HEADER IMMUNE SYSTEM 30-JUN-15 5CBE
TITLE E10 IN COMPLEX WITH CXCL13
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: E10 HEAVY CHAIN;
COMPND 3 CHAIN: A, C;
COMPND 4 ENGINEERED: YES;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: E10 LIGHT CHAIN;
COMPND 7 CHAIN: B, D;
COMPND 8 ENGINEERED: YES;
COMPND 9 MOL_ID: 3;
COMPND 10 MOLECULE: C-X-C MOTIF CHEMOKINE 13;
COMPND 11 CHAIN: E, F;
COMPND 12 SYNONYM: ANGIE,B CELL-ATTRACTING CHEMOKINE 1,BCA-1,B LYMPHOCYTE
COMPND 13 CHEMOATTRACTANT,CXC CHEMOKINE BLC,SMALL-INDUCIBLE CYTOKINE B13;
COMPND 14 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 CELL_LINE: HEK293;
SOURCE 6 GENE: IGHV1-69-2;
SOURCE 7 EXPRESSION_SYSTEM: MAMMALIA;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 40674;
SOURCE 9 EXPRESSION_SYSTEM_CELL_LINE: HEK293F;
SOURCE 10 MOL_ID: 2;
SOURCE 11 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 12 ORGANISM_COMMON: HUMAN;
SOURCE 13 ORGANISM_TAXID: 9606;
SOURCE 14 EXPRESSION_SYSTEM: MAMMALIA;
SOURCE 15 EXPRESSION_SYSTEM_TAXID: 40674;
SOURCE 16 EXPRESSION_SYSTEM_CELL_LINE: HEK293F;
SOURCE 17 MOL_ID: 3;
SOURCE 18 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 19 ORGANISM_COMMON: HUMAN;
SOURCE 20 ORGANISM_TAXID: 9606;
SOURCE 21 GENE: CXCL13, BCA1, BLC, SCYB13;
SOURCE 22 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 23 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS ANTI-CXCL13, E10, SCFV, IMMUNE SYSTEM
EXPDTA X-RAY DIFFRACTION
AUTHOR C.TU,J.BARD,L.MOSYAK
REVDAT 5 27-SEP-23 5CBE 1 REMARK
REVDAT 4 14-NOV-18 5CBE 1 JRNL
REVDAT 3 22-NOV-17 5CBE 1 REMARK
REVDAT 2 01-NOV-17 5CBE 1 REMARK
REVDAT 1 04-NOV-15 5CBE 0
JRNL AUTH C.TU,V.TERRAUBE,A.S.TAM,W.STOCHAJ,B.J.FENNELL,L.LIN,M.STAHL,
JRNL AUTH 2 E.R.LAVALLIE,W.SOMERS,W.J.FINLAY,L.MOSYAK,J.BARD,
JRNL AUTH 3 O.CUNNINGHAM
JRNL TITL A COMBINATION OF STRUCTURAL AND EMPIRICAL ANALYSES
JRNL TITL 2 DELINEATES THE KEY CONTACTS MEDIATING STABILITY AND AFFINITY
JRNL TITL 3 INCREASES IN AN OPTIMIZED BIOTHERAPEUTIC SINGLE-CHAIN FV
JRNL TITL 4 (SCFV).
JRNL REF J. BIOL. CHEM. V. 291 1267 2016
JRNL REFN ESSN 1083-351X
JRNL PMID 26515064
JRNL DOI 10.1074/JBC.M115.688010
REMARK 2
REMARK 2 RESOLUTION. 2.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER 2.11.5
REMARK 3 AUTHORS : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,
REMARK 3 : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,
REMARK 3 : WOMACK,MATTHEWS,TEN EYCK,TRONRUD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 40.92
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 34852
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) : 0.250
REMARK 3 R VALUE (WORKING SET) : 0.248
REMARK 3 FREE R VALUE : 0.275
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.020
REMARK 3 FREE R VALUE TEST SET COUNT : 1751
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 17
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 2.47
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.85
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 2930
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2514
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2795
REMARK 3 BIN R VALUE (WORKING SET) : 0.2506
REMARK 3 BIN FREE R VALUE : 0.2684
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.61
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 135
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4599
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 4
REMARK 3 SOLVENT ATOMS : 93
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 59.02
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 82.67
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -4.66290
REMARK 3 B22 (A**2) : -4.66290
REMARK 3 B33 (A**2) : 9.32590
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.609
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : 0.316
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.237
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 0.322
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : 0.242
REMARK 3
REMARK 3 REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797
REMARK 3 CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.905
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.884
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 4711 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 6401 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 1566 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : 98 ; 2.000 ; HARMONIC
REMARK 3 GENERAL PLANES : 689 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 4711 ; 20.000 ; HARMONIC
REMARK 3 BAD NON-BONDED CONTACTS : NULL ; NULL ; NULL
REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL
REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL
REMARK 3 CHIRAL IMPROPER TORSION : 631 ; 5.000 ; SEMIHARMONIC
REMARK 3 SUM OF OCCUPANCIES : NULL ; NULL ; NULL
REMARK 3 UTILITY DISTANCES : NULL ; NULL ; NULL
REMARK 3 UTILITY ANGLES : NULL ; NULL ; NULL
REMARK 3 UTILITY TORSION : NULL ; NULL ; NULL
REMARK 3 IDEAL-DIST CONTACT TERM : 5074 ; 4.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.008
REMARK 3 BOND ANGLES (DEGREES) : 1.06
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 2.48
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 20.30
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 6
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: { A|* }
REMARK 3 ORIGIN FOR THE GROUP (A): -42.0312 88.5310 -18.4422
REMARK 3 T TENSOR
REMARK 3 T11: -0.4499 T22: -0.4521
REMARK 3 T33: 0.7720 T12: -0.0298
REMARK 3 T13: 0.0410 T23: -0.2166
REMARK 3 L TENSOR
REMARK 3 L11: 3.5723 L22: 1.7793
REMARK 3 L33: 3.5191 L12: -1.1195
REMARK 3 L13: 0.5983 L23: 0.9620
REMARK 3 S TENSOR
REMARK 3 S11: -0.0198 S12: -0.5094 S13: 0.2357
REMARK 3 S21: 0.2863 S22: -0.4320 S23: 1.4955
REMARK 3 S31: -0.0709 S32: -0.4306 S33: 0.4518
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: { B|* }
REMARK 3 ORIGIN FOR THE GROUP (A): -27.4120 84.8883 -33.0132
REMARK 3 T TENSOR
REMARK 3 T11: -0.1485 T22: -0.2249
REMARK 3 T33: 0.0530 T12: 0.0465
REMARK 3 T13: -0.2343 T23: 0.0773
REMARK 3 L TENSOR
REMARK 3 L11: 2.4927 L22: 6.9855
REMARK 3 L33: 4.7645 L12: 0.3403
REMARK 3 L13: 0.6129 L23: 2.1018
REMARK 3 S TENSOR
REMARK 3 S11: 0.0812 S12: 0.3026 S13: -0.1253
REMARK 3 S21: -0.8378 S22: -0.3849 S23: 0.9965
REMARK 3 S31: -0.2367 S32: 0.3081 S33: 0.3037
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: { C|* }
REMARK 3 ORIGIN FOR THE GROUP (A): -14.3918 32.9913 -19.1010
REMARK 3 T TENSOR
REMARK 3 T11: -0.1304 T22: 0.2402
REMARK 3 T33: -0.4590 T12: -0.3379
REMARK 3 T13: 0.0387 T23: -0.1060
REMARK 3 L TENSOR
REMARK 3 L11: 2.0980 L22: 4.1295
REMARK 3 L33: 5.6197 L12: -0.1369
REMARK 3 L13: -0.3430 L23: 4.0310
REMARK 3 S TENSOR
REMARK 3 S11: -0.0036 S12: 0.1802 S13: -0.2710
REMARK 3 S21: -0.1954 S22: -0.0493 S23: -0.0367
REMARK 3 S31: 0.1499 S32: -0.0790 S33: 0.0529
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: { D|* }
REMARK 3 ORIGIN FOR THE GROUP (A): -32.8647 35.7885 -8.9025
REMARK 3 T TENSOR
REMARK 3 T11: -0.2797 T22: 0.8085
REMARK 3 T33: -0.5335 T12: -0.3793
REMARK 3 T13: -0.0206 T23: 0.1239
REMARK 3 L TENSOR
REMARK 3 L11: 3.6656 L22: 3.4958
REMARK 3 L33: 1.1317 L12: 0.4701
REMARK 3 L13: 2.4340 L23: 3.1582
REMARK 3 S TENSOR
REMARK 3 S11: -0.4108 S12: 0.6386 S13: -0.0150
REMARK 3 S21: -0.2868 S22: 0.5442 S23: 0.4531
REMARK 3 S31: -0.1975 S32: -0.4539 S33: -0.1334
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: { E|* }
REMARK 3 ORIGIN FOR THE GROUP (A): -21.9214 76.0432 -1.1157
REMARK 3 T TENSOR
REMARK 3 T11: 0.3815 T22: -0.3381
REMARK 3 T33: -0.2617 T12: 0.0333
REMARK 3 T13: 0.1966 T23: 0.1301
REMARK 3 L TENSOR
REMARK 3 L11: 3.0695 L22: 0.0464
REMARK 3 L33: 6.5379 L12: -0.1816
REMARK 3 L13: 2.4104 L23: -3.2253
REMARK 3 S TENSOR
REMARK 3 S11: -0.0467 S12: -0.2690 S13: 0.0817
REMARK 3 S21: 0.4588 S22: 0.0621 S23: 0.1429
REMARK 3 S31: 0.0822 S32: -0.1274 S33: -0.0154
REMARK 3
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: { F|* }
REMARK 3 ORIGIN FOR THE GROUP (A): -9.6690 59.0684 -7.4758
REMARK 3 T TENSOR
REMARK 3 T11: 0.0305 T22: 0.1606
REMARK 3 T33: -0.2846 T12: 0.0163
REMARK 3 T13: -0.0864 T23: 0.1151
REMARK 3 L TENSOR
REMARK 3 L11: -0.7218 L22: 7.1051
REMARK 3 L33: 1.8669 L12: -1.3248
REMARK 3 L13: -1.2326 L23: -5.3116
REMARK 3 S TENSOR
REMARK 3 S11: -0.1657 S12: 0.4794 S13: 0.4586
REMARK 3 S21: -0.1755 S22: 0.1990 S23: -0.0091
REMARK 3 S31: -0.4422 S32: -0.0697 S33: -0.0333
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 5CBE COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-JUL-15.
REMARK 100 THE DEPOSITION ID IS D_1000211338.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-APR-13
REMARK 200 TEMPERATURE (KELVIN) : 193
REMARK 200 PH : 6
REMARK 200 NUMBER OF CRYSTALS USED : NULL
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) : 1.0
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : PSI PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 34874
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.400
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 11.60
REMARK 200 R MERGE (I) : 0.07000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 30.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.49
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 9.10
REMARK 200 R MERGE FOR SHELL (I) : 0.60500
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.600
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: E10 AND 3GV3/2R3Z/4HSV/3IL8
REMARK 200
REMARK 200 REMARK: LONG ROD
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 57.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.87
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM KH2PO4, 100 MM NAH2PO4, 100 MM
REMARK 280 MES PH 6, 2000 MM NACL, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 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+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+2/3
REMARK 290 6555 -X,-X+Y,-Z+1/3
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 32.66667
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 65.33333
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 65.33333
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 32.66667
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 300 REMARK: TRIMER CONFIRMED BY GEL FILTRATION
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: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3350 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 15260 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -19.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, E
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: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3600 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 15390 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -24.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D, F
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 GLY A 27
REMARK 465 THR A 28
REMARK 465 GLY A 114
REMARK 465 GLY A 115
REMARK 465 GLY A 116
REMARK 465 GLY A 117
REMARK 465 SER A 118
REMARK 465 GLY A 119
REMARK 465 GLY A 120
REMARK 465 GLY A 121
REMARK 465 GLY A 122
REMARK 465 SER A 123
REMARK 465 GLY A 124
REMARK 465 GLY A 125
REMARK 465 GLY A 126
REMARK 465 GLY A 127
REMARK 465 SER A 128
REMARK 465 GLN B 1
REMARK 465 GLY B 107
REMARK 465 ASP B 108
REMARK 465 GLN B 109
REMARK 465 GLU B 110
REMARK 465 PRO B 111
REMARK 465 LYS B 112
REMARK 465 SER B 113
REMARK 465 SER B 114
REMARK 465 ASP B 115
REMARK 465 LYS B 116
REMARK 465 THR B 117
REMARK 465 HIS B 118
REMARK 465 GLY C 114
REMARK 465 GLY C 115
REMARK 465 GLY C 116
REMARK 465 GLY C 117
REMARK 465 SER C 118
REMARK 465 GLY C 119
REMARK 465 GLY C 120
REMARK 465 GLY C 121
REMARK 465 GLY C 122
REMARK 465 SER C 123
REMARK 465 GLY C 124
REMARK 465 GLY C 125
REMARK 465 GLY C 126
REMARK 465 GLY C 127
REMARK 465 SER C 128
REMARK 465 GLY D 107
REMARK 465 ASP D 108
REMARK 465 GLN D 109
REMARK 465 GLU D 110
REMARK 465 PRO D 111
REMARK 465 LYS D 112
REMARK 465 SER D 113
REMARK 465 SER D 114
REMARK 465 ASP D 115
REMARK 465 LYS D 116
REMARK 465 THR D 117
REMARK 465 HIS D 118
REMARK 465 MET E -2
REMARK 465 VAL E -1
REMARK 465 LEU E 0
REMARK 465 GLU E 1
REMARK 465 VAL E 2
REMARK 465 LEU E 67
REMARK 465 ARG E 68
REMARK 465 LYS E 69
REMARK 465 ARG E 70
REMARK 465 SER E 71
REMARK 465 SER E 72
REMARK 465 SER E 73
REMARK 465 THR E 74
REMARK 465 LEU E 75
REMARK 465 PRO E 76
REMARK 465 VAL E 77
REMARK 465 PRO E 78
REMARK 465 VAL E 79
REMARK 465 PHE E 80
REMARK 465 LYS E 81
REMARK 465 ARG E 82
REMARK 465 LYS E 83
REMARK 465 ILE E 84
REMARK 465 PRO E 85
REMARK 465 MET F -2
REMARK 465 VAL F -1
REMARK 465 LEU F 0
REMARK 465 GLU F 1
REMARK 465 VAL F 2
REMARK 465 TYR F 3
REMARK 465 TYR F 4
REMARK 465 SER F 71
REMARK 465 SER F 72
REMARK 465 SER F 73
REMARK 465 THR F 74
REMARK 465 LEU F 75
REMARK 465 PRO F 76
REMARK 465 VAL F 77
REMARK 465 PRO F 78
REMARK 465 VAL F 79
REMARK 465 PHE F 80
REMARK 465 LYS F 81
REMARK 465 ARG F 82
REMARK 465 LYS F 83
REMARK 465 ILE F 84
REMARK 465 PRO F 85
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 VAL A 111 CG1 CG2
REMARK 470 GLN C 3 CG CD OE1 NE2
REMARK 470 LYS D 42 CG CD CE NZ
REMARK 470 LYS D 45 CG CD CE NZ
REMARK 470 ARG F 70 CG CD NE CZ NH1 NH2
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 GLU D 81 CD
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 O VAL B 33 O ASP B 50 2.09
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 TYR A 32 -167.50 -117.93
REMARK 500 ASP B 27B -93.36 -134.19
REMARK 500 TRP B 32 44.32 -75.38
REMARK 500 ASP B 50 -125.27 68.82
REMARK 500 GLU B 83 103.84 -54.57
REMARK 500 SER C 25 -138.96 49.04
REMARK 500 SER C 30 -141.24 -179.37
REMARK 500 TYR C 32 -155.78 -123.35
REMARK 500 GLN C 61 -36.32 -35.95
REMARK 500 GLN C 64 -50.95 -28.28
REMARK 500 GLN D 17 -162.20 -109.69
REMARK 500 ASP D 27B -86.37 -122.65
REMARK 500 ALA D 29 -85.94 -67.07
REMARK 500 TRP D 32 45.17 -68.07
REMARK 500 PRO D 40 -93.88 -10.04
REMARK 500 ASP D 50 -134.84 64.43
REMARK 500 VAL E 17 127.09 -37.52
REMARK 500 ASN E 34 -0.19 61.45
REMARK 500 LYS E 48 -2.17 79.07
REMARK 500 SER F 6 18.76 58.87
REMARK 500 LYS F 48 -1.16 79.30
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 EDO A 201
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5C2B RELATED DB: PDB
REMARK 900 THE PARENTAL SCFV (3B4)
REMARK 900 RELATED ID: 5C6W RELATED DB: PDB
REMARK 900 E10 SCFV
REMARK 900 RELATED ID: 5CBA RELATED DB: PDB
REMARK 900 THE PARENTAL SCFV 3B4 IN COMPLEX WITH CXCL13
DBREF1 5CBE A 1 94 UNP A0A0B4J2H0_HUMAN
DBREF2 5CBE A A0A0B4J2H0 20 117
DBREF 5CBE A 95 128 PDB 5CBE 5CBE 95 128
DBREF 5CBE B 1 90 UNP P04209 LV211_HUMAN 1 92
DBREF 5CBE B 89 118 PDB 5CBE 5CBE 89 118
DBREF1 5CBE C 1 94 UNP A0A0B4J2H0_HUMAN
DBREF2 5CBE C A0A0B4J2H0 20 117
DBREF 5CBE C 95 128 PDB 5CBE 5CBE 95 128
DBREF 5CBE D 1 90 UNP P04209 LV211_HUMAN 1 92
DBREF 5CBE D 89 118 PDB 5CBE 5CBE 89 118
DBREF 5CBE E -1 85 UNP O43927 CXL13_HUMAN 23 109
DBREF 5CBE F -1 85 UNP O43927 CXL13_HUMAN 23 109
SEQADV 5CBE ALA B 13 UNP P04209 GLY 12 CONFLICT
SEQADV 5CBE SER B 27 UNP P04209 THR 26 CONFLICT
SEQADV 5CBE ALA B 29 UNP P04209 GLY 31 CONFLICT
SEQADV 5CBE TRP B 32 UNP P04209 PHE 34 CONFLICT
SEQADV 5CBE PHE B 49 UNP P04209 TYR 51 CONFLICT
SEQADV 5CBE ASN B 53 UNP P04209 SER 55 CONFLICT
SEQADV 5CBE VAL B 58 UNP P04209 ILE 60 CONFLICT
SEQADV 5CBE HIS B 60 UNP P04209 ASN 62 CONFLICT
SEQADV 5CBE ALA B 89 UNP P04209 SER 91 CONFLICT
SEQADV 5CBE ALA D 13 UNP P04209 GLY 12 CONFLICT
SEQADV 5CBE SER D 27 UNP P04209 THR 26 CONFLICT
SEQADV 5CBE ALA D 29 UNP P04209 GLY 31 CONFLICT
SEQADV 5CBE TRP D 32 UNP P04209 PHE 34 CONFLICT
SEQADV 5CBE PHE D 49 UNP P04209 TYR 51 CONFLICT
SEQADV 5CBE ASN D 53 UNP P04209 SER 55 CONFLICT
SEQADV 5CBE VAL D 58 UNP P04209 ILE 60 CONFLICT
SEQADV 5CBE HIS D 60 UNP P04209 ASN 62 CONFLICT
SEQADV 5CBE ALA D 89 UNP P04209 SER 91 CONFLICT
SEQADV 5CBE MET E -2 UNP O43927 INITIATING METHIONINE
SEQADV 5CBE MET F -2 UNP O43927 INITIATING METHIONINE
SEQRES 1 A 142 GLN VAL GLN LEU VAL GLN SER GLY ALA GLU VAL LYS LYS
SEQRES 2 A 142 PRO GLY SER SER VAL LYS VAL SER CYS LYS ALA SER GLY
SEQRES 3 A 142 GLY THR PHE SER SER TYR ALA ILE SER TRP VAL ARG GLN
SEQRES 4 A 142 ALA PRO GLY GLN GLY LEU GLU TRP MET GLY GLY ILE ILE
SEQRES 5 A 142 PRO ILE PHE GLY THR ALA ASN TYR ALA GLN LYS PHE GLN
SEQRES 6 A 142 GLY ARG VAL THR ILE THR ALA ASP GLU SER THR SER THR
SEQRES 7 A 142 ALA TYR MET GLU LEU SER SER LEU ARG SER GLU ASP THR
SEQRES 8 A 142 ALA VAL TYR TYR CYS ALA ARG GLU PRO ASP TYR TYR ASP
SEQRES 9 A 142 SER SER GLY TYR TYR PRO ILE ASP ALA PHE ASP ILE TRP
SEQRES 10 A 142 GLY GLN GLY THR THR VAL THR VAL SER SER GLY GLY GLY
SEQRES 11 A 142 GLY SER GLY GLY GLY GLY SER GLY GLY GLY GLY SER
SEQRES 1 B 122 GLN SER ALA LEU THR GLN PRO ALA SER VAL SER ALA SER
SEQRES 2 B 122 PRO GLY GLN SER ILE THR ILE SER CYS THR GLY THR SER
SEQRES 3 B 122 SER ASP VAL GLY ALA TYR ASP TRP VAL SER TRP TYR GLN
SEQRES 4 B 122 GLN HIS PRO GLY LYS ALA PRO LYS LEU LEU ILE PHE ASP
SEQRES 5 B 122 VAL ASN ASN ARG PRO SER GLY VAL SER HIS ARG PHE SER
SEQRES 6 B 122 GLY SER LYS SER GLY ASN THR ALA SER LEU THR ILE SER
SEQRES 7 B 122 GLY LEU GLN ALA GLU ASP GLU ALA ASP TYR TYR CYS ALA
SEQRES 8 B 122 SER ALA THR LEU LEU ASP THR TYR VAL PHE GLY THR GLY
SEQRES 9 B 122 THR LYS VAL THR VAL LEU GLY ASP GLN GLU PRO LYS SER
SEQRES 10 B 122 SER ASP LYS THR HIS
SEQRES 1 C 142 GLN VAL GLN LEU VAL GLN SER GLY ALA GLU VAL LYS LYS
SEQRES 2 C 142 PRO GLY SER SER VAL LYS VAL SER CYS LYS ALA SER GLY
SEQRES 3 C 142 GLY THR PHE SER SER TYR ALA ILE SER TRP VAL ARG GLN
SEQRES 4 C 142 ALA PRO GLY GLN GLY LEU GLU TRP MET GLY GLY ILE ILE
SEQRES 5 C 142 PRO ILE PHE GLY THR ALA ASN TYR ALA GLN LYS PHE GLN
SEQRES 6 C 142 GLY ARG VAL THR ILE THR ALA ASP GLU SER THR SER THR
SEQRES 7 C 142 ALA TYR MET GLU LEU SER SER LEU ARG SER GLU ASP THR
SEQRES 8 C 142 ALA VAL TYR TYR CYS ALA ARG GLU PRO ASP TYR TYR ASP
SEQRES 9 C 142 SER SER GLY TYR TYR PRO ILE ASP ALA PHE ASP ILE TRP
SEQRES 10 C 142 GLY GLN GLY THR THR VAL THR VAL SER SER GLY GLY GLY
SEQRES 11 C 142 GLY SER GLY GLY GLY GLY SER GLY GLY GLY GLY SER
SEQRES 1 D 122 GLN SER ALA LEU THR GLN PRO ALA SER VAL SER ALA SER
SEQRES 2 D 122 PRO GLY GLN SER ILE THR ILE SER CYS THR GLY THR SER
SEQRES 3 D 122 SER ASP VAL GLY ALA TYR ASP TRP VAL SER TRP TYR GLN
SEQRES 4 D 122 GLN HIS PRO GLY LYS ALA PRO LYS LEU LEU ILE PHE ASP
SEQRES 5 D 122 VAL ASN ASN ARG PRO SER GLY VAL SER HIS ARG PHE SER
SEQRES 6 D 122 GLY SER LYS SER GLY ASN THR ALA SER LEU THR ILE SER
SEQRES 7 D 122 GLY LEU GLN ALA GLU ASP GLU ALA ASP TYR TYR CYS ALA
SEQRES 8 D 122 SER ALA THR LEU LEU ASP THR TYR VAL PHE GLY THR GLY
SEQRES 9 D 122 THR LYS VAL THR VAL LEU GLY ASP GLN GLU PRO LYS SER
SEQRES 10 D 122 SER ASP LYS THR HIS
SEQRES 1 E 88 MET VAL LEU GLU VAL TYR TYR THR SER LEU ARG CYS ARG
SEQRES 2 E 88 CYS VAL GLN GLU SER SER VAL PHE ILE PRO ARG ARG PHE
SEQRES 3 E 88 ILE ASP ARG ILE GLN ILE LEU PRO ARG GLY ASN GLY CYS
SEQRES 4 E 88 PRO ARG LYS GLU ILE ILE VAL TRP LYS LYS ASN LYS SER
SEQRES 5 E 88 ILE VAL CYS VAL ASP PRO GLN ALA GLU TRP ILE GLN ARG
SEQRES 6 E 88 MET MET GLU VAL LEU ARG LYS ARG SER SER SER THR LEU
SEQRES 7 E 88 PRO VAL PRO VAL PHE LYS ARG LYS ILE PRO
SEQRES 1 F 88 MET VAL LEU GLU VAL TYR TYR THR SER LEU ARG CYS ARG
SEQRES 2 F 88 CYS VAL GLN GLU SER SER VAL PHE ILE PRO ARG ARG PHE
SEQRES 3 F 88 ILE ASP ARG ILE GLN ILE LEU PRO ARG GLY ASN GLY CYS
SEQRES 4 F 88 PRO ARG LYS GLU ILE ILE VAL TRP LYS LYS ASN LYS SER
SEQRES 5 F 88 ILE VAL CYS VAL ASP PRO GLN ALA GLU TRP ILE GLN ARG
SEQRES 6 F 88 MET MET GLU VAL LEU ARG LYS ARG SER SER SER THR LEU
SEQRES 7 F 88 PRO VAL PRO VAL PHE LYS ARG LYS ILE PRO
HET EDO A 201 4
HETNAM EDO 1,2-ETHANEDIOL
HETSYN EDO ETHYLENE GLYCOL
FORMUL 7 EDO C2 H6 O2
FORMUL 8 HOH *93(H2 O)
HELIX 1 AA1 ARG A 83 THR A 87 5 5
HELIX 2 AA2 GLN B 79 GLU B 83 5 5
HELIX 3 AA3 ARG C 83 THR C 87 5 5
HELIX 4 AA4 GLN D 79 GLU D 83 5 5
HELIX 5 AA5 PRO E 20 ARG E 22 5 3
HELIX 6 AA6 ALA E 57 ARG E 62 1 6
HELIX 7 AA7 MET E 63 VAL E 66 5 4
HELIX 8 AA8 PRO F 20 ARG F 22 5 3
HELIX 9 AA9 ALA F 57 ARG F 68 1 12
SHEET 1 AA1 4 LEU A 4 GLN A 6 0
SHEET 2 AA1 4 VAL A 18 ALA A 24 -1 O LYS A 23 N VAL A 5
SHEET 3 AA1 4 THR A 77 LEU A 82 -1 O ALA A 78 N CYS A 22
SHEET 4 AA1 4 VAL A 67 ASP A 72 -1 N THR A 68 O GLU A 81
SHEET 1 AA2 6 GLU A 10 LYS A 12 0
SHEET 2 AA2 6 THR A 107 VAL A 111 1 O THR A 110 N GLU A 10
SHEET 3 AA2 6 ALA A 88 GLU A 95 -1 N ALA A 88 O VAL A 109
SHEET 4 AA2 6 ALA A 33 GLN A 39 -1 N SER A 35 O ALA A 93
SHEET 5 AA2 6 LEU A 45 ILE A 52 -1 O GLY A 49 N TRP A 36
SHEET 6 AA2 6 THR A 56 TYR A 59 -1 O THR A 56 N ILE A 52
SHEET 1 AA3 2 ASP A 97 ASP A 100 0
SHEET 2 AA3 2 GLY A 100C PRO A 100F-1 O TYR A 100E N TYR A 98
SHEET 1 AA4 5 SER B 9 ALA B 13 0
SHEET 2 AA4 5 THR B 102 VAL B 106 1 O LYS B 103 N VAL B 11
SHEET 3 AA4 5 ASP B 85 ALA B 91 -1 N TYR B 86 O THR B 102
SHEET 4 AA4 5 VAL B 33 GLN B 38 -1 N SER B 34 O ALA B 89
SHEET 5 AA4 5 LYS B 45 ILE B 48 -1 O LEU B 47 N TRP B 35
SHEET 1 AA5 4 SER B 9 ALA B 13 0
SHEET 2 AA5 4 THR B 102 VAL B 106 1 O LYS B 103 N VAL B 11
SHEET 3 AA5 4 ASP B 85 ALA B 91 -1 N TYR B 86 O THR B 102
SHEET 4 AA5 4 TYR B 96 PHE B 98 -1 O VAL B 97 N SER B 90
SHEET 1 AA6 3 ILE B 19 THR B 24 0
SHEET 2 AA6 3 THR B 70 ILE B 75 -1 O ALA B 71 N CYS B 23
SHEET 3 AA6 3 PHE B 62 SER B 67 -1 N SER B 63 O THR B 74
SHEET 1 AA7 4 VAL C 5 GLN C 6 0
SHEET 2 AA7 4 VAL C 18 LYS C 23 -1 O LYS C 23 N VAL C 5
SHEET 3 AA7 4 THR C 77 LEU C 82 -1 O ALA C 78 N CYS C 22
SHEET 4 AA7 4 VAL C 67 ASP C 72 -1 N THR C 70 O TYR C 79
SHEET 1 AA8 6 GLU C 10 LYS C 12 0
SHEET 2 AA8 6 THR C 107 VAL C 111 1 O THR C 110 N LYS C 12
SHEET 3 AA8 6 ALA C 88 GLU C 95 -1 N ALA C 88 O VAL C 109
SHEET 4 AA8 6 ALA C 33 GLN C 39 -1 N ALA C 33 O GLU C 95
SHEET 5 AA8 6 LEU C 45 ILE C 52 -1 O GLY C 49 N TRP C 36
SHEET 6 AA8 6 THR C 56 TYR C 59 -1 O THR C 56 N ILE C 52
SHEET 1 AA9 2 ASP C 97 TYR C 99 0
SHEET 2 AA9 2 TYR C 100D PRO C 100F-1 O TYR C 100E N TYR C 98
SHEET 1 AB1 5 SER D 9 SER D 12 0
SHEET 2 AB1 5 THR D 102 THR D 105 1 O LYS D 103 N VAL D 11
SHEET 3 AB1 5 ASP D 85 ALA D 91 -1 N TYR D 86 O THR D 102
SHEET 4 AB1 5 VAL D 33 GLN D 38 -1 N SER D 34 O ALA D 89
SHEET 5 AB1 5 LYS D 45 ILE D 48 -1 O LEU D 47 N TRP D 35
SHEET 1 AB2 4 SER D 9 SER D 12 0
SHEET 2 AB2 4 THR D 102 THR D 105 1 O LYS D 103 N VAL D 11
SHEET 3 AB2 4 ASP D 85 ALA D 91 -1 N TYR D 86 O THR D 102
SHEET 4 AB2 4 TYR D 96 PHE D 98 -1 O VAL D 97 N SER D 90
SHEET 1 AB3 3 ILE D 19 THR D 24 0
SHEET 2 AB3 3 THR D 70 ILE D 75 -1 O ALA D 71 N CYS D 23
SHEET 3 AB3 3 PHE D 62 SER D 67 -1 N SER D 63 O THR D 74
SHEET 1 AB4 3 ILE E 24 LEU E 30 0
SHEET 2 AB4 3 GLU E 40 LYS E 45 -1 O GLU E 40 N LEU E 30
SHEET 3 AB4 3 ILE E 50 VAL E 53 -1 O VAL E 51 N VAL E 43
SHEET 1 AB5 3 ILE F 24 LEU F 30 0
SHEET 2 AB5 3 GLU F 40 LYS F 45 -1 O TRP F 44 N ARG F 26
SHEET 3 AB5 3 ILE F 50 VAL F 53 -1 O VAL F 51 N VAL F 43
SSBOND 1 CYS A 22 CYS A 92 1555 1555 2.04
SSBOND 2 CYS B 23 CYS B 88 1555 1555 2.03
SSBOND 3 CYS C 22 CYS C 92 1555 1555 2.04
SSBOND 4 CYS D 23 CYS D 88 1555 1555 2.03
SSBOND 5 CYS E 9 CYS E 36 1555 1555 2.03
SSBOND 6 CYS E 11 CYS E 52 1555 1555 2.05
SSBOND 7 CYS F 9 CYS F 36 1555 1555 2.04
SSBOND 8 CYS F 11 CYS F 52 1555 1555 2.03
CISPEP 1 SER A 112 SER A 113 0 1.10
CISPEP 2 SER D 56 GLY D 57 0 2.08
CISPEP 3 THR F 5 SER F 6 0 -1.66
CISPEP 4 ASN F 34 GLY F 35 0 -2.41
SITE 1 AC1 4 ASP A 100H ALA A 100I TRP B 32 ASP B 50
CRYST1 125.000 125.000 98.000 90.00 90.00 120.00 P 31 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 0.008000 0.004619 0.000000 0.00000
SCALE2 0.000000 0.009238 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010204 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
