HEADER HYDROLASE 02-NOV-16 5M9T
TITLE HUMAN ANGIOGENIN ALS VARIANT H114R
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ANGIOGENIN;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: RIBONUCLEASE 5,RNASE 5;
COMPND 5 EC: 3.1.27.-;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: ANG, RNASE5;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008
KEYWDS ALS, RNASE, ANGIOGENESIS, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR W.J.BRADSHAW,S.REHMAN,T.T.K.PHAM,N.THIYAGARAJAN,R.L.LEE,
AUTHOR 2 V.SUBRAMANIAN,K.R.ACHARYA
REVDAT 2 17-JAN-24 5M9T 1 REMARK
REVDAT 1 22-FEB-17 5M9T 0
JRNL AUTH W.J.BRADSHAW,S.REHMAN,T.T.PHAM,N.THIYAGARAJAN,R.L.LEE,
JRNL AUTH 2 V.SUBRAMANIAN,K.R.ACHARYA
JRNL TITL STRUCTURAL INSIGHTS INTO HUMAN ANGIOGENIN VARIANTS
JRNL TITL 2 IMPLICATED IN PARKINSON'S DISEASE AND AMYOTROPHIC LATERAL
JRNL TITL 3 SCLEROSIS.
JRNL REF SCI REP V. 7 41996 2017
JRNL REFN ESSN 2045-2322
JRNL PMID 28176817
JRNL DOI 10.1038/SREP41996
REMARK 2
REMARK 2 RESOLUTION. 2.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0151
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 70.50
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 95.7
REMARK 3 NUMBER OF REFLECTIONS : 15455
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) : 0.186
REMARK 3 R VALUE (WORKING SET) : 0.182
REMARK 3 FREE R VALUE : 0.236
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.800
REMARK 3 FREE R VALUE TEST SET COUNT : 955
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) : 2.20
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.26
REMARK 3 REFLECTION IN BIN (WORKING SET) : 845
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 74.59
REMARK 3 BIN R VALUE (WORKING SET) : 0.2930
REMARK 3 BIN FREE R VALUE SET COUNT : 68
REMARK 3 BIN FREE R VALUE : 0.2900
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1962
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 11
REMARK 3 SOLVENT ATOMS : 67
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 49.75
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.12000
REMARK 3 B22 (A**2) : 1.12000
REMARK 3 B33 (A**2) : -3.62000
REMARK 3 B12 (A**2) : 0.56000
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): 0.222
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.196
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.156
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.470
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.962
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.931
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2050 ; 0.011 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 1929 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2766 ; 1.598 ; 1.929
REMARK 3 BOND ANGLES OTHERS (DEGREES): 4419 ; 0.976 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 249 ; 6.991 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 110 ;33.590 ;22.000
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 356 ;16.073 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 29 ;17.276 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 283 ; 0.123 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2341 ; 0.006 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 544 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
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): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
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): 978 ; 3.338 ; 4.671
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 977 ; 3.318 ; 4.669
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1221 ; 5.288 ; 6.988
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 1222 ; 5.289 ; 6.992
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1072 ; 3.851 ; 5.195
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 1069 ; 3.838 ; 5.190
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 1539 ; 6.273 ; 7.593
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 2222 ; 8.879 ;53.464
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 2216 ; 8.887 ;53.437
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 : NULL
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 5M9T COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 02-NOV-16.
REMARK 100 THE DEPOSITION ID IS D_1200002163.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 11-FEB-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : I03
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9763
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M-F
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DIALS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 16435
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.200
REMARK 200 RESOLUTION RANGE LOW (A) : 70.500
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.8
REMARK 200 DATA REDUNDANCY : 9.500
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 12.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.27
REMARK 200 COMPLETENESS FOR SHELL (%) : 75.9
REMARK 200 DATA REDUNDANCY IN SHELL : 3.60
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.800
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: 1ANG
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 57.19
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.87
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.01 M NA BORATE 1.1 M NA CITRATE, PH
REMARK 280 8.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 289K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1
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 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+1/3
REMARK 290 6555 -X,-X+Y,-Z+2/3
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 57.32333
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 28.66167
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 28.66167
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 57.32333
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 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 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 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 0
REMARK 465 MET B 0
REMARK 465 GLN B 1
REMARK 465 ASP B 2
REMARK 465 PRO B 123
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 ARG A 66 -144.36 48.09
REMARK 500 ASN A 68 35.27 -152.97
REMARK 500 PRO A 90 157.17 -48.96
REMARK 500 ARG B 21 33.22 -143.94
REMARK 500 ARG B 66 -117.54 2.41
REMARK 500 ARG B 66 -116.51 0.47
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 GOL A 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BO4 A 202
DBREF 5M9T A 1 123 UNP P03950 ANGI_HUMAN 25 147
DBREF 5M9T B 1 123 UNP P03950 ANGI_HUMAN 25 147
SEQADV 5M9T MET A 0 UNP P03950 INITIATING METHIONINE
SEQADV 5M9T ARG A 114 UNP P03950 HIS 138 ENGINEERED MUTATION
SEQADV 5M9T MET B 0 UNP P03950 INITIATING METHIONINE
SEQADV 5M9T ARG B 114 UNP P03950 HIS 138 ENGINEERED MUTATION
SEQRES 1 A 124 MET GLN ASP ASN SER ARG TYR THR HIS PHE LEU THR GLN
SEQRES 2 A 124 HIS TYR ASP ALA LYS PRO GLN GLY ARG ASP ASP ARG TYR
SEQRES 3 A 124 CYS GLU SER ILE MET ARG ARG ARG GLY LEU THR SER PRO
SEQRES 4 A 124 CYS LYS ASP ILE ASN THR PHE ILE HIS GLY ASN LYS ARG
SEQRES 5 A 124 SER ILE LYS ALA ILE CYS GLU ASN LYS ASN GLY ASN PRO
SEQRES 6 A 124 HIS ARG GLU ASN LEU ARG ILE SER LYS SER SER PHE GLN
SEQRES 7 A 124 VAL THR THR CYS LYS LEU HIS GLY GLY SER PRO TRP PRO
SEQRES 8 A 124 PRO CYS GLN TYR ARG ALA THR ALA GLY PHE ARG ASN VAL
SEQRES 9 A 124 VAL VAL ALA CYS GLU ASN GLY LEU PRO VAL ARG LEU ASP
SEQRES 10 A 124 GLN SER ILE PHE ARG ARG PRO
SEQRES 1 B 124 MET GLN ASP ASN SER ARG TYR THR HIS PHE LEU THR GLN
SEQRES 2 B 124 HIS TYR ASP ALA LYS PRO GLN GLY ARG ASP ASP ARG TYR
SEQRES 3 B 124 CYS GLU SER ILE MET ARG ARG ARG GLY LEU THR SER PRO
SEQRES 4 B 124 CYS LYS ASP ILE ASN THR PHE ILE HIS GLY ASN LYS ARG
SEQRES 5 B 124 SER ILE LYS ALA ILE CYS GLU ASN LYS ASN GLY ASN PRO
SEQRES 6 B 124 HIS ARG GLU ASN LEU ARG ILE SER LYS SER SER PHE GLN
SEQRES 7 B 124 VAL THR THR CYS LYS LEU HIS GLY GLY SER PRO TRP PRO
SEQRES 8 B 124 PRO CYS GLN TYR ARG ALA THR ALA GLY PHE ARG ASN VAL
SEQRES 9 B 124 VAL VAL ALA CYS GLU ASN GLY LEU PRO VAL ARG LEU ASP
SEQRES 10 B 124 GLN SER ILE PHE ARG ARG PRO
HET GOL A 201 6
HET BO4 A 202 5
HETNAM GOL GLYCEROL
HETNAM BO4 BORATE ION
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 3 GOL C3 H8 O3
FORMUL 4 BO4 B H4 O4 1-
FORMUL 5 HOH *67(H2 O)
HELIX 1 AA1 SER A 4 TYR A 14 1 11
HELIX 2 AA2 ASP A 22 ARG A 33 1 12
HELIX 3 AA3 ASN A 49 ALA A 55 1 7
HELIX 4 AA4 ILE A 56 GLU A 58 5 3
HELIX 5 AA5 GLN A 117 ARG A 121 5 5
HELIX 6 AA6 SER B 4 TYR B 14 1 11
HELIX 7 AA7 ASP B 22 ARG B 33 1 12
HELIX 8 AA8 ASN B 49 ALA B 55 1 7
HELIX 9 AA9 ILE B 56 GLU B 58 5 3
HELIX 10 AB1 GLN B 117 ARG B 122 5 6
SHEET 1 AA1 3 ILE A 42 ILE A 46 0
SHEET 2 AA1 3 PHE A 76 LEU A 83 -1 O CYS A 81 N ASN A 43
SHEET 3 AA1 3 TYR A 94 ARG A 101 -1 O GLY A 99 N VAL A 78
SHEET 1 AA2 4 GLY A 62 HIS A 65 0
SHEET 2 AA2 4 LEU A 69 SER A 72 -1 O ILE A 71 N ASN A 63
SHEET 3 AA2 4 VAL A 104 GLU A 108 -1 O VAL A 105 N ARG A 70
SHEET 4 AA2 4 LEU A 111 LEU A 115 -1 O VAL A 113 N ALA A 106
SHEET 1 AA3 3 ILE B 42 ILE B 46 0
SHEET 2 AA3 3 PHE B 76 HIS B 84 -1 O CYS B 81 N ASN B 43
SHEET 3 AA3 3 GLN B 93 ARG B 101 -1 O GLY B 99 N VAL B 78
SHEET 1 AA4 4 GLY B 62 HIS B 65 0
SHEET 2 AA4 4 LEU B 69 SER B 72 -1 O ILE B 71 N ASN B 63
SHEET 3 AA4 4 VAL B 104 GLU B 108 -1 O VAL B 105 N ARG B 70
SHEET 4 AA4 4 LEU B 111 LEU B 115 -1 O VAL B 113 N ALA B 106
SSBOND 1 CYS A 26 CYS A 81 1555 1555 2.12
SSBOND 2 CYS A 39 CYS A 92 1555 1555 2.05
SSBOND 3 CYS A 57 CYS A 107 1555 1555 2.08
SSBOND 4 CYS B 26 CYS B 81 1555 1555 2.11
SSBOND 5 CYS B 39 CYS B 92 1555 1555 2.03
SSBOND 6 CYS B 57 CYS B 107 1555 1555 2.06
CISPEP 1 SER A 37 PRO A 38 0 -3.36
CISPEP 2 PRO A 90 PRO A 91 0 -3.19
CISPEP 3 SER B 37 PRO B 38 0 -8.61
CISPEP 4 PRO B 90 PRO B 91 0 -1.02
SITE 1 AC1 3 ASN A 49 LYS A 50 ARG A 51
SITE 1 AC2 2 LYS A 73 ARG B 21
CRYST1 81.426 81.426 85.985 90.00 90.00 120.00 P 32 2 1 12
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 0.012281 0.007091 0.000000 0.00000
SCALE2 0.000000 0.014181 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011630 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
