HEADER UNKNOWN FUNCTION 31-JUL-01 1JOV
TITLE CRYSTAL STRUCTURE ANALYSIS OF HI1317
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HI1317;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HAEMOPHILUS INFLUENZAE;
SOURCE 3 ORGANISM_TAXID: 727;
SOURCE 4 GENE: HI1317;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS HYPOTHETICAL PROTEIN, STRUCTURE 2 FUNCTION PROJECT, S2F,
KEYWDS 2 STRUCTURAL GENOMICS, UNKNOWN FUNCTION
EXPDTA X-RAY DIFFRACTION
AUTHOR N.BONANDER,M.TORDOVA,A.J.HOWARD,E.EISENSTEIN,G.GILLILAND,
AUTHOR 2 STRUCTURE 2 FUNCTION PROJECT (S2F)
REVDAT 2 24-FEB-09 1JOV 1 VERSN
REVDAT 1 24-JUN-03 1JOV 0
JRNL AUTH N.BONANDER,M.TORDOVA,A.J.HOWARD,E.EISENSTEIN,
JRNL AUTH 2 G.GILLILAND
JRNL TITL CRYSTAL 1.57-A CRYSTAL STRUCTURE OF HI1317
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 1.57 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.57
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 15.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 94.3
REMARK 3 NUMBER OF REFLECTIONS : 33851
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING + TEST SET) : NULL
REMARK 3 R VALUE (WORKING SET) : 0.208
REMARK 3 FREE R VALUE : 0.260
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2261
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 21
REMARK 3 SOLVENT ATOMS : 235
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 21.40
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 31.50
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.99000
REMARK 3 B22 (A**2) : 3.08000
REMARK 3 B33 (A**2) : -2.01000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.11000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.111
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.116
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.097
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.770
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 DISTANCE RESTRAINTS. RMS SIGMA
REMARK 3 BOND LENGTH (A) : NULL ; NULL
REMARK 3 ANGLE DISTANCE (A) : NULL ; NULL
REMARK 3 INTRAPLANAR 1-4 DISTANCE (A) : NULL ; NULL
REMARK 3 H-BOND OR METAL COORDINATION (A) : NULL ; NULL
REMARK 3
REMARK 3 PLANE RESTRAINT (A) : NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINT (A**3) : NULL ; NULL
REMARK 3
REMARK 3 NON-BONDED CONTACT RESTRAINTS.
REMARK 3 SINGLE TORSION (A) : NULL ; NULL
REMARK 3 MULTIPLE TORSION (A) : NULL ; NULL
REMARK 3 H-BOND (X...Y) (A) : NULL ; NULL
REMARK 3 H-BOND (X-H...Y) (A) : NULL ; NULL
REMARK 3
REMARK 3 CONFORMATIONAL TORSION ANGLE RESTRAINTS.
REMARK 3 SPECIFIED (DEGREES) : NULL ; NULL
REMARK 3 PLANAR (DEGREES) : NULL ; NULL
REMARK 3 STAGGERED (DEGREES) : NULL ; NULL
REMARK 3 TRANSVERSE (DEGREES) : NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1JOV COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 10-AUG-01.
REMARK 100 THE RCSB ID CODE IS RCSB014014.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 115
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 17-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.000
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : BRUKER
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 33851
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.570
REMARK 200 RESOLUTION RANGE LOW (A) : 15.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 94.3
REMARK 200 DATA REDUNDANCY : 6.600
REMARK 200 R MERGE (I) : 0.03100
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 13.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.57
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.61
REMARK 200 COMPLETENESS FOR SHELL (%) : 81.7
REMARK 200 DATA REDUNDANCY IN SHELL : 4.20
REMARK 200 R MERGE FOR SHELL (I) : 0.24000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.100
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 43.40
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.19
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% 4K-PEG, 0.2M LISO4, 0.1 M TRIS
REMARK 280 PH 8.5 , VAPOR DIFFUSION, HANGING DROP
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 40.27000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 19.43000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 40.27000
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 19.43000
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: 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 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 A 539 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 540 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 GLY A 270
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 ARG A 251 CZ ARG A 251 NH1 -0.087
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 ASP A 192 CB - CG - OD2 ANGL. DEV. = 7.6 DEGREES
REMARK 500 MET A 236 CG - SD - CE ANGL. DEV. = 9.8 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 LYS A 7 135.48 -171.10
REMARK 500 ASN A 19 -115.10 54.74
REMARK 500 ALA A 40 53.38 38.88
REMARK 500 ASN A 49 -7.29 83.75
REMARK 500 TYR A 77 140.43 -175.34
REMARK 500 THR A 130 -137.77 -134.82
REMARK 500 GLU A 189 172.27 177.14
REMARK 500 TRP A 229 -113.06 56.90
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 SO4 A 280
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TRS A 300
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TRS A 305
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: HI1317 RELATED DB: TARGETDB
DBREF 1JOV A 1 270 UNP Q9RP27 Q9RP27_HAEIN 1 270
SEQRES 1 A 270 MET LYS THR THR LEU LEU LYS THR LEU THR PRO GLU LEU
SEQRES 2 A 270 HIS LEU VAL GLN HIS ASN ASP ILE PRO VAL LEU HIS LEU
SEQRES 3 A 270 LYS HIS ALA VAL GLY THR ALA LYS ILE SER LEU GLN GLY
SEQRES 4 A 270 ALA GLN LEU ILE SER TRP LYS PRO GLN ASN ALA LYS GLN
SEQRES 5 A 270 ASP VAL LEU TRP LEU SER GLU VAL GLU PRO PHE LYS ASN
SEQRES 6 A 270 GLY ASN ALA ILE ARG GLY GLY VAL PRO ILE CYS TYR PRO
SEQRES 7 A 270 TRP PHE GLY GLY VAL LYS GLN PRO ALA HIS GLY THR ALA
SEQRES 8 A 270 ARG ILE ARG LEU TRP GLN LEU SER HIS TYR TYR ILE SER
SEQRES 9 A 270 VAL HIS LYS VAL ARG LEU GLU PHE GLU LEU PHE SER ASP
SEQRES 10 A 270 LEU ASN ILE ILE GLU ALA LYS VAL SER MET VAL PHE THR
SEQRES 11 A 270 ASP LYS CYS HIS LEU THR PHE THR HIS TYR GLY GLU GLU
SEQRES 12 A 270 SER ALA GLN ALA ALA LEU HIS THR TYR PHE ASN ILE GLY
SEQRES 13 A 270 ASP ILE ASN GLN VAL GLU VAL GLN GLY LEU PRO GLU THR
SEQRES 14 A 270 CYS PHE ASN SER LEU ASN GLN GLN GLN GLU ASN VAL PRO
SEQRES 15 A 270 SER PRO ARG HIS ILE SER GLU ASN VAL ASP CYS ILE TYR
SEQRES 16 A 270 SER ALA GLU ASN MET GLN ASN GLN ILE LEU ASP LYS SER
SEQRES 17 A 270 PHE ASN ARG THR ILE ALA LEU HIS HIS HIS ASN ALA SER
SEQRES 18 A 270 GLN PHE VAL LEU TRP ASN PRO TRP HIS LYS LYS THR SER
SEQRES 19 A 270 GLY MET SER GLU THR GLY TYR GLN LYS MET LEU CYS LEU
SEQRES 20 A 270 GLU THR ALA ARG ILE HIS HIS LEU LEU GLU PHE GLY GLU
SEQRES 21 A 270 SER LEU SER VAL GLU ILE SER LEU LYS GLY
HET SO4 A 280 5
HET TRS A 300 8
HET TRS A 305 8
HETNAM SO4 SULFATE ION
HETNAM TRS 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL
HETSYN TRS TRIS BUFFER
FORMUL 2 SO4 O4 S 2-
FORMUL 3 TRS 2(C4 H12 N O3 1+)
FORMUL 5 HOH *235(H2 O)
HELIX 1 1 PHE A 80 LYS A 84 5 5
HELIX 2 2 THR A 90 ARG A 94 5 5
HELIX 3 3 ASP A 157 ASN A 159 5 3
HELIX 4 4 THR A 239 GLN A 242 5 4
SHEET 1 A 5 THR A 3 THR A 10 0
SHEET 2 A 5 LEU A 13 HIS A 18 -1 O LEU A 13 N THR A 10
SHEET 3 A 5 ILE A 21 HIS A 28 -1 O ILE A 21 N HIS A 18
SHEET 4 A 5 GLY A 31 SER A 36 -1 O GLY A 31 N HIS A 28
SHEET 5 A 5 GLN A 41 PRO A 47 -1 O GLN A 41 N SER A 36
SHEET 1 B 7 GLN A 177 ASN A 180 0
SHEET 2 B 7 THR A 169 ASN A 172 -1 O CYS A 170 N GLU A 179
SHEET 3 B 7 VAL A 191 SER A 196 -1 N ILE A 194 O PHE A 171
SHEET 4 B 7 GLN A 222 ASN A 227 -1 O PHE A 223 N TYR A 195
SHEET 5 B 7 MET A 244 LEU A 256 -1 O CYS A 246 N TRP A 226
SHEET 6 B 7 ALA A 145 LEU A 149 -1 O ALA A 145 N LEU A 256
SHEET 7 B 7 ILE A 75 CYS A 76 -1 N CYS A 76 O ALA A 148
SHEET 1 C 6 GLN A 177 ASN A 180 0
SHEET 2 C 6 THR A 169 ASN A 172 -1 O CYS A 170 N GLU A 179
SHEET 3 C 6 VAL A 191 SER A 196 -1 N ILE A 194 O PHE A 171
SHEET 4 C 6 GLN A 222 ASN A 227 -1 O PHE A 223 N TYR A 195
SHEET 5 C 6 MET A 244 LEU A 256 -1 O CYS A 246 N TRP A 226
SHEET 6 C 6 TYR A 152 ASN A 154 -1 N PHE A 153 O LEU A 245
SHEET 1 D 8 GLN A 97 SER A 104 0
SHEET 2 D 8 LYS A 107 PHE A 115 -1 O LYS A 107 N SER A 104
SHEET 3 D 8 ILE A 121 PHE A 129 -1 N GLU A 122 O LEU A 114
SHEET 4 D 8 CYS A 133 HIS A 139 -1 N HIS A 134 O VAL A 128
SHEET 5 D 8 SER A 261 LYS A 269 -1 O LEU A 262 N PHE A 137
SHEET 6 D 8 ARG A 211 HIS A 218 -1 N THR A 212 O LYS A 269
SHEET 7 D 8 GLN A 201 ASP A 206 -1 O ASN A 202 N LEU A 215
SHEET 8 D 8 VAL A 161 GLN A 164 -1 O GLU A 162 N LEU A 205
SSBOND 1 CYS A 170 CYS A 193 1555 1555 2.05
CISPEP 1 TYR A 77 PRO A 78 0 3.04
CISPEP 2 GLN A 85 PRO A 86 0 0.97
CISPEP 3 SER A 183 PRO A 184 0 6.15
SITE 1 AC1 6 ARG A 70 ARG A 92 HOH A 469 HOH A 470
SITE 2 AC1 6 HOH A 471 HOH A 472
SITE 1 AC2 6 LYS A 46 LYS A 51 GLN A 52 ASP A 53
SITE 2 AC2 6 HOH A 473 HOH A 474
SITE 1 AC3 4 GLN A 201 SER A 234 GLY A 235 HOH A 492
CRYST1 80.540 38.860 92.360 90.00 110.16 90.00 C 1 2 1 4
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 0.012417 0.000000 0.004558 0.00000
SCALE2 0.000000 0.025735 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011533 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
