HEADER HYDROLASE 18-MAR-11 3R4Y
TITLE CRYSTAL STRUCTURE OF ALPHA-NEOAGAROBIOSE HYDROLASE (ALPHA-NABH) FROM
TITLE 2 SACCHAROPHAGUS DEGRADANS 2-40
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GLYCOSYL HYDROLASE FAMILY 32, N TERMINAL;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: ALPHA-NEOAGAROBIOSE HYDROLASE;
COMPND 5 EC: 3.2.1.-;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SACCHAROPHAGUS DEGRADANS;
SOURCE 3 ORGANISM_TAXID: 203122;
SOURCE 4 STRAIN: 2-40;
SOURCE 5 GENE: SDE_2657;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: B834(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PJL
KEYWDS AGAR METABOLISM, NEOAGAROBIOSE, 3, 6-ANHYDRO-L-GALACTOSE, BIOENERGY,
KEYWDS 2 HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR S.LEE,J.Y.LEE,S.C.HA,D.H.SHIN,K.H.KIM,W.G.BANG,S.H.KIM,I.G.CHOI
REVDAT 2 20-MAR-24 3R4Y 1 SEQADV
REVDAT 1 01-FEB-12 3R4Y 0
JRNL AUTH S.C.HA,S.LEE,J.LEE,H.T.KIM,H.J.KO,K.H.KIM,I.G.CHOI
JRNL TITL CRYSTAL STRUCTURE OF A KEY ENZYME IN THE AGAROLYTIC PATHWAY,
JRNL TITL 2 ALPHA-NEOAGAROBIOSE HYDROLASE FROM SACCHAROPHAGUS DEGRADANS
JRNL TITL 3 2-40
JRNL REF BIOCHEM.BIOPHYS.RES.COMMUN. V. 412 238 2011
JRNL REFN ISSN 0006-291X
JRNL PMID 21810409
JRNL DOI 10.1016/J.BBRC.2011.07.073
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.69
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 50502
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.164
REMARK 3 R VALUE (WORKING SET) : 0.161
REMARK 3 FREE R VALUE : 0.206
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2710
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.05
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3331
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 BIN R VALUE (WORKING SET) : 0.1700
REMARK 3 BIN FREE R VALUE SET COUNT : 158
REMARK 3 BIN FREE R VALUE : 0.2410
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5755
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 303
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 23.83
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.06000
REMARK 3 B22 (A**2) : -0.01000
REMARK 3 B33 (A**2) : 0.06000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.03000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.145
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.094
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.279
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.959
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.934
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 5935 ; 0.015 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 8060 ; 1.627 ; 1.931
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 715 ; 7.416 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 297 ;34.977 ;24.141
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 928 ;16.801 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 28 ;19.759 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 805 ; 0.119 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4684 ; 0.006 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 2665 ; 0.207 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 4009 ; 0.318 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 456 ; 0.153 ; 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): 39 ; 0.199 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 9 ; 0.083 ; 0.200
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 3645 ; 1.226 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 5734 ; 1.977 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2683 ; 3.112 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2326 ; 4.725 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3R4Y COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 01-APR-11.
REMARK 100 THE DEPOSITION ID IS D_1000064494.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 20-JAN-09
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 5.0.2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9784
REMARK 200 MONOCHROMATOR : DOUBLE-CRYSTAL, SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 55856
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.980
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.4
REMARK 200 DATA REDUNDANCY : 3.800
REMARK 200 R MERGE (I) : 0.08600
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 25.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.98
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.05
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.1
REMARK 200 DATA REDUNDANCY IN SHELL : 3.90
REMARK 200 R MERGE FOR SHELL (I) : 0.46000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 4.100
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: SOLVE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 52.61
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.60
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 2.4M SODIUM MALONATE, PH 7.0, VAPOR
REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 295K
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 64.93500
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 38.40500
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 64.93500
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 38.40500
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 6340 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 26670 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -35.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH B 421 LIES ON A SPECIAL POSITION.
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 SER A 2
REMARK 465 ASP A 3
REMARK 465 SER A 4
REMARK 465 LYS A 5
REMARK 465 VAL A 6
REMARK 465 ASN A 7
REMARK 465 LYS A 8
REMARK 465 GLU A 317
REMARK 465 SER A 318
REMARK 465 HIS A 371
REMARK 465 HIS A 372
REMARK 465 HIS A 373
REMARK 465 HIS A 374
REMARK 465 MET B 1
REMARK 465 SER B 2
REMARK 465 ASP B 3
REMARK 465 SER B 4
REMARK 465 LYS B 5
REMARK 465 VAL B 6
REMARK 465 ASN B 7
REMARK 465 LYS B 8
REMARK 465 ASP B 319
REMARK 465 SER B 320
REMARK 465 ASP B 321
REMARK 465 HIS B 371
REMARK 465 HIS B 372
REMARK 465 HIS B 373
REMARK 465 HIS B 374
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 GLY B 135 N - CA - C ANGL. DEV. = -15.4 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 ASP A 61 44.32 -97.15
REMARK 500 LYS A 102 -22.96 85.20
REMARK 500 THR A 127 62.89 62.96
REMARK 500 ASN A 134 69.53 39.62
REMARK 500 THR A 186 167.79 70.96
REMARK 500 SER A 229 -153.25 -119.67
REMARK 500 ASN A 231 -161.11 -118.11
REMARK 500 HIS A 264 -101.45 -135.06
REMARK 500 THR A 281 -62.89 79.13
REMARK 500 SER A 320 101.89 139.78
REMARK 500 ASP B 61 34.12 -98.16
REMARK 500 LYS B 102 -15.88 79.02
REMARK 500 THR B 127 60.40 64.81
REMARK 500 THR B 186 179.59 72.68
REMARK 500 SER B 229 -150.99 -122.94
REMARK 500 ASN B 231 -157.63 -117.17
REMARK 500 HIS B 264 -94.94 -132.15
REMARK 500 THR B 281 -58.54 77.67
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 VAL A 59 ASP A 60 -149.82
REMARK 500 ASN A 134 GLY A 135 -57.43
REMARK 500 ASN B 134 GLY B 135 -52.40
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3R4Z RELATED DB: PDB
DBREF 3R4Y A 1 368 UNP Q21HB2 Q21HB2_SACD2 1 368
DBREF 3R4Y B 1 368 UNP Q21HB2 Q21HB2_SACD2 1 368
SEQADV 3R4Y HIS A 369 UNP Q21HB2 EXPRESSION TAG
SEQADV 3R4Y HIS A 370 UNP Q21HB2 EXPRESSION TAG
SEQADV 3R4Y HIS A 371 UNP Q21HB2 EXPRESSION TAG
SEQADV 3R4Y HIS A 372 UNP Q21HB2 EXPRESSION TAG
SEQADV 3R4Y HIS A 373 UNP Q21HB2 EXPRESSION TAG
SEQADV 3R4Y HIS A 374 UNP Q21HB2 EXPRESSION TAG
SEQADV 3R4Y HIS B 369 UNP Q21HB2 EXPRESSION TAG
SEQADV 3R4Y HIS B 370 UNP Q21HB2 EXPRESSION TAG
SEQADV 3R4Y HIS B 371 UNP Q21HB2 EXPRESSION TAG
SEQADV 3R4Y HIS B 372 UNP Q21HB2 EXPRESSION TAG
SEQADV 3R4Y HIS B 373 UNP Q21HB2 EXPRESSION TAG
SEQADV 3R4Y HIS B 374 UNP Q21HB2 EXPRESSION TAG
SEQRES 1 A 374 MET SER ASP SER LYS VAL ASN LYS LYS LEU SER LYS ALA
SEQRES 2 A 374 SER LEU ARG ALA ILE GLU ARG GLY TYR ASP GLU LYS GLY
SEQRES 3 A 374 PRO GLU TRP LEU PHE GLU PHE ASP ILE THR PRO LEU LYS
SEQRES 4 A 374 GLY ASP LEU ALA TYR GLU GLU GLY VAL ILE ARG ARG ASP
SEQRES 5 A 374 PRO SER ALA VAL LEU LYS VAL ASP ASP GLU TYR HIS VAL
SEQRES 6 A 374 TRP TYR THR LYS GLY GLU GLY GLU THR VAL GLY PHE GLY
SEQRES 7 A 374 SER ASP ASN PRO GLU ASP LYS VAL PHE PRO TRP ASP LYS
SEQRES 8 A 374 THR GLU VAL TRP HIS ALA THR SER LYS ASP LYS ILE THR
SEQRES 9 A 374 TRP LYS GLU ILE GLY PRO ALA ILE GLN ARG GLY ALA ALA
SEQRES 10 A 374 GLY ALA TYR ASP ASP ARG ALA VAL PHE THR PRO GLU VAL
SEQRES 11 A 374 LEU ARG HIS ASN GLY THR TYR TYR LEU VAL TYR GLN THR
SEQRES 12 A 374 VAL LYS ALA PRO TYR LEU ASN ARG SER LEU GLU HIS ILE
SEQRES 13 A 374 ALA ILE ALA TYR SER ASP SER PRO PHE GLY PRO TRP THR
SEQRES 14 A 374 LYS SER ASP ALA PRO ILE LEU SER PRO GLU ASN ASP GLY
SEQRES 15 A 374 VAL TRP ASP THR ASP GLU ASP ASN ARG PHE LEU VAL LYS
SEQRES 16 A 374 GLU LYS GLY SER PHE ASP SER HIS LYS VAL HIS ASP PRO
SEQRES 17 A 374 CYS LEU MET PHE PHE ASN ASN ARG PHE TYR LEU TYR TYR
SEQRES 18 A 374 LYS GLY GLU THR MET GLY GLU SER MET ASN MET GLY GLY
SEQRES 19 A 374 ARG GLU ILE LYS HIS GLY VAL ALA ILE ALA ASP SER PRO
SEQRES 20 A 374 LEU GLY PRO TYR THR LYS SER GLU TYR ASN PRO ILE THR
SEQRES 21 A 374 ASN SER GLY HIS GLU VAL ALA VAL TRP PRO TYR LYS GLY
SEQRES 22 A 374 GLY MET ALA THR MET LEU THR THR ASP GLY PRO GLU LYS
SEQRES 23 A 374 ASN THR CYS GLN TRP ALA GLU ASP GLY ILE ASN PHE ASP
SEQRES 24 A 374 ILE MET SER HIS ILE LYS GLY ALA PRO GLU ALA VAL GLY
SEQRES 25 A 374 PHE PHE ARG PRO GLU SER ASP SER ASP ASP PRO ILE SER
SEQRES 26 A 374 GLY ILE GLU TRP GLY LEU SER HIS LYS TYR ASP ALA SER
SEQRES 27 A 374 TRP ASN TRP ASN TYR LEU CYS PHE PHE LYS THR ARG ARG
SEQRES 28 A 374 GLN VAL LEU ASP ALA GLY SER TYR GLN GLN THR GLY ASP
SEQRES 29 A 374 SER GLY ALA VAL HIS HIS HIS HIS HIS HIS
SEQRES 1 B 374 MET SER ASP SER LYS VAL ASN LYS LYS LEU SER LYS ALA
SEQRES 2 B 374 SER LEU ARG ALA ILE GLU ARG GLY TYR ASP GLU LYS GLY
SEQRES 3 B 374 PRO GLU TRP LEU PHE GLU PHE ASP ILE THR PRO LEU LYS
SEQRES 4 B 374 GLY ASP LEU ALA TYR GLU GLU GLY VAL ILE ARG ARG ASP
SEQRES 5 B 374 PRO SER ALA VAL LEU LYS VAL ASP ASP GLU TYR HIS VAL
SEQRES 6 B 374 TRP TYR THR LYS GLY GLU GLY GLU THR VAL GLY PHE GLY
SEQRES 7 B 374 SER ASP ASN PRO GLU ASP LYS VAL PHE PRO TRP ASP LYS
SEQRES 8 B 374 THR GLU VAL TRP HIS ALA THR SER LYS ASP LYS ILE THR
SEQRES 9 B 374 TRP LYS GLU ILE GLY PRO ALA ILE GLN ARG GLY ALA ALA
SEQRES 10 B 374 GLY ALA TYR ASP ASP ARG ALA VAL PHE THR PRO GLU VAL
SEQRES 11 B 374 LEU ARG HIS ASN GLY THR TYR TYR LEU VAL TYR GLN THR
SEQRES 12 B 374 VAL LYS ALA PRO TYR LEU ASN ARG SER LEU GLU HIS ILE
SEQRES 13 B 374 ALA ILE ALA TYR SER ASP SER PRO PHE GLY PRO TRP THR
SEQRES 14 B 374 LYS SER ASP ALA PRO ILE LEU SER PRO GLU ASN ASP GLY
SEQRES 15 B 374 VAL TRP ASP THR ASP GLU ASP ASN ARG PHE LEU VAL LYS
SEQRES 16 B 374 GLU LYS GLY SER PHE ASP SER HIS LYS VAL HIS ASP PRO
SEQRES 17 B 374 CYS LEU MET PHE PHE ASN ASN ARG PHE TYR LEU TYR TYR
SEQRES 18 B 374 LYS GLY GLU THR MET GLY GLU SER MET ASN MET GLY GLY
SEQRES 19 B 374 ARG GLU ILE LYS HIS GLY VAL ALA ILE ALA ASP SER PRO
SEQRES 20 B 374 LEU GLY PRO TYR THR LYS SER GLU TYR ASN PRO ILE THR
SEQRES 21 B 374 ASN SER GLY HIS GLU VAL ALA VAL TRP PRO TYR LYS GLY
SEQRES 22 B 374 GLY MET ALA THR MET LEU THR THR ASP GLY PRO GLU LYS
SEQRES 23 B 374 ASN THR CYS GLN TRP ALA GLU ASP GLY ILE ASN PHE ASP
SEQRES 24 B 374 ILE MET SER HIS ILE LYS GLY ALA PRO GLU ALA VAL GLY
SEQRES 25 B 374 PHE PHE ARG PRO GLU SER ASP SER ASP ASP PRO ILE SER
SEQRES 26 B 374 GLY ILE GLU TRP GLY LEU SER HIS LYS TYR ASP ALA SER
SEQRES 27 B 374 TRP ASN TRP ASN TYR LEU CYS PHE PHE LYS THR ARG ARG
SEQRES 28 B 374 GLN VAL LEU ASP ALA GLY SER TYR GLN GLN THR GLY ASP
SEQRES 29 B 374 SER GLY ALA VAL HIS HIS HIS HIS HIS HIS
FORMUL 3 HOH *303(H2 O)
HELIX 1 1 SER A 11 GLY A 21 1 11
HELIX 2 2 TYR A 22 LYS A 25 5 4
HELIX 3 3 ILE A 324 ILE A 327 5 4
HELIX 4 4 SER B 11 GLY B 21 1 11
HELIX 5 5 TYR B 22 LYS B 25 5 4
HELIX 6 6 ASP B 322 ILE B 327 5 6
HELIX 7 7 THR B 362 SER B 365 5 4
SHEET 1 A 5 GLY A 312 PHE A 313 0
SHEET 2 A 5 TRP A 329 TYR A 335 -1 O LEU A 331 N GLY A 312
SHEET 3 A 5 ASN A 342 ARG A 351 -1 O PHE A 347 N GLY A 330
SHEET 4 A 5 PHE A 31 PRO A 37 -1 N THR A 36 O PHE A 346
SHEET 5 A 5 ALA A 367 HIS A 369 1 O VAL A 368 N PHE A 33
SHEET 1 B 5 LYS A 39 GLY A 40 0
SHEET 2 B 5 THR A 104 ILE A 112 1 O TRP A 105 N LYS A 39
SHEET 3 B 5 GLU A 93 SER A 99 -1 N VAL A 94 O ALA A 111
SHEET 4 B 5 GLU A 62 GLU A 71 -1 N TYR A 63 O SER A 99
SHEET 5 B 5 VAL A 48 ARG A 51 -1 N ILE A 49 O GLY A 70
SHEET 1 C 5 LYS A 39 GLY A 40 0
SHEET 2 C 5 THR A 104 ILE A 112 1 O TRP A 105 N LYS A 39
SHEET 3 C 5 GLU A 93 SER A 99 -1 N VAL A 94 O ALA A 111
SHEET 4 C 5 GLU A 62 GLU A 71 -1 N TYR A 63 O SER A 99
SHEET 5 C 5 LEU A 57 VAL A 59 -1 N VAL A 59 O GLU A 62
SHEET 1 D 4 ALA A 124 HIS A 133 0
SHEET 2 D 4 THR A 136 VAL A 144 -1 O GLN A 142 N PHE A 126
SHEET 3 D 4 HIS A 155 SER A 161 -1 O SER A 161 N TYR A 137
SHEET 4 D 4 THR A 169 LYS A 170 -1 O THR A 169 N TYR A 160
SHEET 1 E 2 VAL A 183 TRP A 184 0
SHEET 2 E 2 VAL A 194 GLU A 196 -1 O LYS A 195 N VAL A 183
SHEET 1 F 4 LYS A 204 PHE A 213 0
SHEET 2 F 4 ARG A 216 GLU A 224 -1 O TYR A 218 N MET A 211
SHEET 3 F 4 ILE A 237 ALA A 244 -1 O LYS A 238 N GLY A 223
SHEET 4 F 4 THR A 252 LYS A 253 -1 O THR A 252 N ILE A 243
SHEET 1 G 2 MET A 230 ASN A 231 0
SHEET 2 G 2 GLY A 234 ARG A 235 -1 O GLY A 234 N ASN A 231
SHEET 1 H 4 VAL A 268 TYR A 271 0
SHEET 2 H 4 GLY A 274 LEU A 279 -1 O ALA A 276 N TRP A 269
SHEET 3 H 4 THR A 288 ALA A 292 -1 O ALA A 292 N MET A 275
SHEET 4 H 4 ASP A 299 HIS A 303 -1 O MET A 301 N CYS A 289
SHEET 1 I 5 GLY B 312 PHE B 313 0
SHEET 2 I 5 TRP B 329 TYR B 335 -1 O LEU B 331 N GLY B 312
SHEET 3 I 5 ASN B 342 ARG B 351 -1 O TYR B 343 N LYS B 334
SHEET 4 I 5 PHE B 31 PRO B 37 -1 N THR B 36 O PHE B 346
SHEET 5 I 5 ALA B 367 HIS B 369 1 O VAL B 368 N ILE B 35
SHEET 1 J 5 LYS B 39 GLY B 40 0
SHEET 2 J 5 THR B 104 ILE B 112 1 O TRP B 105 N LYS B 39
SHEET 3 J 5 GLU B 93 SER B 99 -1 N THR B 98 O LYS B 106
SHEET 4 J 5 GLU B 62 GLU B 71 -1 N TYR B 63 O SER B 99
SHEET 5 J 5 VAL B 48 ARG B 51 -1 N ILE B 49 O GLY B 70
SHEET 1 K 5 LYS B 39 GLY B 40 0
SHEET 2 K 5 THR B 104 ILE B 112 1 O TRP B 105 N LYS B 39
SHEET 3 K 5 GLU B 93 SER B 99 -1 N THR B 98 O LYS B 106
SHEET 4 K 5 GLU B 62 GLU B 71 -1 N TYR B 63 O SER B 99
SHEET 5 K 5 LEU B 57 VAL B 59 -1 N VAL B 59 O GLU B 62
SHEET 1 L 4 ALA B 124 HIS B 133 0
SHEET 2 L 4 THR B 136 VAL B 144 -1 O GLN B 142 N PHE B 126
SHEET 3 L 4 HIS B 155 SER B 161 -1 O SER B 161 N TYR B 137
SHEET 4 L 4 THR B 169 LYS B 170 -1 O THR B 169 N TYR B 160
SHEET 1 M 2 VAL B 183 TRP B 184 0
SHEET 2 M 2 VAL B 194 GLU B 196 -1 O LYS B 195 N VAL B 183
SHEET 1 N 4 LYS B 204 PHE B 213 0
SHEET 2 N 4 ARG B 216 GLU B 224 -1 O TYR B 218 N MET B 211
SHEET 3 N 4 ILE B 237 ALA B 244 -1 O ALA B 242 N LEU B 219
SHEET 4 N 4 THR B 252 LYS B 253 -1 O THR B 252 N ILE B 243
SHEET 1 O 2 MET B 230 ASN B 231 0
SHEET 2 O 2 GLY B 234 ARG B 235 -1 O GLY B 234 N ASN B 231
SHEET 1 P 4 VAL B 268 TYR B 271 0
SHEET 2 P 4 GLY B 274 LEU B 279 -1 O ALA B 276 N TRP B 269
SHEET 3 P 4 THR B 288 ALA B 292 -1 O ALA B 292 N MET B 275
SHEET 4 P 4 ASP B 299 HIS B 303 -1 O MET B 301 N CYS B 289
CISPEP 1 ASP A 60 ASP A 61 0 -3.00
CISPEP 2 ALA A 146 PRO A 147 0 -1.70
CISPEP 3 GLY A 166 PRO A 167 0 -0.21
CISPEP 4 GLY A 249 PRO A 250 0 1.54
CISPEP 5 ASN A 257 PRO A 258 0 -4.34
CISPEP 6 ASP A 319 SER A 320 0 -15.98
CISPEP 7 ASP B 60 ASP B 61 0 5.04
CISPEP 8 ALA B 146 PRO B 147 0 -2.38
CISPEP 9 GLY B 166 PRO B 167 0 -4.01
CISPEP 10 GLY B 249 PRO B 250 0 7.62
CISPEP 11 ASN B 257 PRO B 258 0 -4.67
CRYST1 129.870 76.810 90.110 90.00 101.86 90.00 C 1 2 1 8
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 0.007692 0.000000 0.001635 0.00000
SCALE2 0.000000 0.012987 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011359 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
