HEADER IMMUNE SYSTEM 21-FEB-17 5N7W
TITLE COMPUTATIONALLY DESIGNED FUNCTIONAL ANTIBODY
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ANTIBODY FRAGMENT HEAVY CHAIN;
COMPND 3 CHAIN: A, H;
COMPND 4 ENGINEERED: YES;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: ANTIBODY FRAGMENT LIGHT CHAIN;
COMPND 7 CHAIN: B, L;
COMPND 8 ENGINEERED: YES;
COMPND 9 MOL_ID: 3;
COMPND 10 MOLECULE: INTERLEUKIN-17A;
COMPND 11 CHAIN: X, Y;
COMPND 12 SYNONYM: IL-17A,CYTOTOXIC T-LYMPHOCYTE-ASSOCIATED ANTIGEN 8,CTLA-8;
COMPND 13 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;
SOURCE 6 EXPRESSION_SYSTEM_COMMON: CHINESE HAMSTER;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 10029;
SOURCE 8 MOL_ID: 2;
SOURCE 9 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 10 ORGANISM_COMMON: HUMAN;
SOURCE 11 ORGANISM_TAXID: 9606;
SOURCE 12 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;
SOURCE 13 EXPRESSION_SYSTEM_COMMON: CHINESE HAMSTER;
SOURCE 14 EXPRESSION_SYSTEM_TAXID: 10029;
SOURCE 15 MOL_ID: 3;
SOURCE 16 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 17 ORGANISM_COMMON: HUMAN;
SOURCE 18 ORGANISM_TAXID: 9606;
SOURCE 19 GENE: IL17A, CTLA8, IL17;
SOURCE 20 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;
SOURCE 21 EXPRESSION_SYSTEM_COMMON: CHINESE HAMSTER;
SOURCE 22 EXPRESSION_SYSTEM_TAXID: 10029
KEYWDS COMPUTATIONALLY DESIGNED ANTIBODY IL17, IMMUNE SYSTEM
EXPDTA X-RAY DIFFRACTION
AUTHOR D.HARGREAVES,J.BREED
REVDAT 3 05-DEC-18 5N7W 1 JRNL
REVDAT 2 21-NOV-18 5N7W 1 JRNL
REVDAT 1 14-NOV-18 5N7W 0
JRNL AUTH G.NIMROD,S.FISCHMAN,M.AUSTIN,A.HERMAN,F.KEYES,O.LEIDERMAN,
JRNL AUTH 2 D.HARGREAVES,M.STRAJBL,J.BREED,S.KLOMPUS,K.MINTON,J.SPOONER,
JRNL AUTH 3 A.BUCHANAN,T.J.VAUGHAN,Y.OFRAN
JRNL TITL COMPUTATIONAL DESIGN OF EPITOPE-SPECIFIC FUNCTIONAL
JRNL TITL 2 ANTIBODIES.
JRNL REF CELL REP V. 25 2121 2018
JRNL REFN ESSN 2211-1247
JRNL PMID 30463010
JRNL DOI 10.1016/J.CELREP.2018.10.081
REMARK 2
REMARK 2 RESOLUTION. 1.96 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0135
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) : 1.96
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 75.87
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.4
REMARK 3 NUMBER OF REFLECTIONS : 82363
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) : 0.202
REMARK 3 R VALUE (WORKING SET) : 0.199
REMARK 3 FREE R VALUE : 0.250
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT : 4249
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) : 1.96
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.01
REMARK 3 REFLECTION IN BIN (WORKING SET) : 4714
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 74.07
REMARK 3 BIN R VALUE (WORKING SET) : 0.3660
REMARK 3 BIN FREE R VALUE SET COUNT : 254
REMARK 3 BIN FREE R VALUE : 0.3950
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 8244
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 678
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 52.53
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 3.13000
REMARK 3 B22 (A**2) : -2.67000
REMARK 3 B33 (A**2) : -0.42000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.15000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.176
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.166
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.154
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.898
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.963
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.942
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 8485 ; 0.016 ; 0.020
REMARK 3 BOND LENGTHS OTHERS (A): 7724 ; 0.006 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 11582 ; 1.842 ; 1.941
REMARK 3 BOND ANGLES OTHERS (DEGREES): 17885 ; 1.390 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1061 ; 7.389 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 336 ;33.370 ;24.077
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1310 ;15.653 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 34 ;17.880 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1280 ; 0.117 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 9542 ; 0.010 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 1914 ; 0.006 ; 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): 4271 ; 4.760 ; 5.113
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 4270 ; 4.759 ; 5.112
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 5323 ; 6.741 ; 7.644
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 5324 ; 6.740 ; 7.645
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 4214 ; 5.047 ; 5.411
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 4215 ; 5.046 ; 5.412
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 6260 ; 7.315 ; 7.961
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 9478 ;10.140 ;40.427
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 9479 ;10.140 ;40.431
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 NCS TYPE: LOCAL
REMARK 3 NUMBER OF DIFFERENT NCS PAIRS : 3
REMARK 3 GROUP CHAIN1 RANGE CHAIN2 RANGE COUNT RMS WEIGHT
REMARK 3 1 A 1 220 H 1 220 22532 0.08 0.05
REMARK 3 2 B 1 209 L 1 209 21840 0.12 0.05
REMARK 3 3 X 10 125 Y 10 125 10092 0.12 0.05
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 5N7W COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 21-FEB-17.
REMARK 100 THE DEPOSITION ID IS D_1200003629.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 09-DEC-14
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 4.5
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) : 0.97625
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 S 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XIA2
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 86657
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.960
REMARK 200 RESOLUTION RANGE LOW (A) : 75.870
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.5
REMARK 200 DATA REDUNDANCY : 3.100
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 13.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.96
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.01
REMARK 200 COMPLETENESS FOR SHELL (%) : 74.4
REMARK 200 DATA REDUNDANCY IN SHELL : 1.80
REMARK 200 R MERGE FOR SHELL (I) : 0.47000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.100
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: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.24
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.47
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 18% (W/V) PEG-MME 2000, 100MM PCTP
REMARK 280 PH4.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 99.99000
REMARK 290 SMTRY3 2 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: HEXAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 15480 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 48960 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -101.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, H, L, X, Y
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 SER A 221
REMARK 465 CYS A 222
REMARK 465 ASP A 223
REMARK 465 LYS A 224
REMARK 465 THR B 211
REMARK 465 GLU B 212
REMARK 465 CYS B 213
REMARK 465 SER B 214
REMARK 465 SER H 134
REMARK 465 LYS H 135
REMARK 465 SER H 136
REMARK 465 THR H 137
REMARK 465 SER H 138
REMARK 465 GLY H 139
REMARK 465 ASP H 223
REMARK 465 LYS H 224
REMARK 465 GLU L 212
REMARK 465 CYS L 213
REMARK 465 SER L 214
REMARK 465 MET X -22
REMARK 465 THR X -21
REMARK 465 PRO X -20
REMARK 465 GLY X -19
REMARK 465 LYS X -18
REMARK 465 THR X -17
REMARK 465 SER X -16
REMARK 465 LEU X -15
REMARK 465 VAL X -14
REMARK 465 SER X -13
REMARK 465 LEU X -12
REMARK 465 LEU X -11
REMARK 465 LEU X -10
REMARK 465 LEU X -9
REMARK 465 LEU X -8
REMARK 465 SER X -7
REMARK 465 LEU X -6
REMARK 465 GLU X -5
REMARK 465 ALA X -4
REMARK 465 ILE X -3
REMARK 465 VAL X -2
REMARK 465 LYS X -1
REMARK 465 ALA X 0
REMARK 465 GLY X 1
REMARK 465 ILE X 2
REMARK 465 THR X 3
REMARK 465 ILE X 4
REMARK 465 PRO X 5
REMARK 465 ARG X 6
REMARK 465 HIS X 29
REMARK 465 ASN X 30
REMARK 465 ARG X 31
REMARK 465 ASN X 32
REMARK 465 THR X 33
REMARK 465 ASN X 34
REMARK 465 THR X 35
REMARK 465 ASN X 36
REMARK 465 PRO X 37
REMARK 465 LYS X 38
REMARK 465 ARG X 39
REMARK 465 SER X 40
REMARK 465 ILE X 127
REMARK 465 VAL X 128
REMARK 465 HIS X 129
REMARK 465 HIS X 130
REMARK 465 VAL X 131
REMARK 465 ALA X 132
REMARK 465 MET Y -22
REMARK 465 THR Y -21
REMARK 465 PRO Y -20
REMARK 465 GLY Y -19
REMARK 465 LYS Y -18
REMARK 465 THR Y -17
REMARK 465 SER Y -16
REMARK 465 LEU Y -15
REMARK 465 VAL Y -14
REMARK 465 SER Y -13
REMARK 465 LEU Y -12
REMARK 465 LEU Y -11
REMARK 465 LEU Y -10
REMARK 465 LEU Y -9
REMARK 465 LEU Y -8
REMARK 465 SER Y -7
REMARK 465 LEU Y -6
REMARK 465 GLU Y -5
REMARK 465 ALA Y -4
REMARK 465 ILE Y -3
REMARK 465 VAL Y -2
REMARK 465 LYS Y -1
REMARK 465 ALA Y 0
REMARK 465 GLY Y 1
REMARK 465 ILE Y 2
REMARK 465 THR Y 3
REMARK 465 ILE Y 4
REMARK 465 PRO Y 5
REMARK 465 ARG Y 6
REMARK 465 ASN Y 7
REMARK 465 PRO Y 8
REMARK 465 GLY Y 9
REMARK 465 ASN Y 30
REMARK 465 ARG Y 31
REMARK 465 ASN Y 32
REMARK 465 THR Y 33
REMARK 465 ASN Y 34
REMARK 465 THR Y 35
REMARK 465 ASN Y 36
REMARK 465 PRO Y 37
REMARK 465 LYS Y 38
REMARK 465 ARG Y 39
REMARK 465 SER Y 40
REMARK 465 SER Y 41
REMARK 465 ILE Y 127
REMARK 465 VAL Y 128
REMARK 465 HIS Y 129
REMARK 465 HIS Y 130
REMARK 465 VAL Y 131
REMARK 465 ALA Y 132
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 NH2 ARG B 53 O HOH B 301 1.88
REMARK 500 O SER L 60 O HOH L 301 2.12
REMARK 500 O SER B 60 O HOH B 302 2.15
REMARK 500 OE1 GLU L 126 O HOH L 302 2.15
REMARK 500 O PRO H 129 OG SER L 123 2.16
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 OD2 ASP A 214 OH TYR H 80 2856 2.11
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 107 CB - CG - OD1 ANGL. DEV. = 6.8 DEGREES
REMARK 500 ASP B 70 CB - CG - OD1 ANGL. DEV. = 5.7 DEGREES
REMARK 500 ASP H 107 CB - CG - OD1 ANGL. DEV. = 6.1 DEGREES
REMARK 500 LEU H 184 CA - CB - CG ANGL. DEV. = 21.7 DEGREES
REMARK 500 LEU L 11 CA - CB - CG ANGL. DEV. = 16.9 DEGREES
REMARK 500 LEU L 11 CB - CG - CD2 ANGL. DEV. = 11.4 DEGREES
REMARK 500 ASP L 70 CB - CG - OD1 ANGL. DEV. = 5.7 DEGREES
REMARK 500 ASP X 58 CB - CG - OD1 ANGL. DEV. = 5.8 DEGREES
REMARK 500 ASP Y 58 CB - CG - OD1 ANGL. DEV. = 5.9 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 133 -73.27 -33.91
REMARK 500 SER A 134 -55.31 97.03
REMARK 500 LYS A 135 22.74 -72.17
REMARK 500 SER A 136 -175.13 -68.01
REMARK 500 THR A 137 149.62 68.26
REMARK 500 SER A 138 -78.45 166.01
REMARK 500 THR A 197 -61.22 -97.67
REMARK 500 THR B 51 -49.03 74.54
REMARK 500 ALA B 84 174.71 179.69
REMARK 500 ASP B 153 -110.62 53.40
REMARK 500 THR H 197 -61.56 -96.55
REMARK 500 ASN H 210 78.99 37.52
REMARK 500 LYS H 220 -160.33 -105.16
REMARK 500 SER H 221 70.45 -66.91
REMARK 500 THR L 51 -49.00 76.34
REMARK 500 SER L 52 -0.27 -143.46
REMARK 500 ASP L 153 -107.83 54.44
REMARK 500 ASN L 172 33.77 -98.25
REMARK 500 GLU L 200 57.27 38.53
REMARK 500 PRO X 11 -144.27 -33.58
REMARK 500 ASN X 12 149.54 -170.57
REMARK 500 LYS X 16 -45.43 -14.14
REMARK 500 HIS X 105 63.64 71.10
REMARK 500 PRO Y 11 -143.02 -33.10
REMARK 500 LYS Y 16 -46.04 -15.48
REMARK 500 HIS Y 105 62.94 71.90
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH B 484 DISTANCE = 9.05 ANGSTROMS
DBREF 5N7W A 1 224 PDB 5N7W 5N7W 1 224
DBREF 5N7W B 1 214 PDB 5N7W 5N7W 1 214
DBREF 5N7W H 1 224 PDB 5N7W 5N7W 1 224
DBREF 5N7W L 1 214 PDB 5N7W 5N7W 1 214
DBREF 5N7W X -22 132 UNP Q16552 IL17_HUMAN 1 155
DBREF 5N7W Y -22 132 UNP Q16552 IL17_HUMAN 1 155
SEQRES 1 A 224 GLN VAL LYS LEU VAL GLN SER GLY ALA GLU VAL LYS LYS
SEQRES 2 A 224 PRO GLY ALA SER VAL LYS VAL SER CYS LYS ALA SER GLY
SEQRES 3 A 224 TYR THR PHE SER SER TYR TRP ILE ALA TRP VAL ARG GLN
SEQRES 4 A 224 ALA PRO GLY GLN GLY LEU GLU TRP ILE GLY GLU ILE LEU
SEQRES 5 A 224 PRO GLY SER GLY SER THR ASN TYR ALA GLN LYS PHE GLN
SEQRES 6 A 224 GLY ARG ALA THR MET THR ALA ASP THR SER THR SER THR
SEQRES 7 A 224 VAL TYR MET GLU LEU SER SER LEU ARG SER GLU ASP THR
SEQRES 8 A 224 ALA VAL TYR TYR CYS ALA ARG PHE PRO TYR TYR TYR GLY
SEQRES 9 A 224 ASN TRP ASP VAL TRP GLY GLN GLY THR THR VAL THR VAL
SEQRES 10 A 224 SER SER ALA SER THR LYS GLY PRO SER VAL PHE PRO LEU
SEQRES 11 A 224 ALA PRO SER SER LYS SER THR SER GLY GLY THR ALA ALA
SEQRES 12 A 224 LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU PRO VAL
SEQRES 13 A 224 THR VAL SER TRP ASN SER GLY ALA LEU THR SER GLY VAL
SEQRES 14 A 224 HIS THR PHE PRO ALA VAL LEU GLN SER SER GLY LEU TYR
SEQRES 15 A 224 SER LEU SER SER VAL VAL THR VAL PRO SER SER SER LEU
SEQRES 16 A 224 GLY THR GLN THR TYR ILE CYS ASN VAL ASN HIS LYS PRO
SEQRES 17 A 224 SER ASN THR LYS VAL ASP LYS ARG VAL GLU PRO LYS SER
SEQRES 18 A 224 CYS ASP LYS
SEQRES 1 B 214 ASP ILE GLN MET THR GLN SER PRO SER SER LEU SER ALA
SEQRES 2 B 214 SER VAL GLY ASP ARG VAL THR ILE THR CYS GLN ALA SER
SEQRES 3 B 214 GLN ASP ILE TRP TRP TYR LEU ASN TRP TYR GLN GLN LYS
SEQRES 4 B 214 PRO GLY LYS ALA PRO LYS LEU LEU ILE TYR TYR THR SER
SEQRES 5 B 214 ARG LEU HIS SER GLY VAL PRO SER ARG PHE SER GLY SER
SEQRES 6 B 214 GLY SER GLY THR ASP TYR THR PHE THR ILE SER SER LEU
SEQRES 7 B 214 GLN PRO GLU ASP ILE ALA THR TYR TYR CYS GLN GLN GLY
SEQRES 8 B 214 PHE TYR LEU PRO TRP THR PHE GLY GLY GLY THR LYS VAL
SEQRES 9 B 214 GLU ILE LYS LEU GLY GLN PRO LYS ALA ALA PRO SER VAL
SEQRES 10 B 214 THR LEU PHE PRO PRO SER SER GLU GLU LEU GLN ALA ASN
SEQRES 11 B 214 LYS ALA THR LEU VAL CYS LEU ILE SER ASP PHE TYR PRO
SEQRES 12 B 214 GLY ALA VAL THR VAL ALA TRP LYS ALA ASP SER SER PRO
SEQRES 13 B 214 VAL LYS ALA GLY VAL GLU THR THR THR PRO SER LYS GLN
SEQRES 14 B 214 SER ASN ASN LYS TYR ALA ALA SER SER TYR LEU SER LEU
SEQRES 15 B 214 THR PRO GLU GLN TRP LYS SER HIS ARG SER TYR SER CYS
SEQRES 16 B 214 GLN VAL THR HIS GLU GLY SER THR VAL GLU LYS THR VAL
SEQRES 17 B 214 ALA PRO THR GLU CYS SER
SEQRES 1 H 224 GLN VAL LYS LEU VAL GLN SER GLY ALA GLU VAL LYS LYS
SEQRES 2 H 224 PRO GLY ALA SER VAL LYS VAL SER CYS LYS ALA SER GLY
SEQRES 3 H 224 TYR THR PHE SER SER TYR TRP ILE ALA TRP VAL ARG GLN
SEQRES 4 H 224 ALA PRO GLY GLN GLY LEU GLU TRP ILE GLY GLU ILE LEU
SEQRES 5 H 224 PRO GLY SER GLY SER THR ASN TYR ALA GLN LYS PHE GLN
SEQRES 6 H 224 GLY ARG ALA THR MET THR ALA ASP THR SER THR SER THR
SEQRES 7 H 224 VAL TYR MET GLU LEU SER SER LEU ARG SER GLU ASP THR
SEQRES 8 H 224 ALA VAL TYR TYR CYS ALA ARG PHE PRO TYR TYR TYR GLY
SEQRES 9 H 224 ASN TRP ASP VAL TRP GLY GLN GLY THR THR VAL THR VAL
SEQRES 10 H 224 SER SER ALA SER THR LYS GLY PRO SER VAL PHE PRO LEU
SEQRES 11 H 224 ALA PRO SER SER LYS SER THR SER GLY GLY THR ALA ALA
SEQRES 12 H 224 LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU PRO VAL
SEQRES 13 H 224 THR VAL SER TRP ASN SER GLY ALA LEU THR SER GLY VAL
SEQRES 14 H 224 HIS THR PHE PRO ALA VAL LEU GLN SER SER GLY LEU TYR
SEQRES 15 H 224 SER LEU SER SER VAL VAL THR VAL PRO SER SER SER LEU
SEQRES 16 H 224 GLY THR GLN THR TYR ILE CYS ASN VAL ASN HIS LYS PRO
SEQRES 17 H 224 SER ASN THR LYS VAL ASP LYS ARG VAL GLU PRO LYS SER
SEQRES 18 H 224 CYS ASP LYS
SEQRES 1 L 214 ASP ILE GLN MET THR GLN SER PRO SER SER LEU SER ALA
SEQRES 2 L 214 SER VAL GLY ASP ARG VAL THR ILE THR CYS GLN ALA SER
SEQRES 3 L 214 GLN ASP ILE TRP TRP TYR LEU ASN TRP TYR GLN GLN LYS
SEQRES 4 L 214 PRO GLY LYS ALA PRO LYS LEU LEU ILE TYR TYR THR SER
SEQRES 5 L 214 ARG LEU HIS SER GLY VAL PRO SER ARG PHE SER GLY SER
SEQRES 6 L 214 GLY SER GLY THR ASP TYR THR PHE THR ILE SER SER LEU
SEQRES 7 L 214 GLN PRO GLU ASP ILE ALA THR TYR TYR CYS GLN GLN GLY
SEQRES 8 L 214 PHE TYR LEU PRO TRP THR PHE GLY GLY GLY THR LYS VAL
SEQRES 9 L 214 GLU ILE LYS LEU GLY GLN PRO LYS ALA ALA PRO SER VAL
SEQRES 10 L 214 THR LEU PHE PRO PRO SER SER GLU GLU LEU GLN ALA ASN
SEQRES 11 L 214 LYS ALA THR LEU VAL CYS LEU ILE SER ASP PHE TYR PRO
SEQRES 12 L 214 GLY ALA VAL THR VAL ALA TRP LYS ALA ASP SER SER PRO
SEQRES 13 L 214 VAL LYS ALA GLY VAL GLU THR THR THR PRO SER LYS GLN
SEQRES 14 L 214 SER ASN ASN LYS TYR ALA ALA SER SER TYR LEU SER LEU
SEQRES 15 L 214 THR PRO GLU GLN TRP LYS SER HIS ARG SER TYR SER CYS
SEQRES 16 L 214 GLN VAL THR HIS GLU GLY SER THR VAL GLU LYS THR VAL
SEQRES 17 L 214 ALA PRO THR GLU CYS SER
SEQRES 1 X 155 MET THR PRO GLY LYS THR SER LEU VAL SER LEU LEU LEU
SEQRES 2 X 155 LEU LEU SER LEU GLU ALA ILE VAL LYS ALA GLY ILE THR
SEQRES 3 X 155 ILE PRO ARG ASN PRO GLY CYS PRO ASN SER GLU ASP LYS
SEQRES 4 X 155 ASN PHE PRO ARG THR VAL MET VAL ASN LEU ASN ILE HIS
SEQRES 5 X 155 ASN ARG ASN THR ASN THR ASN PRO LYS ARG SER SER ASP
SEQRES 6 X 155 TYR TYR ASN ARG SER THR SER PRO TRP ASN LEU HIS ARG
SEQRES 7 X 155 ASN GLU ASP PRO GLU ARG TYR PRO SER VAL ILE TRP GLU
SEQRES 8 X 155 ALA LYS CYS ARG HIS LEU GLY CYS ILE ASN ALA ASP GLY
SEQRES 9 X 155 ASN VAL ASP TYR HIS MET ASN SER VAL PRO ILE GLN GLN
SEQRES 10 X 155 GLU ILE LEU VAL LEU ARG ARG GLU PRO PRO HIS CYS PRO
SEQRES 11 X 155 ASN SER PHE ARG LEU GLU LYS ILE LEU VAL SER VAL GLY
SEQRES 12 X 155 CYS THR CYS VAL THR PRO ILE VAL HIS HIS VAL ALA
SEQRES 1 Y 155 MET THR PRO GLY LYS THR SER LEU VAL SER LEU LEU LEU
SEQRES 2 Y 155 LEU LEU SER LEU GLU ALA ILE VAL LYS ALA GLY ILE THR
SEQRES 3 Y 155 ILE PRO ARG ASN PRO GLY CYS PRO ASN SER GLU ASP LYS
SEQRES 4 Y 155 ASN PHE PRO ARG THR VAL MET VAL ASN LEU ASN ILE HIS
SEQRES 5 Y 155 ASN ARG ASN THR ASN THR ASN PRO LYS ARG SER SER ASP
SEQRES 6 Y 155 TYR TYR ASN ARG SER THR SER PRO TRP ASN LEU HIS ARG
SEQRES 7 Y 155 ASN GLU ASP PRO GLU ARG TYR PRO SER VAL ILE TRP GLU
SEQRES 8 Y 155 ALA LYS CYS ARG HIS LEU GLY CYS ILE ASN ALA ASP GLY
SEQRES 9 Y 155 ASN VAL ASP TYR HIS MET ASN SER VAL PRO ILE GLN GLN
SEQRES 10 Y 155 GLU ILE LEU VAL LEU ARG ARG GLU PRO PRO HIS CYS PRO
SEQRES 11 Y 155 ASN SER PHE ARG LEU GLU LYS ILE LEU VAL SER VAL GLY
SEQRES 12 Y 155 CYS THR CYS VAL THR PRO ILE VAL HIS HIS VAL ALA
FORMUL 7 HOH *678(H2 O)
HELIX 1 AA1 THR A 28 TYR A 32 5 5
HELIX 2 AA2 GLN A 62 GLN A 65 5 4
HELIX 3 AA3 ARG A 87 THR A 91 5 5
HELIX 4 AA4 SER A 162 ALA A 164 5 3
HELIX 5 AA5 LYS A 207 ASN A 210 5 4
HELIX 6 AA6 GLN B 79 ILE B 83 5 5
HELIX 7 AA7 SER B 123 ALA B 129 1 7
HELIX 8 AA8 THR B 183 SER B 189 1 7
HELIX 9 AA9 THR H 28 TYR H 32 5 5
HELIX 10 AB1 GLN H 62 GLN H 65 5 4
HELIX 11 AB2 ARG H 87 THR H 91 5 5
HELIX 12 AB3 SER H 162 ALA H 164 5 3
HELIX 13 AB4 LYS H 207 ASN H 210 5 4
HELIX 14 AB5 GLN L 79 ILE L 83 5 5
HELIX 15 AB6 SER L 123 ALA L 129 1 7
HELIX 16 AB7 THR L 183 SER L 189 1 7
HELIX 17 AB8 ASP X 42 SER X 47 1 6
HELIX 18 AB9 TYR Y 43 SER Y 47 1 5
SHEET 1 A 4 LYS A 3 GLN A 6 0
SHEET 2 A 4 VAL A 18 SER A 25 -1
SHEET 3 A 4 THR A 78 LEU A 83 -1
SHEET 4 A 4 ALA A 68 ASP A 73 -1
SHEET 1 B 6 GLU A 10 LYS A 12 0
SHEET 2 B 6 THR A 113 VAL A 117 1
SHEET 3 B 6 ALA A 92 PHE A 99 -1
SHEET 4 B 6 TRP A 33 GLN A 39 -1
SHEET 5 B 6 GLU A 46 LEU A 52 -1
SHEET 6 B 6 THR A 58 TYR A 60 -1
SHEET 1 C 4 SER A 126 LEU A 130 0
SHEET 2 C 4 THR A 141 LYS A 149 -1
SHEET 3 C 4 LEU A 184 PRO A 191 -1
SHEET 4 C 4 VAL A 169 THR A 171 -1
SHEET 1 D 3 THR A 157 TRP A 160 0
SHEET 2 D 3 ILE A 201 HIS A 206 -1
SHEET 3 D 3 THR A 211 ARG A 216 -1
SHEET 1 E 2 ALA A 97 PRO A 100 0
SHEET 2 E 2 ASN A 105 TRP A 109 -1
SHEET 1 F 4 MET B 4 SER B 7 0
SHEET 2 F 4 VAL B 19 ALA B 25 -1
SHEET 3 F 4 ASP B 70 ILE B 75 -1
SHEET 4 F 4 PHE B 62 SER B 67 -1
SHEET 1 G 5 SER B 10 ALA B 13 0
SHEET 2 G 5 THR B 102 ILE B 106 1
SHEET 3 G 5 ALA B 84 GLN B 90 -1
SHEET 4 G 5 LEU B 33 GLN B 38 -1
SHEET 5 G 5 LYS B 45 ILE B 48 -1
SHEET 1 H 4 SER B 116 PHE B 120 0
SHEET 2 H 4 ALA B 132 SER B 139 -1
SHEET 3 H 4 ALA B 176 LEU B 182 -1
SHEET 4 H 4 VAL B 161 THR B 163 -1
SHEET 1 I 3 THR B 147 ALA B 152 0
SHEET 2 I 3 TYR B 193 HIS B 199 -1
SHEET 3 I 3 SER B 202 VAL B 208 -1
SHEET 1 J 4 LYS H 3 GLN H 6 0
SHEET 2 J 4 VAL H 18 SER H 25 -1
SHEET 3 J 4 THR H 78 LEU H 83 -1
SHEET 4 J 4 ALA H 68 ASP H 73 -1
SHEET 1 K 6 GLU H 10 LYS H 12 0
SHEET 2 K 6 THR H 113 VAL H 117 1
SHEET 3 K 6 ALA H 92 PHE H 99 -1
SHEET 4 K 6 TRP H 33 ALA H 40 -1
SHEET 5 K 6 LEU H 45 LEU H 52 -1
SHEET 6 K 6 THR H 58 TYR H 60 -1
SHEET 1 L 4 SER H 126 LEU H 130 0
SHEET 2 L 4 THR H 141 LYS H 149 -1
SHEET 3 L 4 LEU H 184 PRO H 191 -1
SHEET 4 L 4 VAL H 169 THR H 171 -1
SHEET 1 M 3 THR H 157 TRP H 160 0
SHEET 2 M 3 ILE H 201 HIS H 206 -1
SHEET 3 M 3 THR H 211 ARG H 216 -1
SHEET 1 N 4 MET L 4 SER L 7 0
SHEET 2 N 4 VAL L 19 ALA L 25 -1
SHEET 3 N 4 ASP L 70 ILE L 75 -1
SHEET 4 N 4 PHE L 62 SER L 67 -1
SHEET 1 O 5 SER L 10 SER L 14 0
SHEET 2 O 5 THR L 102 LYS L 107 1
SHEET 3 O 5 ALA L 84 GLN L 90 -1
SHEET 4 O 5 LEU L 33 GLN L 38 -1
SHEET 5 O 5 LYS L 45 ILE L 48 -1
SHEET 1 P 4 SER L 116 PHE L 120 0
SHEET 2 P 4 ALA L 132 SER L 139 -1
SHEET 3 P 4 ALA L 176 LEU L 182 -1
SHEET 4 P 4 VAL L 161 THR L 163 -1
SHEET 1 Q 3 THR L 147 ALA L 152 0
SHEET 2 Q 3 TYR L 193 HIS L 199 -1
SHEET 3 Q 3 SER L 202 VAL L 208 -1
SHEET 1 R 2 TRP X 51 GLU X 57 0
SHEET 2 R 2 VAL X 65 CYS X 71 -1
SHEET 1 S 3 GLY X 75 ILE X 77 0
SHEET 2 S 3 VAL X 83 ARG X 101 -1
SHEET 3 S 3 PHE X 110 THR X 125 -1
SHEET 1 T 2 TRP Y 51 GLU Y 57 0
SHEET 2 T 2 VAL Y 65 CYS Y 71 -1
SHEET 1 U 3 GLY Y 75 ILE Y 77 0
SHEET 2 U 3 VAL Y 83 ARG Y 101 -1
SHEET 3 U 3 PHE Y 110 THR Y 125 -1
SSBOND 1 CYS A 22 CYS A 96 1555 1555 2.04
SSBOND 2 CYS A 146 CYS A 202 1555 1555 2.10
SSBOND 3 CYS B 23 CYS B 88 1555 1555 2.15
SSBOND 4 CYS B 136 CYS B 195 1555 1555 2.07
SSBOND 5 CYS H 22 CYS H 96 1555 1555 2.10
SSBOND 6 CYS H 146 CYS H 202 1555 1555 2.09
SSBOND 7 CYS L 23 CYS L 88 1555 1555 2.20
SSBOND 8 CYS L 136 CYS L 195 1555 1555 2.09
SSBOND 9 CYS X 10 CYS X 106 1555 1555 2.11
SSBOND 10 CYS X 71 CYS X 121 1555 1555 2.05
SSBOND 11 CYS X 76 CYS X 123 1555 1555 2.07
SSBOND 12 CYS Y 10 CYS Y 106 1555 1555 2.00
SSBOND 13 CYS Y 71 CYS Y 121 1555 1555 2.04
SSBOND 14 CYS Y 76 CYS Y 123 1555 1555 2.06
CISPEP 1 PHE A 152 PRO A 153 0 -5.02
CISPEP 2 GLU A 154 PRO A 155 0 0.52
CISPEP 3 SER B 7 PRO B 8 0 -4.70
CISPEP 4 LEU B 94 PRO B 95 0 2.04
CISPEP 5 TYR B 142 PRO B 143 0 -2.71
CISPEP 6 PHE H 152 PRO H 153 0 -8.74
CISPEP 7 GLU H 154 PRO H 155 0 -2.07
CISPEP 8 SER L 7 PRO L 8 0 0.42
CISPEP 9 LEU L 94 PRO L 95 0 0.49
CISPEP 10 TYR L 142 PRO L 143 0 -0.76
CISPEP 11 PHE X 18 PRO X 19 0 1.63
CISPEP 12 TYR X 62 PRO X 63 0 -1.22
CISPEP 13 PRO X 103 PRO X 104 0 6.76
CISPEP 14 PHE Y 18 PRO Y 19 0 1.10
CISPEP 15 TYR Y 62 PRO Y 63 0 -3.44
CISPEP 16 PRO Y 103 PRO Y 104 0 5.64
CRYST1 42.240 199.980 76.350 90.00 96.42 90.00 P 1 21 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 0.023674 0.000000 0.002664 0.00000
SCALE2 0.000000 0.005001 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013180 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
