HEADER LYASE 21-JUL-19 6PVV
TITLE RNASE A IN COMPLEX WITH P5A
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: RIBONUCLEASE PANCREATIC;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: RNASE 1,RNASE A;
COMPND 5 EC: 4.6.1.18
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BOS TAURUS;
SOURCE 3 ORGANISM_COMMON: BOVINE;
SOURCE 4 ORGANISM_TAXID: 9913
KEYWDS RNASE A, NUCLEOTIDE, POLY-PHOSPHATE, LYASE
EXPDTA X-RAY DIFFRACTION
AUTHOR I.W.WINDSOR,S.M.SHEPPARD,C.C.CUMMINS,R.T.RAINES
REVDAT 4 11-OCT-23 6PVV 1 REMARK
REVDAT 3 04-DEC-19 6PVV 1 JRNL
REVDAT 2 13-NOV-19 6PVV 1 JRNL
REVDAT 1 06-NOV-19 6PVV 0
JRNL AUTH S.M.SHEPARD,I.W.WINDSOR,R.T.RAINES,C.C.CUMMINS
JRNL TITL NUCLEOSIDE TETRA- AND PENTAPHOSPHATES PREPARED USING A
JRNL TITL 2 TETRAPHOSPHORYLATION REAGENT ARE POTENT INHIBITORS OF
JRNL TITL 3 RIBONUCLEASE A.
JRNL REF J.AM.CHEM.SOC. V. 141 18400 2019
JRNL REFN ESSN 1520-5126
JRNL PMID 31651164
JRNL DOI 10.1021/JACS.9B09760
REMARK 2
REMARK 2 RESOLUTION. 1.65 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX
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) : 1.65
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.25
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 3 NUMBER OF REFLECTIONS : 27898
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.194
REMARK 3 R VALUE (WORKING SET) : 0.192
REMARK 3 FREE R VALUE : 0.223
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 6.630
REMARK 3 FREE R VALUE TEST SET COUNT : 1849
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 29.2500 - 3.8700 1.00 2113 150 0.1759 0.1797
REMARK 3 2 3.8700 - 3.0700 1.00 2038 145 0.1641 0.1723
REMARK 3 3 3.0700 - 2.6800 1.00 2020 138 0.1853 0.2114
REMARK 3 4 2.6800 - 2.4400 1.00 2034 146 0.1912 0.2943
REMARK 3 5 2.4400 - 2.2600 1.00 1987 144 0.1906 0.2086
REMARK 3 6 2.2600 - 2.1300 1.00 2020 143 0.1918 0.2177
REMARK 3 7 2.1300 - 2.0200 1.00 1990 138 0.1945 0.2583
REMARK 3 8 2.0200 - 1.9300 1.00 1992 145 0.2038 0.2630
REMARK 3 9 1.9300 - 1.8600 1.00 1991 143 0.2163 0.2956
REMARK 3 10 1.8600 - 1.8000 1.00 1979 142 0.2426 0.3183
REMARK 3 11 1.8000 - 1.7400 1.00 2007 140 0.2454 0.3025
REMARK 3 12 1.7400 - 1.6600 1.00 1949 143 0.2435 0.2642
REMARK 3 13 1.6900 - 1.6500 0.95 1929 132 0.2637 0.2743
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) : 0.200
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 22.440
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 17.01
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 25.48
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 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 6PVV COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-JUL-19.
REMARK 100 THE DEPOSITION ID IS D_1000242961.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 18-APR-19
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : SEALED TUBE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : BRUKER IMUS MICROFOCUS
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 : BRUKER PHOTON III
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : SAINT
REMARK 200 DATA SCALING SOFTWARE : SADABS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 27900
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.650
REMARK 200 RESOLUTION RANGE LOW (A) : 29.250
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 200 DATA REDUNDANCY : 12.40
REMARK 200 R MERGE (I) : 0.08600
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 18.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.65
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.71
REMARK 200 COMPLETENESS FOR SHELL (%) : 95.9
REMARK 200 DATA REDUNDANCY IN SHELL : 3.06
REMARK 200 R MERGE FOR SHELL (I) : 0.50300
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.000
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: 1AFU
REMARK 200
REMARK 200 REMARK: PLATES
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 41.74
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.11
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20 MM SODIUM CITRATE, 20% PEG 4000, PH
REMARK 280 5.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K
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 49.89500
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 16.12500
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 49.89500
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 16.12500
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
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 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 303 LIES ON A SPECIAL POSITION.
REMARK 375 HOH B 382 LIES ON A SPECIAL POSITION.
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 OG SER A 59 O HOH A 301 2.03
REMARK 500 O HOH A 301 O HOH B 344 2.04
REMARK 500
REMARK 500 REMARK: NULL
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 NZ LYS B 91 O3B 5FA A 201 3555 1.97
REMARK 500 OG1 THR A 70 OE2 GLU B 111 4546 2.17
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 21 -94.99 -67.38
REMARK 500 ARG A 39 -179.51 -173.29
REMARK 500 HIS A 48 65.05 -101.76
REMARK 500 GLN A 60 -137.44 -102.85
REMARK 500 ASN A 94 67.30 -105.71
REMARK 500 HIS B 48 65.50 -103.03
REMARK 500 GLN B 60 -130.42 -108.77
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 5FA A 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 5FA B 201
DBREF 6PVV A 1 124 UNP P61823 RNAS1_BOVIN 27 150
DBREF 6PVV B 1 124 UNP P61823 RNAS1_BOVIN 27 150
SEQRES 1 A 124 LYS GLU THR ALA ALA ALA LYS PHE GLU ARG GLN HIS MET
SEQRES 2 A 124 ASP SER SER THR SER ALA ALA SER SER SER ASN TYR CYS
SEQRES 3 A 124 ASN GLN MET MET LYS SER ARG ASN LEU THR LYS ASP ARG
SEQRES 4 A 124 CYS LYS PRO VAL ASN THR PHE VAL HIS GLU SER LEU ALA
SEQRES 5 A 124 ASP VAL GLN ALA VAL CYS SER GLN LYS ASN VAL ALA CYS
SEQRES 6 A 124 LYS ASN GLY GLN THR ASN CYS TYR GLN SER TYR SER THR
SEQRES 7 A 124 MET SER ILE THR ASP CYS ARG GLU THR GLY SER SER LYS
SEQRES 8 A 124 TYR PRO ASN CYS ALA TYR LYS THR THR GLN ALA ASN LYS
SEQRES 9 A 124 HIS ILE ILE VAL ALA CYS GLU GLY ASN PRO TYR VAL PRO
SEQRES 10 A 124 VAL HIS PHE ASP ALA SER VAL
SEQRES 1 B 124 LYS GLU THR ALA ALA ALA LYS PHE GLU ARG GLN HIS MET
SEQRES 2 B 124 ASP SER SER THR SER ALA ALA SER SER SER ASN TYR CYS
SEQRES 3 B 124 ASN GLN MET MET LYS SER ARG ASN LEU THR LYS ASP ARG
SEQRES 4 B 124 CYS LYS PRO VAL ASN THR PHE VAL HIS GLU SER LEU ALA
SEQRES 5 B 124 ASP VAL GLN ALA VAL CYS SER GLN LYS ASN VAL ALA CYS
SEQRES 6 B 124 LYS ASN GLY GLN THR ASN CYS TYR GLN SER TYR SER THR
SEQRES 7 B 124 MET SER ILE THR ASP CYS ARG GLU THR GLY SER SER LYS
SEQRES 8 B 124 TYR PRO ASN CYS ALA TYR LYS THR THR GLN ALA ASN LYS
SEQRES 9 B 124 HIS ILE ILE VAL ALA CYS GLU GLY ASN PRO TYR VAL PRO
SEQRES 10 B 124 VAL HIS PHE ASP ALA SER VAL
HET 5FA A 201 39
HET 5FA B 201 39
HETNAM 5FA ADENOSINE-5'-PENTAPHOSPHATE
FORMUL 3 5FA 2(C10 H18 N5 O19 P5)
FORMUL 5 HOH *231(H2 O)
HELIX 1 AA1 THR A 3 MET A 13 1 11
HELIX 2 AA2 ASN A 24 ARG A 33 1 10
HELIX 3 AA3 SER A 50 ALA A 56 1 7
HELIX 4 AA4 VAL A 57 GLN A 60 5 4
HELIX 5 AA5 THR B 3 MET B 13 1 11
HELIX 6 AA6 ASN B 24 ARG B 33 1 10
HELIX 7 AA7 SER B 50 ALA B 56 1 7
HELIX 8 AA8 VAL B 57 GLN B 60 5 4
SHEET 1 AA1 5 VAL A 43 VAL A 47 0
SHEET 2 AA1 5 MET A 79 GLU A 86 -1 O CYS A 84 N ASN A 44
SHEET 3 AA1 5 TYR A 97 GLU A 111 -1 O THR A 100 N ASP A 83
SHEET 4 AA1 5 CYS A 72 GLN A 74 -1 N TYR A 73 O VAL A 108
SHEET 5 AA1 5 LYS A 61 VAL A 63 -1 N LYS A 61 O GLN A 74
SHEET 1 AA2 4 VAL A 43 VAL A 47 0
SHEET 2 AA2 4 MET A 79 GLU A 86 -1 O CYS A 84 N ASN A 44
SHEET 3 AA2 4 TYR A 97 GLU A 111 -1 O THR A 100 N ASP A 83
SHEET 4 AA2 4 VAL A 116 VAL A 124 -1 O VAL A 118 N ALA A 109
SHEET 1 AA3 5 VAL B 43 VAL B 47 0
SHEET 2 AA3 5 MET B 79 GLU B 86 -1 O CYS B 84 N ASN B 44
SHEET 3 AA3 5 TYR B 97 GLU B 111 -1 O THR B 100 N ASP B 83
SHEET 4 AA3 5 CYS B 72 GLN B 74 -1 N TYR B 73 O VAL B 108
SHEET 5 AA3 5 LYS B 61 VAL B 63 -1 N LYS B 61 O GLN B 74
SHEET 1 AA4 4 VAL B 43 VAL B 47 0
SHEET 2 AA4 4 MET B 79 GLU B 86 -1 O CYS B 84 N ASN B 44
SHEET 3 AA4 4 TYR B 97 GLU B 111 -1 O THR B 100 N ASP B 83
SHEET 4 AA4 4 VAL B 116 VAL B 124 -1 O VAL B 118 N ALA B 109
SSBOND 1 CYS A 26 CYS A 84 1555 1555 2.06
SSBOND 2 CYS A 40 CYS A 95 1555 1555 2.02
SSBOND 3 CYS A 58 CYS A 110 1555 1555 2.02
SSBOND 4 CYS A 65 CYS A 72 1555 1555 2.09
SSBOND 5 CYS B 26 CYS B 84 1555 1555 2.06
SSBOND 6 CYS B 40 CYS B 95 1555 1555 2.04
SSBOND 7 CYS B 58 CYS B 110 1555 1555 2.03
SSBOND 8 CYS B 65 CYS B 72 1555 1555 2.05
CISPEP 1 TYR A 92 PRO A 93 0 2.88
CISPEP 2 ASN A 113 PRO A 114 0 6.97
CISPEP 3 TYR B 92 PRO B 93 0 4.81
CISPEP 4 ASN B 113 PRO B 114 0 3.36
SITE 1 AC1 18 LYS A 7 GLN A 11 HIS A 12 LYS A 41
SITE 2 AC1 18 CYS A 65 ASN A 67 GLN A 69 ASN A 71
SITE 3 AC1 18 ALA A 109 GLU A 111 HIS A 119 PHE A 120
SITE 4 AC1 18 HOH A 311 HOH A 321 HOH A 323 HOH A 366
SITE 5 AC1 18 THR B 70 LYS B 91
SITE 1 AC2 18 LYS B 7 GLN B 11 HIS B 12 LYS B 41
SITE 2 AC2 18 CYS B 65 LYS B 66 ASN B 67 GLN B 69
SITE 3 AC2 18 ASN B 71 ALA B 109 GLU B 111 VAL B 118
SITE 4 AC2 18 HIS B 119 PHE B 120 HOH B 301 HOH B 302
SITE 5 AC2 18 HOH B 320 HOH B 340
CRYST1 99.790 32.250 71.950 90.00 90.30 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 0.010021 0.000000 0.000052 0.00000
SCALE2 0.000000 0.031008 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013899 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
