HEADER COMPLEX (ENZYME/INHIBITOR) 14-NOV-97 1AY7
TITLE RIBONUCLEASE SA COMPLEX WITH BARSTAR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GUANYL-SPECIFIC RIBONUCLEASE SA;
COMPND 3 CHAIN: A;
COMPND 4 EC: 3.1.27.3;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: BARSTAR;
COMPND 8 CHAIN: B;
COMPND 9 ENGINEERED: YES;
COMPND 10 OTHER_DETAILS: BARNASE INHIBITOR
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: STREPTOMYCES AUREOFACIENS;
SOURCE 3 ORGANISM_TAXID: 1894;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: XL1-BLUE;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: PMT1126;
SOURCE 8 MOL_ID: 2;
SOURCE 9 ORGANISM_SCIENTIFIC: BACILLUS AMYLOLIQUEFACIENS;
SOURCE 10 ORGANISM_TAXID: 1390;
SOURCE 11 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 12 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 13 EXPRESSION_SYSTEM_STRAIN: XL1-BLUE;
SOURCE 14 EXPRESSION_SYSTEM_PLASMID: PMT1126
KEYWDS RIBONUCLEASE, INHIBITOR, STREPTOMYCES AUREOFACIENS, COMPLEX (ENZYME-
KEYWDS 2 INHIBITOR), COMPLEX (ENZYME-INHIBITOR) COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR J.SEVCIK,L.URBANIKOVA,Z.DAUTER,K.S.WILSON
REVDAT 4 02-AUG-23 1AY7 1 REMARK SEQADV
REVDAT 3 24-FEB-09 1AY7 1 VERSN
REVDAT 2 20-APR-99 1AY7 3 COMPND REMARK HETATM JRNL
REVDAT 2 2 3 KEYWDS
REVDAT 1 02-MAR-99 1AY7 0
JRNL AUTH J.SEVCIK,L.URBANIKOVA,Z.DAUTER,K.S.WILSON
JRNL TITL RECOGNITION OF RNASE SA BY THE INHIBITOR BARSTAR: STRUCTURE
JRNL TITL 2 OF THE COMPLEX AT 1.7 A RESOLUTION.
JRNL REF ACTA CRYSTALLOGR.,SECT.D V. 54 954 1998
JRNL REFN ISSN 0907-4449
JRNL PMID 9757110
JRNL DOI 10.1107/S0907444998004429
REMARK 2
REMARK 2 RESOLUTION. 1.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 25.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 27352
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : FREE R
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.162
REMARK 3 R VALUE (WORKING SET) : 0.160
REMARK 3 FREE R VALUE : 0.190
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2739
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1466
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 190
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 20.00
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 24.80
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 23.80000
REMARK 3 B22 (A**2) : 23.80000
REMARK 3 B33 (A**2) : 21.80000
REMARK 3 B12 (A**2) : 3.50000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): NULL
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): NULL
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 DISTANCE RESTRAINTS. RMS SIGMA
REMARK 3 BOND LENGTH (A) : 0.025 ; 0.020
REMARK 3 ANGLE DISTANCE (A) : 0.040 ; 0.040
REMARK 3 INTRAPLANAR 1-4 DISTANCE (A) : 0.089 ; 0.050
REMARK 3 H-BOND OR METAL COORDINATION (A) : NULL ; NULL
REMARK 3
REMARK 3 PLANE RESTRAINT (A) : 0.035 ; 0.040
REMARK 3 CHIRAL-CENTER RESTRAINT (A**3) : 0.257 ; 0.150
REMARK 3
REMARK 3 NON-BONDED CONTACT RESTRAINTS.
REMARK 3 SINGLE TORSION (A) : 0.187 ; 0.300
REMARK 3 MULTIPLE TORSION (A) : 0.264 ; 0.300
REMARK 3 H-BOND (X...Y) (A) : 0.143 ; 0.300
REMARK 3 H-BOND (X-H...Y) (A) : 0.143 ; 0.300
REMARK 3
REMARK 3 CONFORMATIONAL TORSION ANGLE RESTRAINTS.
REMARK 3 SPECIFIED (DEGREES) : NULL ; NULL
REMARK 3 PLANAR (DEGREES) : 12.800; 7.000
REMARK 3 STAGGERED (DEGREES) : 17.000; 15.000
REMARK 3 TRANSVERSE (DEGREES) : 23.500; 20.000
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 2.900 ; 3.000
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 4.200 ; 5.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 5.500 ; 6.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 7.400 ; 8.000
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: ESTIMATED COORDINATE ERROR. ESD FROM
REMARK 3 CRUICKSHANK (A) : 0.078 ESD FROM SIGMAA (A) : 0.061
REMARK 4
REMARK 4 1AY7 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000171400.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NOV-96
REMARK 200 TEMPERATURE (KELVIN) : 293
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : EMBL/DESY, HAMBURG
REMARK 200 BEAMLINE : X31
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.95
REMARK 200 MONOCHROMATOR : SI(111)
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 27413
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.700
REMARK 200 RESOLUTION RANGE LOW (A) : 25.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 4.700
REMARK 200 R MERGE (I) : 0.04600
REMARK 200 R SYM (I) : 0.04600
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 27.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.72
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.8
REMARK 200 DATA REDUNDANCY IN SHELL : 4.20
REMARK 200 R MERGE FOR SHELL (I) : 0.30800
REMARK 200 R SYM FOR SHELL (I) : 0.30800
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.700
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: PDB ENTRY 1BRS
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 69.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.35
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 7.0
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 65
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+1/6
REMARK 290 6555 X-Y,X,Z+5/6
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 90.53333
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 45.26667
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 67.90000
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 22.63333
REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 113.16667
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 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 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH A 188 O HOH A 219 6554 2.18
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 TYR A 30 CB - CG - CD1 ANGL. DEV. = -5.8 DEGREES
REMARK 500 ASP A 33 CB - CG - OD1 ANGL. DEV. = 5.9 DEGREES
REMARK 500 ASP A 33 CB - CG - OD2 ANGL. DEV. = -7.0 DEGREES
REMARK 500 PHE A 37 CB - CG - CD1 ANGL. DEV. = -6.1 DEGREES
REMARK 500 PHE A 37 CG - CD1 - CE1 ANGL. DEV. = -6.6 DEGREES
REMARK 500 ARG A 40 NE - CZ - NH2 ANGL. DEV. = -4.0 DEGREES
REMARK 500 TYR A 49 CB - CG - CD2 ANGL. DEV. = -6.1 DEGREES
REMARK 500 TYR A 51 CB - CG - CD1 ANGL. DEV. = -5.3 DEGREES
REMARK 500 TYR A 52 CG - CD1 - CE1 ANGL. DEV. = -5.5 DEGREES
REMARK 500 TYR A 55 CB - CG - CD2 ANGL. DEV. = -3.9 DEGREES
REMARK 500 ARG A 68 CG - CD - NE ANGL. DEV. = -14.7 DEGREES
REMARK 500 ARG A 68 NE - CZ - NH1 ANGL. DEV. = 5.3 DEGREES
REMARK 500 GLN A 77 CA - CB - CG ANGL. DEV. = -13.7 DEGREES
REMARK 500 TYR A 81 CB - CG - CD2 ANGL. DEV. = -3.6 DEGREES
REMARK 500 TYR A 81 CG - CD2 - CE2 ANGL. DEV. = -6.1 DEGREES
REMARK 500 ASP A 84 CB - CG - OD2 ANGL. DEV. = 7.5 DEGREES
REMARK 500 PHE A 89 CB - CG - CD1 ANGL. DEV. = -6.0 DEGREES
REMARK 500 ASP A 93 CB - CG - OD2 ANGL. DEV. = -8.4 DEGREES
REMARK 500 LYS B 1 O - C - N ANGL. DEV. = 10.8 DEGREES
REMARK 500 ARG B 11 NE - CZ - NH2 ANGL. DEV. = -3.4 DEGREES
REMARK 500 SER B 12 CA - CB - OG ANGL. DEV. = 17.0 DEGREES
REMARK 500 ASP B 15 CB - CG - OD2 ANGL. DEV. = -8.1 DEGREES
REMARK 500 TYR B 30 CB - CG - CD2 ANGL. DEV. = 5.8 DEGREES
REMARK 500 TYR B 30 CB - CG - CD1 ANGL. DEV. = -5.1 DEGREES
REMARK 500 GLY B 31 O - C - N ANGL. DEV. = -10.4 DEGREES
REMARK 500 GLU B 46 OE1 - CD - OE2 ANGL. DEV. = 7.8 DEGREES
REMARK 500 TYR B 47 CB - CG - CD1 ANGL. DEV. = -4.6 DEGREES
REMARK 500 ARG B 54 NE - CZ - NH1 ANGL. DEV. = -3.2 DEGREES
REMARK 500 ARG B 75 NE - CZ - NH2 ANGL. DEV. = -4.2 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 SER A 3 56.09 -95.52
REMARK 500 TRP B 44 -42.22 -157.22
REMARK 500 GLN B 61 -80.58 -57.56
REMARK 500 LEU B 62 -39.98 -37.90
REMARK 500 ASN B 65 32.14 76.80
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 ASN B 65 GLY B 66 148.57
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 SER A 3 17.56
REMARK 500 GLY A 26 14.07
REMARK 500 PHE A 28 -15.93
REMARK 500 TYR A 30 10.93
REMARK 500 SER A 42 -13.60
REMARK 500 TYR A 55 10.22
REMARK 500 GLY A 61 10.56
REMARK 500 ALA A 75 13.20
REMARK 500 GLY B 43 13.08
REMARK 500 TYR B 47 16.59
REMARK 500 THR B 63 13.01
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1AY7 A 1 96 UNP P05798 RNSA_STRAU 1 96
DBREF 1AY7 B 1 89 UNP P11540 BARS_BACAM 1 89
SEQADV 1AY7 THR A 72 UNP P05798 CYS 72 CONFLICT
SEQRES 1 A 96 ASP VAL SER GLY THR VAL CYS LEU SER ALA LEU PRO PRO
SEQRES 2 A 96 GLU ALA THR ASP THR LEU ASN LEU ILE ALA SER ASP GLY
SEQRES 3 A 96 PRO PHE PRO TYR SER GLN ASP GLY VAL VAL PHE GLN ASN
SEQRES 4 A 96 ARG GLU SER VAL LEU PRO THR GLN SER TYR GLY TYR TYR
SEQRES 5 A 96 HIS GLU TYR THR VAL ILE THR PRO GLY ALA ARG THR ARG
SEQRES 6 A 96 GLY THR ARG ARG ILE ILE THR GLY GLU ALA THR GLN GLU
SEQRES 7 A 96 ASP TYR TYR THR GLY ASP HIS TYR ALA THR PHE SER LEU
SEQRES 8 A 96 ILE ASP GLN THR CYS
SEQRES 1 B 89 LYS LYS ALA VAL ILE ASN GLY GLU GLN ILE ARG SER ILE
SEQRES 2 B 89 SER ASP LEU HIS GLN THR LEU LYS LYS GLU LEU ALA LEU
SEQRES 3 B 89 PRO GLU TYR TYR GLY GLU ASN LEU ASP ALA LEU TRP ASP
SEQRES 4 B 89 CYS LEU THR GLY TRP VAL GLU TYR PRO LEU VAL LEU GLU
SEQRES 5 B 89 TRP ARG GLN PHE GLU GLN SER LYS GLN LEU THR GLU ASN
SEQRES 6 B 89 GLY ALA GLU SER VAL LEU GLN VAL PHE ARG GLU ALA LYS
SEQRES 7 B 89 ALA GLU GLY CYS ASP ILE THR ILE ILE LEU SER
FORMUL 3 HOH *190(H2 O)
HELIX 1 1 LEU A 8 ALA A 10 5 3
HELIX 2 2 PRO A 13 ALA A 23 1 11
HELIX 3 3 GLY B 7 GLN B 9 5 3
HELIX 4 4 ILE B 13 GLU B 23 1 11
HELIX 5 5 LEU B 34 GLY B 43 1 10
HELIX 6 6 PHE B 56 THR B 63 1 8
HELIX 7 7 GLY B 66 GLU B 80 1 15
SHEET 1 A 2 THR A 5 CYS A 7 0
SHEET 2 A 2 LEU A 91 ASP A 93 1 N LEU A 91 O VAL A 6
SHEET 1 B 3 HIS A 53 THR A 56 0
SHEET 2 B 3 ARG A 69 THR A 72 -1 N THR A 72 O HIS A 53
SHEET 3 B 3 ASP A 79 THR A 82 -1 N THR A 82 O ARG A 69
SHEET 1 C 3 LYS B 2 ASN B 6 0
SHEET 2 C 3 LEU B 49 ARG B 54 1 N VAL B 50 O ALA B 3
SHEET 3 C 3 ILE B 84 LEU B 88 1 N THR B 85 O LEU B 49
SSBOND 1 CYS A 7 CYS A 96 1555 1555 2.04
CISPEP 1 GLY A 26 PRO A 27 0 21.35
CISPEP 2 TYR B 47 PRO B 48 0 24.92
CRYST1 56.950 56.950 135.800 90.00 90.00 120.00 P 65 6
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 0.017559 0.010138 0.000000 0.00000
SCALE2 0.000000 0.020276 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007364 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
