LYS GLU LEU
SEQRES 10 C 327 GLY ILE TYR VAL ILE ILE ASP TRP HIS ILE LEU ASN ASP
SEQRES 11 C 327 GLY ASN PRO ASN GLN ASN LYS GLU LYS ALA LYS GLU PHE
SEQRES 12 C 327 PHE LYS GLU MET SER SER LEU TYR GLY ASN THR PRO ASN
SEQRES 13 C 327 VAL ILE TYR GLU ILE ALA ASN GLU PRO ASN GLY ASP VAL
SEQRES 14 C 327 ASN TRP LYS ARG ASP ILE LYS PRO TYR ALA GLU GLU VAL
SEQRES 15 C 327 ILE SER VAL ILE ARG LYS ASN ASP PRO ASP ASN ILE ILE
SEQRES 16 C 327 ILE VAL GLY THR GLY THR TRP SER GLN ASP VAL ASN ASP
SEQRES 17 C 327 ALA ALA ASP ASP GLN LEU LYS ASP ALA ASN VAL MET TYR
SEQRES 18 C 327 ALA LEU HIS PHE TYR ALA GLY THR HIS GLY GLN PHE LEU
SEQRES 19 C 327 ARG ASP LYS ALA ASN TYR ALA LEU SER LYS GLY ALA PRO
SEQRES 20 C 327 ILE PHE VAL THR GLU TRP GLY THR SER ASP ALA SER GLY
SEQRES 21 C 327 ASN GLY GLY VAL PHE LEU ASP GLN SER ARG GLU TRP LEU
SEQRES 22 C 327 LYS TYR LEU ASP SER LYS THR ILE SER TRP VAL ASN TRP
SEQRES 23 C 327 ASN LEU SER ASP LYS GLN GLU SER SER SER ALA LEU LYS
SEQRES 24 C 327 PRO GLY ALA SER LYS THR GLY GLY TRP ARG LEU SER ASP
SEQRES 25 C 327 LEU SER ALA SER GLY THR PHE VAL ARG GLU ASN ILE LEU
SEQRES 26 C 327 GLY THR
SEQRES 1 D 327 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 D 327 LEU VAL PRO ARG GLY SER HIS MET ALA SER ALA ALA GLY
SEQRES 3 D 327 THR LYS THR PRO VAL ALA LYS ASN GLY GLN LEU SER ILE
SEQRES 4 D 327 LYS GLY THR GLN LEU VAL ASN ARG ASP GLY LYS ALA VAL
SEQRES 5 D 327 GLN LEU LYS GLY ILE SER SER HIS GLY LEU GLN TRP TYR
SEQRES 6 D 327 GLY GLU TYR VAL ASN LYS ASP SER LEU LYS TRP LEU ARG
SEQRES 7 D 327 ASP ASP TRP GLY ILE THR VAL PHE ARG ALA ALA MET TYR
SEQRES 8 D 327 THR ALA ASP GLY GLY TYR ILE ASP ASN PRO SER VAL LYS
SEQRES 9 D 327 ASN LYS VAL LYS GLU ALA VAL GLU ALA ALA LYS GLU LEU
SEQRES 10 D 327 GLY ILE TYR VAL ILE ILE ASP TRP HIS ILE LEU ASN ASP
SEQRES 11 D 327 GLY ASN PRO ASN GLN ASN LYS GLU LYS ALA LYS GLU PHE
SEQRES 12 D 327 PHE LYS GLU MET SER SER LEU TYR GLY ASN THR PRO ASN
SEQRES 13 D 327 VAL ILE TYR GLU ILE ALA ASN GLU PRO ASN GLY ASP VAL
SEQRES 14 D 327 ASN TRP LYS ARG ASP ILE LYS PRO TYR ALA GLU GLU VAL
SEQRES 15 D 327 ILE SER VAL ILE ARG LYS ASN ASP PRO ASP ASN ILE ILE
SEQRES 16 D 327 ILE VAL GLY THR GLY THR TRP SER GLN ASP VAL ASN ASP
SEQRES 17 D 327 ALA ALA ASP ASP GLN LEU LYS ASP ALA ASN VAL MET TYR
SEQRES 18 D 327 ALA LEU HIS PHE TYR ALA GLY THR HIS GLY GLN PHE LEU
SEQRES 19 D 327 ARG ASP LYS ALA ASN TYR ALA LEU SER LYS GLY ALA PRO
SEQRES 20 D 327 ILE PHE VAL THR GLU TRP GLY THR SER ASP ALA SER GLY
SEQRES 21 D 327 ASN GLY GLY VAL PHE LEU ASP GLN SER ARG GLU TRP LEU
SEQRES 22 D 327 LYS TYR LEU ASP SER LYS THR ILE SER TRP VAL ASN TRP
SEQRES 23 D 327 ASN LEU SER ASP LYS GLN GLU SER SER SER ALA LEU LYS
SEQRES 24 D 327 PRO GLY ALA SER LYS THR GLY GLY TRP ARG LEU SER ASP
SEQRES 25 D 327 LEU SER ALA SER GLY THR PHE VAL ARG GLU ASN ILE LEU
SEQRES 26 D 327 GLY THR
FORMUL 5 HOH *30(H2 O)
HELIX 1 1 GLY A 66 GLY A 71 1 6
HELIX 2 2 GLU A 72 VAL A 74 5 3
HELIX 3 3 ASN A 75 GLY A 87 1 13
HELIX 4 4 ASN A 105 SER A 107 5 3
HELIX 5 5 VAL A 108 GLY A 123 1 16
HELIX 6 6 ASN A 137 GLN A 140 5 4
HELIX 7 7 ASN A 141 GLY A 157 1 17
HELIX 8 8 ASP A 179 LYS A 193 1 15
HELIX 9 9 THR A 204 GLN A 209 1 6
HELIX 10 10 ASP A 210 ASP A 217 1 8
HELIX 11 11 GLY A 236 LYS A 249 1 14
HELIX 12 12 PHE A 270 LYS A 284 1 15
HELIX 13 13 SER A 319 ASN A 328 1 10
HELIX 14 14 THR B 34 GLY B 40 1 7
HELIX 15 15 GLY B 66 GLY B 71 1 6
HELIX 16 16 GLU B 72 VAL B 74 5 3
HELIX 17 17 ASN B 75 ASP B 85 1 11
HELIX 18 18 ASN B 105 SER B 107 5 3
HELIX 19 19 VAL B 108 GLY B 123 1 16
HELIX 20 20 ASN B 141 GLY B 157 1 17
HELIX 21 21 ASP B 179 ASP B 195 1 17
HELIX 22 22 THR B 204 GLN B 209 1 6
HELIX 23 23 ASP B 210 ASP B 216 1 7
HELIX 24 24 GLY B 236 SER B 248 1 13
HELIX 25 25 PHE B 270 LYS B 284 1 15
HELIX 26 26 ARG B 314 LEU B 318 5 5
HELIX 27 27 SER B 319 GLY B 331 1 13
HELIX 28 28 TYR C 70 VAL C 74 5 5
HELIX 29 29 ASN C 75 TRP C 86 1 12
HELIX 30 30 VAL C 108 GLY C 123 1 16
HELIX 31 31 ASN C 141 GLY C 157 1 17
HELIX 32 32 ASP C 179 LYS C 193 1 15
HELIX 33 33 THR C 204 GLN C 209 1 6
HELIX 34 34 ASP C 210 ALA C 215 1 6
HELIX 35 35 GLY C 236 LYS C 249 1 14
HELIX 36 36 PHE C 270 LYS C 284 1 15
HELIX 37 37 ARG C 314 LEU C 318 5 5
HELIX 38 38 SER C 319 GLY C 331 1 13
HELIX 39 39 PRO D 35 GLY D 40 1 6
HELIX 40 40 GLY D 66 GLY D 71 1 6
HELIX 41 41 GLU D 72 VAL D 74 5 3
HELIX 42 42 ASN D 75 ASP D 85 1 11
HELIX 43 43 ASN D 105 SER D 107 5 3
HELIX 44 44 VAL D 108 GLU D 121 1 14
HELIX 45 45 ASN D 137 GLN D 140 5 4
HELIX 46 46 ASN D 141 TYR D 156 1 16
HELIX 47 47 ASP D 179 LYS D 193 1 15
HELIX 48 48 THR D 204 GLN D 209 1 6
HELIX 49 49 VAL D 211 ASP D 216 1 6
HELIX 50 50 GLY D 236 SER D 248 1 13
HELIX 51 51 PHE D 270 LYS D 284 1 15
HELIX 52 52 SER D 319 LEU D 330 1 12
SHEET 1 A 2 SER A 43 LYS A 45 0
SHEET 2 A 2 GLN A 48 VAL A 50 -1 O VAL A 50 N SER A 43
SHEET 1 B 9 LYS A 60 SER A 64 0
SHEET 2 B 9 VAL A 90 TYR A 96 1 O ARG A 92 N SER A 64
SHEET 3 B 9 TYR A 125 HIS A 131 1 O ILE A 127 N ALA A 93
SHEET 4 B 9 VAL A 162 GLU A 165 1 O GLU A 165 N TRP A 130
SHEET 5 B 9 ILE A 200 VAL A 202 1 O ILE A 201 N TYR A 164
SHEET 6 B 9 VAL A 224 TYR A 231 1 O MET A 225 N VAL A 202
SHEET 7 B 9 ILE A 253 GLY A 259 1 O PHE A 254 N TYR A 226
SHEET 8 B 9 TRP A 288 LEU A 293 1 O TRP A 291 N TRP A 258
SHEET 9 B 9 LYS A 60 SER A 64 1 N SER A 63 O LEU A 293
SHEET 1 C 2 SER B 43 LYS B 45 0
SHEET 2 C 2 GLN B 48 VAL B 50 -1 O VAL B 50 N SER B 43
SHEET 1 D 9 LYS B 60 SER B 64 0
SHEET 2 D 9 VAL B 90 TYR B 96 1 O ARG B 92 N SER B 64
SHEET 3 D 9 TYR B 125 HIS B 131 1 O ILE B 127 N ALA B 93
SHEET 4 D 9 VAL B 162 GLU B 165 1 O ILE B 163 N ILE B 128
SHEET 5 D 9 ILE B 200 VAL B 202 1 O ILE B 201 N TYR B 164
SHEET 6 D 9 VAL B 224 TYR B 231 1 O MET B 225 N VAL B 202
SHEET 7 D 9 ILE B 253 GLY B 259 1 O PHE B 254 N TYR B 226
SHEET 8 D 9 TRP B 288 LEU B 293 1 O TRP B 291 N TRP B 258
SHEET 9 D 9 LYS B 60 SER B 64 1 N SER B 63 O ASN B 290
SHEET 1 E 2 SER C 43 LYS C 45 0
SHEET 2 E 2 GLN C 48 VAL C 50 -1 O VAL C 50 N SER C 43
SHEET 1 F 8 ILE C 200 ILE C 201 0
SHEET 2 F 8 VAL C 162 GLU C 165 1 N TYR C 164 O ILE C 201
SHEET 3 F 8 TYR C 125 HIS C 131 1 N ILE C 128 O ILE C 163
SHEET 4 F 8 VAL C 90 TYR C 96 1 N PHE C 91 O TYR C 125
SHEET 5 F 8 LYS C 60 SER C 64 1 N ILE C 62 O ARG C 92
SHEET 6 F 8 TRP C 288 LEU C 293 1 O LEU C 293 N SER C 63
SHEET 7 F 8 ILE C 253 GLY C 259 1 N VAL C 255 O VAL C 289
SHEET 8 F 8 TYR C 226 ALA C 227 1 N TYR C 226 O PHE C 254
SHEET 1 G 8 ILE C 200 ILE C 201 0
SHEET 2 G 8 VAL C 162 GLU C 165 1 N TYR C 164 O ILE C 201
SHEET 3 G 8 TYR C 125 HIS C 131 1 N ILE C 128 O ILE C 163
SHEET 4 G 8 VAL C 90 TYR C 96 1 N PHE C 91 O TYR C 125
SHEET 5 G 8 LYS C 60 SER C 64 1 N ILE C 62 O ARG C 92
SHEET 6 G 8 TRP C 288 LEU C 293 1 O LEU C 293 N SER C 63
SHEET 7 G 8 ILE C 253 GLY C 259 1 N VAL C 255 O VAL C 289
SHEET 8 G 8 PHE C 230 TYR C 231 1 N PHE C 230 O GLY C 259
SHEET 1 H 2 SER D 43 LYS D 45 0
SHEET 2 H 2 GLN D 48 VAL D 50 -1 O VAL D 50 N SER D 43
SHEET 1 I 9 LYS D 60 SER D 63 0
SHEET 2 I 9 PHE D 91 TYR D 96 1 O ARG D 92 N ILE D 62
SHEET 3 I 9 VAL D 126 HIS D 131 1 O ILE D 127 N ALA D 93
SHEET 4 I 9 VAL D 162 GLU D 165 1 O GLU D 165 N ILE D 128
SHEET 5 I 9 ILE D 199 VAL D 202 1 O ILE D 201 N TYR D 164
SHEET 6 I 9 VAL D 224 TYR D 231 1 O MET D 225 N ILE D 200
SHEET 7 I 9 ILE D 253 GLY D 259 1 O PHE D 254 N LEU D 228
SHEET 8 I 9 TRP D 288 ASN D 290 1 O VAL D 289 N VAL D 255
SHEET 9 I 9 LYS D 60 SER D 63 1 N GLY D 61 O ASN D 290
CISPEP 1 TRP A 291 ASN A 292 0 7.62
CISPEP 2 TRP B 291 ASN B 292 0 3.06
CISPEP 3 TRP C 291 ASN C 292 0 -1.11
CISPEP 4 TRP D 291 ASN D 292 0 0.91
CRYST1 155.359 81.080 114.270 90.00 104.29 90.00 C 1 2 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 0.006437 0.000000 0.001639 0.00000
SCALE2 0.000000 0.012333 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009031 0.00000
(ATOM LINES ARE NOT SHOWN.)
END