HEADER IMMUNE SYSTEM 13-AUG-13 4M8Q
TITLE ONTOGENY OF RECOGNITION SPECIFICITY AND FUNCTIONALITY FOR THE ANTI-HIV
TITLE 2 NEUTRALIZING ANTIBODY 4E10
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GEP1 FV HEAVY CHAIN;
COMPND 3 CHAIN: A, H;
COMPND 4 ENGINEERED: YES;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: GEP1 FV LIGHT CHAIN;
COMPND 7 CHAIN: B, L;
COMPND 8 FRAGMENT: UNP RESIDUES 21-129;
COMPND 9 SYNONYM: IG KAPPA CHAIN V-III REGION HIC;
COMPND 10 ENGINEERED: YES;
COMPND 11 MOL_ID: 3;
COMPND 12 MOLECULE: 4E10 EPITOPE SCAFFOLD T117;
COMPND 13 CHAIN: C, S;
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 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 MOL_ID: 2;
SOURCE 8 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 9 ORGANISM_COMMON: HUMAN;
SOURCE 10 ORGANISM_TAXID: 9606;
SOURCE 11 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 12 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 13 MOL_ID: 3;
SOURCE 14 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;
SOURCE 15 ORGANISM_TAXID: 32630;
SOURCE 16 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 17 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS HIV, 4E10, GEP, GERMLINE, FV, IMMUNOGLOBULIN, ANTIBODY, 4E10 EPITOPE,
KEYWDS 2 IMMUNE SYSTEM
EXPDTA X-RAY DIFFRACTION
AUTHOR K.A.K.FINTON
REVDAT 2 07-MAR-18 4M8Q 1 REMARK
REVDAT 1 08-OCT-14 4M8Q 0
JRNL AUTH K.A.FINTON,D.FRIEND,J.JAFFE,M.GEWE,M.A.HOLMES,H.B.LARMAN,
JRNL AUTH 2 A.STUART,K.LARIMORE,P.D.GREENBERG,S.J.ELLEDGE,L.STAMATATOS,
JRNL AUTH 3 R.K.STRONG
JRNL TITL ONTOGENY OF RECOGNITION SPECIFICITY AND FUNCTIONALITY FOR
JRNL TITL 2 THE BROADLY NEUTRALIZING ANTI-HIV ANTIBODY 4E10.
JRNL REF PLOS PATHOG. V. 10 04403 2014
JRNL REFN ISSN 1553-7366
JRNL PMID 25254371
JRNL DOI 10.1371/JOURNAL.PPAT.1004403
REMARK 2
REMARK 2 RESOLUTION. 2.89 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.7.0029
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.89
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 24.61
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.1
REMARK 3 NUMBER OF REFLECTIONS : 17070
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) : 0.263
REMARK 3 R VALUE (WORKING SET) : 0.261
REMARK 3 FREE R VALUE : 0.302
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 919
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) : 2.89
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.96
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1147
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 92.99
REMARK 3 BIN R VALUE (WORKING SET) : 0.4400
REMARK 3 BIN FREE R VALUE SET COUNT : 74
REMARK 3 BIN FREE R VALUE : 0.6620
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5424
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 0
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 57.09
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.66000
REMARK 3 B22 (A**2) : 2.84000
REMARK 3 B33 (A**2) : -0.87000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -2.53000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 2.013
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.501
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.428
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 50.231
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.902
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.866
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 5563 ; 0.004 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 4823 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 7634 ; 0.733 ; 1.941
REMARK 3 BOND ANGLES OTHERS (DEGREES): 10987 ; 0.647 ; 3.001
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 758 ; 3.686 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 197 ;28.774 ;24.213
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 679 ;10.441 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 16 ;11.380 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 875 ; 0.046 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 6559 ; 0.002 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 1268 ; 0.000 ; 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): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
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 : 6
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 1 A 113
REMARK 3 ORIGIN FOR THE GROUP (A): 0.9710 -27.3830 -48.4360
REMARK 3 T TENSOR
REMARK 3 T11: 0.2448 T22: 0.2898
REMARK 3 T33: 0.2171 T12: 0.0876
REMARK 3 T13: -0.1541 T23: -0.0860
REMARK 3 L TENSOR
REMARK 3 L11: 3.8701 L22: 5.7089
REMARK 3 L33: 5.7228 L12: 0.0763
REMARK 3 L13: 0.4176 L23: -0.1736
REMARK 3 S TENSOR
REMARK 3 S11: 0.0635 S12: 0.0644 S13: -0.2207
REMARK 3 S21: 0.3086 S22: 0.0905 S23: -0.4695
REMARK 3 S31: 0.8574 S32: 0.0664 S33: -0.1540
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 1 B 105
REMARK 3 ORIGIN FOR THE GROUP (A): 7.7010 -14.8320 -32.4970
REMARK 3 T TENSOR
REMARK 3 T11: 0.2670 T22: 0.5840
REMARK 3 T33: 0.3635 T12: 0.2566
REMARK 3 T13: -0.2947 T23: -0.2738
REMARK 3 L TENSOR
REMARK 3 L11: 2.6837 L22: 3.8328
REMARK 3 L33: 7.5970 L12: -0.5510
REMARK 3 L13: 0.3484 L23: 0.3431
REMARK 3 S TENSOR
REMARK 3 S11: -0.3640 S12: -0.7738 S13: 0.5078
REMARK 3 S21: 0.3391 S22: 0.5379 S23: -0.2779
REMARK 3 S31: -0.1793 S32: 0.2332 S33: -0.1739
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 13 C 160
REMARK 3 ORIGIN FOR THE GROUP (A): 25.2650 8.1100 22.9780
REMARK 3 T TENSOR
REMARK 3 T11: 0.3562 T22: 0.3675
REMARK 3 T33: 0.4428 T12: -0.0557
REMARK 3 T13: 0.1677 T23: -0.0163
REMARK 3 L TENSOR
REMARK 3 L11: 5.0975 L22: 9.2318
REMARK 3 L33: 3.5947 L12: 2.3059
REMARK 3 L13: 0.5332 L23: 3.3906
REMARK 3 S TENSOR
REMARK 3 S11: 0.1255 S12: -0.3479 S13: 0.6192
REMARK 3 S21: 0.4418 S22: 0.0106 S23: 0.5803
REMARK 3 S31: -0.4603 S32: 0.2254 S33: -0.1361
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : H 1 H 112
REMARK 3 ORIGIN FOR THE GROUP (A): 16.7220 -17.7780 13.5210
REMARK 3 T TENSOR
REMARK 3 T11: 0.0648 T22: 0.2554
REMARK 3 T33: 0.0924 T12: 0.0001
REMARK 3 T13: 0.0762 T23: 0.0186
REMARK 3 L TENSOR
REMARK 3 L11: 5.4038 L22: 6.2989
REMARK 3 L33: 3.5426 L12: 0.0232
REMARK 3 L13: 0.2483 L23: 1.1953
REMARK 3 S TENSOR
REMARK 3 S11: 0.0475 S12: -0.1941 S13: -0.0363
REMARK 3 S21: 0.4785 S22: -0.1957 S23: 0.5545
REMARK 3 S31: 0.1601 S32: -0.0364 S33: 0.1482
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : L 1 L 105
REMARK 3 ORIGIN FOR THE GROUP (A): 18.6020 -12.8040 -7.1380
REMARK 3 T TENSOR
REMARK 3 T11: 0.1843 T22: 0.4114
REMARK 3 T33: 0.0961 T12: 0.1575
REMARK 3 T13: -0.0410 T23: 0.0691
REMARK 3 L TENSOR
REMARK 3 L11: 5.6378 L22: 4.5775
REMARK 3 L33: 9.3020 L12: -0.9260
REMARK 3 L13: -1.3282 L23: 2.1862
REMARK 3 S TENSOR
REMARK 3 S11: 0.4701 S12: 0.7297 S13: 0.1652
REMARK 3 S21: -0.6483 S22: -0.5464 S23: -0.0494
REMARK 3 S31: -0.6956 S32: 0.0167 S33: 0.0763
REMARK 3
REMARK 3 TLS GROUP : 6
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : S 8 S 161
REMARK 3 ORIGIN FOR THE GROUP (A): 11.5460 -10.2510 -68.1080
REMARK 3 T TENSOR
REMARK 3 T11: 0.3480 T22: 0.3682
REMARK 3 T33: 0.7500 T12: 0.0260
REMARK 3 T13: 0.2351 T23: -0.1968
REMARK 3 L TENSOR
REMARK 3 L11: 3.7919 L22: 5.0826
REMARK 3 L33: 3.7940 L12: -1.0586
REMARK 3 L13: -1.0748 L23: -0.9346
REMARK 3 S TENSOR
REMARK 3 S11: 0.2459 S12: 0.1293 S13: 0.7022
REMARK 3 S21: -0.9649 S22: 0.2601 S23: -0.8549
REMARK 3 S31: -0.4657 S32: 0.0921 S33: -0.5060
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
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 4M8Q COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 30-AUG-13.
REMARK 100 THE DEPOSITION ID IS D_1000081607.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 17-APR-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU MICROMAX-007 HF
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.54
REMARK 200 MONOCHROMATOR : OSMIC VARIMAX
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RIGAKU SATURN 944+
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 17941
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.890
REMARK 200 RESOLUTION RANGE LOW (A) : 24.610
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.89
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.95
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.8
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
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 (%): 46.38
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.29
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M KCL, 12% W/V PEG 8000, 5% V/V
REMARK 280 GLYCEROL, PH 7, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K
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 38.83700
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3
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: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3180 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 16540 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -25.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, S
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: 3080 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 16140 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -23.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, H, L
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: 3
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 8160 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 30780 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -61.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, S
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 APPLY THE FOLLOWING TO CHAINS: C, H, L
REMARK 350 BIOMT1 2 1.000000 0.000000 0.000000 -43.37021
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 -72.14095
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 -1
REMARK 465 SER A 0
REMARK 465 TRP A 100B
REMARK 465 LEU A 100C
REMARK 465 ILE B 106
REMARK 465 LYS B 107
REMARK 465 ARG B 108
REMARK 465 LEU B 109
REMARK 465 VAL B 110
REMARK 465 PRO B 111
REMARK 465 ARG B 112
REMARK 465 HIS C 1
REMARK 465 HIS C 2
REMARK 465 HIS C 3
REMARK 465 HIS C 4
REMARK 465 HIS C 5
REMARK 465 HIS C 6
REMARK 465 ASN C 7
REMARK 465 ALA C 8
REMARK 465 MET C 9
REMARK 465 GLN C 10
REMARK 465 GLY C 11
REMARK 465 ILE C 12
REMARK 465 GLU C 161
REMARK 465 GLY H -1
REMARK 465 SER H 0
REMARK 465 LEU H 100C
REMARK 465 SER H 113
REMARK 465 ILE L 106
REMARK 465 LYS L 107
REMARK 465 ARG L 108
REMARK 465 LEU L 109
REMARK 465 VAL L 110
REMARK 465 PRO L 111
REMARK 465 ARG L 112
REMARK 465 HIS S 1
REMARK 465 HIS S 2
REMARK 465 HIS S 3
REMARK 465 HIS S 4
REMARK 465 HIS S 5
REMARK 465 HIS S 6
REMARK 465 ASN S 7
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 11 CG1 CG2
REMARK 470 LYS A 12 CG CD CE NZ
REMARK 470 LYS A 13 CG CD CE NZ
REMARK 470 SER A 31 OG
REMARK 470 ILE A 34 CD1
REMARK 470 VAL A 37 CG1 CG2
REMARK 470 GLN A 61 CG CD OE1 NE2
REMARK 470 LYS A 62 CG CD CE NZ
REMARK 470 GLN A 64 CG CD OE1 NE2
REMARK 470 ARG A 66 CG CD NE CZ NH1 NH2
REMARK 470 VAL A 67 CG1 CG2
REMARK 470 SER A 82B OG
REMARK 470 LEU A 82C CG CD1 CD2
REMARK 470 ARG A 83 CG CD NE CZ NH1 NH2
REMARK 470 SER A 84 OG
REMARK 470 LYS A 100E CG CD CE NZ
REMARK 470 SER A 112 OG
REMARK 470 SER A 113 OG
REMARK 470 SER B 14 OG
REMARK 470 ARG B 18 CG CD NE CZ NH1 NH2
REMARK 470 ARG B 24 CG CD NE CZ NH1 NH2
REMARK 470 SER B 27A OG
REMARK 470 SER B 29 OG
REMARK 470 SER B 30 OG
REMARK 470 SER B 31 OG
REMARK 470 TYR B 32 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LEU B 33 CG CD1 CD2
REMARK 470 ASP B 60 CG OD1 OD2
REMARK 470 SER B 65 OG
REMARK 470 ASP B 70 CG OD1 OD2
REMARK 470 GLU B 81 CG CD OE1 OE2
REMARK 470 PHE B 83 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 SER B 94 OG
REMARK 470 LYS B 103 CG CD CE NZ
REMARK 470 GLU B 105 CG CD OE1 OE2
REMARK 470 ARG C 15 CG CD NE CZ NH1 NH2
REMARK 470 ARG C 16 CG CD NE CZ NH1 NH2
REMARK 470 HIS C 17 CG ND1 CD2 CE1 NE2
REMARK 470 ARG C 20 CZ NH1 NH2
REMARK 470 LEU C 22 CG CD1 CD2
REMARK 470 LYS C 24 CG CD CE NZ
REMARK 470 GLU C 25 CG CD OE1 OE2
REMARK 470 LYS C 33 CG CD CE NZ
REMARK 470 LEU C 35 CG CD1 CD2
REMARK 470 ILE C 40 CG1 CG2 CD1
REMARK 470 ASN C 41 CG OD1 ND2
REMARK 470 VAL C 45 CG1 CG2
REMARK 470 SER C 47 OG
REMARK 470 ARG C 56 CG CD NE CZ NH1 NH2
REMARK 470 GLN C 58 CG CD OE1 NE2
REMARK 470 GLU C 67 CG CD OE1 OE2
REMARK 470 VAL C 71 CG1 CG2
REMARK 470 ILE C 73 CD1
REMARK 470 LYS C 79 CG CD CE NZ
REMARK 470 GLN C 83 CG CD OE1 NE2
REMARK 470 ILE C 90 CD1
REMARK 470 GLU C 93 CG CD OE1 OE2
REMARK 470 GLU C 103 CG CD OE1 OE2
REMARK 470 VAL C 109 CG1 CG2
REMARK 470 ARG C 110 CG CD NE CZ NH1 NH2
REMARK 470 GLN C 135 CG CD OE1 NE2
REMARK 470 GLU C 137 CG CD OE1 OE2
REMARK 470 GLN C 141 CG CD OE1 NE2
REMARK 470 GLN C 142 CG CD OE1 NE2
REMARK 470 LEU C 144 CD1 CD2
REMARK 470 ILE C 151 CD1
REMARK 470 SER C 154 OG
REMARK 470 ILE C 155 CD1
REMARK 470 ARG C 158 CG CD NE
REMARK 470 ILE C 159 CD1
REMARK 470 SER C 160 OG
REMARK 470 GLN H 1 CG CD OE1 NE2
REMARK 470 VAL H 11 CG1 CG2
REMARK 470 LYS H 13 CG CD CE NZ
REMARK 470 SER H 16 OG
REMARK 470 SER H 17 OG
REMARK 470 SER H 30 OG
REMARK 470 SER H 31 OG
REMARK 470 PHE H 54 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 GLN H 61 CG CD OE1 NE2
REMARK 470 LYS H 62 CG CD CE NZ
REMARK 470 GLN H 64 CG CD OE1 NE2
REMARK 470 LYS H 73 CG CD CE NZ
REMARK 470 SER H 82B OG
REMARK 470 SER H 84 OG
REMARK 470 LYS H 100E CG CD CE NZ
REMARK 470 GLU L 1 CG CD OE1 OE2
REMARK 470 SER L 12 OG
REMARK 470 ARG L 18 CG CD NE CZ NH1 NH2
REMARK 470 SER L 29 OG
REMARK 470 SER L 30 OG
REMARK 470 ARG L 45 CG CD NE CZ NH1 NH2
REMARK 470 ASP L 60 CG OD1 OD2
REMARK 470 SER L 63 OG
REMARK 470 SER L 65 OG
REMARK 470 SER L 67 OG
REMARK 470 ASP L 70 CG OD1 OD2
REMARK 470 GLU L 81 CG CD OE1 OE2
REMARK 470 PHE L 83 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LYS L 103 CG CD CE NZ
REMARK 470 MET S 9 CG SD CE
REMARK 470 GLN S 10 CG CD OE1 NE2
REMARK 470 ILE S 12 CD1
REMARK 470 ARG S 15 CG CD NE CZ NH1 NH2
REMARK 470 ARG S 16 CG CD NE CZ NH1 NH2
REMARK 470 HIS S 17 CG ND1 CD2 CE1 NE2
REMARK 470 VAL S 19 CG1 CG2
REMARK 470 ARG S 20 CG CD NE CZ NH1 NH2
REMARK 470 LEU S 22 CG CD1 CD2
REMARK 470 LYS S 24 CG CD CE NZ
REMARK 470 GLU S 25 CG CD OE1 OE2
REMARK 470 VAL S 26 CG1 CG2
REMARK 470 GLN S 28 CG CD OE1 NE2
REMARK 470 ILE S 31 CG1 CG2 CD1
REMARK 470 LYS S 33 CG CD CE NZ
REMARK 470 LEU S 35 CG CD1 CD2
REMARK 470 ASN S 41 CG OD1 ND2
REMARK 470 ASP S 42 CG OD1 OD2
REMARK 470 VAL S 45 CG1 CG2
REMARK 470 ASP S 51 CG OD1 OD2
REMARK 470 THR S 55 OG1 CG2
REMARK 470 ARG S 56 CG CD NE CZ NH1 NH2
REMARK 470 GLN S 58 CG CD OE1 NE2
REMARK 470 SER S 78 OG
REMARK 470 GLN S 83 CG CD OE1 NE2
REMARK 470 VAL S 88 CG1 CG2
REMARK 470 ILE S 90 CD1
REMARK 470 LEU S 91 CG CD1 CD2
REMARK 470 GLU S 93 CG CD OE1 OE2
REMARK 470 VAL S 95 CG1 CG2
REMARK 470 GLU S 103 CG CD OE1 OE2
REMARK 470 ASP S 105 CG OD1 OD2
REMARK 470 VAL S 107 CG1 CG2
REMARK 470 ARG S 110 CG CD NE CZ NH1 NH2
REMARK 470 VAL S 126 CG1 CG2
REMARK 470 GLU S 137 CG CD OE1 OE2
REMARK 470 ASP S 138 CG OD1 OD2
REMARK 470 MET S 140 CE
REMARK 470 GLN S 142 CG CD OE1 NE2
REMARK 470 LEU S 144 O
REMARK 470 VAL S 145 CG1 CG2
REMARK 470 MET S 146 CE
REMARK 470 ASP S 149 CG OD1 OD2
REMARK 470 SER S 154 OG
REMARK 470 ILE S 155 CD1
REMARK 470 TYR S 156 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 THR S 157 OG1 CG2
REMARK 470 ARG S 158 CG CD NE CZ NH1 NH2
REMARK 470 ILE S 159 CG1 CG2 CD1
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 PRO A 41 109.90 -54.04
REMARK 500 LEU B 47 -62.09 -100.31
REMARK 500 ALA B 51 -62.82 67.64
REMARK 500 ASP C 48 43.71 -98.83
REMARK 500 GLN H 64 109.17 -59.07
REMARK 500 ALA L 51 -65.02 66.03
REMARK 500 ASP S 48 40.85 -99.62
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4M62 RELATED DB: PDB
DBREF 4M8Q B 1 108 UNP P18136 KV313_HUMAN 21 129
DBREF 4M8Q L 1 108 UNP P18136 KV313_HUMAN 21 129
DBREF 4M8Q A -1 113 PDB 4M8Q 4M8Q -1 113
DBREF 4M8Q H -1 113 PDB 4M8Q 4M8Q -1 113
DBREF 4M8Q C 1 161 PDB 4M8Q 4M8Q 1 161
DBREF 4M8Q S 1 161 PDB 4M8Q 4M8Q 1 161
SEQADV 4M8Q SER B 96 UNP P18136 TRP 117 CONFLICT
SEQADV 4M8Q LEU B 109 UNP P18136 EXPRESSION TAG
SEQADV 4M8Q VAL B 110 UNP P18136 EXPRESSION TAG
SEQADV 4M8Q PRO B 111 UNP P18136 EXPRESSION TAG
SEQADV 4M8Q ARG B 112 UNP P18136 EXPRESSION TAG
SEQADV 4M8Q SER L 96 UNP P18136 TRP 117 CONFLICT
SEQADV 4M8Q LEU L 109 UNP P18136 EXPRESSION TAG
SEQADV 4M8Q VAL L 110 UNP P18136 EXPRESSION TAG
SEQADV 4M8Q PRO L 111 UNP P18136 EXPRESSION TAG
SEQADV 4M8Q ARG L 112 UNP P18136 EXPRESSION TAG
SEQRES 1 A 129 GLY SER GLN VAL GLN LEU VAL GLN SER GLY ALA GLU VAL
SEQRES 2 A 129 LYS LYS PRO GLY SER SER VAL LYS VAL SER CYS LYS ALA
SEQRES 3 A 129 SER GLY GLY THR PHE SER SER TYR ALA ILE SER TRP VAL
SEQRES 4 A 129 ARG GLN ALA PRO GLY GLN GLY LEU GLU TRP MET GLY GLY
SEQRES 5 A 129 ILE ILE PRO ILE PHE GLY THR ALA ASN TYR ALA GLN LYS
SEQRES 6 A 129 PHE GLN GLY ARG VAL THR ILE THR ALA ASP LYS SER THR
SEQRES 7 A 129 SER THR ALA TYR MET GLU LEU SER SER LEU ARG SER GLU
SEQRES 8 A 129 ASP THR ALA VAL TYR TYR CYS ALA ARG GLU GLY THR THR
SEQRES 9 A 129 GLY TRP GLY TRP LEU GLY LYS PRO ILE GLY ALA PHE ALA
SEQRES 10 A 129 TYR TRP GLY GLN GLY THR LEU VAL THR VAL SER SER
SEQRES 1 B 113 GLU ILE VAL LEU THR GLN SER PRO GLY THR LEU SER LEU
SEQRES 2 B 113 SER PRO GLY GLU ARG ALA THR LEU SER CYS ARG ALA SER
SEQRES 3 B 113 GLN SER VAL SER SER SER TYR LEU ALA TRP TYR GLN GLN
SEQRES 4 B 113 LYS PRO GLY GLN ALA PRO ARG LEU LEU ILE TYR GLY ALA
SEQRES 5 B 113 SER SER ARG ALA THR GLY ILE PRO ASP ARG PHE SER GLY
SEQRES 6 B 113 SER GLY SER GLY THR ASP PHE THR LEU THR ILE SER ARG
SEQRES 7 B 113 LEU GLU PRO GLU ASP PHE ALA VAL TYR TYR CYS GLN GLN
SEQRES 8 B 113 TYR GLY SER SER PRO SER THR PHE GLY GLN GLY THR LYS
SEQRES 9 B 113 VAL GLU ILE LYS ARG LEU VAL PRO ARG
SEQRES 1 C 161 HIS HIS HIS HIS HIS HIS ASN ALA MET GLN GLY ILE HIS
SEQRES 2 C 161 PHE ARG ARG HIS TYR VAL ARG HIS LEU PRO LYS GLU VAL
SEQRES 3 C 161 SER GLN ASN ASP ILE ILE LYS ALA LEU ALA SER PRO LEU
SEQRES 4 C 161 ILE ASN ASP GLY MET VAL VAL SER ASP PHE ALA ASP HIS
SEQRES 5 C 161 VAL ILE THR ARG GLU GLN ASN PHE PRO THR GLY LEU PRO
SEQRES 6 C 161 VAL GLU PRO VAL GLY VAL ALA ILE PRO HIS THR ASP SER
SEQRES 7 C 161 LYS TYR VAL ARG GLN ASN ALA ILE SER VAL GLY ILE LEU
SEQRES 8 C 161 ALA GLU PRO VAL ASN PHE GLU ASP ALA GLY GLY GLU PRO
SEQRES 9 C 161 ASP PRO VAL PRO VAL ARG VAL VAL PHE MET LEU ALA LEU
SEQRES 10 C 161 GLY ASN TRP PHE ASP ILE THR ASN VAL LEU TRP TRP ILE
SEQRES 11 C 161 MET ASP VAL ILE GLN ASP GLU ASP PHE MET GLN GLN LEU
SEQRES 12 C 161 LEU VAL MET ASN ASP ASP GLU ILE TYR GLN SER ILE TYR
SEQRES 13 C 161 THR ARG ILE SER GLU
SEQRES 1 H 129 GLY SER GLN VAL GLN LEU VAL GLN SER GLY ALA GLU VAL
SEQRES 2 H 129 LYS LYS PRO GLY SER SER VAL LYS VAL SER CYS LYS ALA
SEQRES 3 H 129 SER GLY GLY THR PHE SER SER TYR ALA ILE SER TRP VAL
SEQRES 4 H 129 ARG GLN ALA PRO GLY GLN GLY LEU GLU TRP MET GLY GLY
SEQRES 5 H 129 ILE ILE PRO ILE PHE GLY THR ALA ASN TYR ALA GLN LYS
SEQRES 6 H 129 PHE GLN GLY ARG VAL THR ILE THR ALA ASP LYS SER THR
SEQRES 7 H 129 SER THR ALA TYR MET GLU LEU SER SER LEU ARG SER GLU
SEQRES 8 H 129 ASP THR ALA VAL TYR TYR CYS ALA ARG GLU GLY THR THR
SEQRES 9 H 129 GLY TRP GLY TRP LEU GLY LYS PRO ILE GLY ALA PHE ALA
SEQRES 10 H 129 TYR TRP GLY GLN GLY THR LEU VAL THR VAL SER SER
SEQRES 1 L 113 GLU ILE VAL LEU THR GLN SER PRO GLY THR LEU SER LEU
SEQRES 2 L 113 SER PRO GLY GLU ARG ALA THR LEU SER CYS ARG ALA SER
SEQRES 3 L 113 GLN SER VAL SER SER SER TYR LEU ALA TRP TYR GLN GLN
SEQRES 4 L 113 LYS PRO GLY GLN ALA PRO ARG LEU LEU ILE TYR GLY ALA
SEQRES 5 L 113 SER SER ARG ALA THR GLY ILE PRO ASP ARG PHE SER GLY
SEQRES 6 L 113 SER GLY SER GLY THR ASP PHE THR LEU THR ILE SER ARG
SEQRES 7 L 113 LEU GLU PRO GLU ASP PHE ALA VAL TYR TYR CYS GLN GLN
SEQRES 8 L 113 TYR GLY SER SER PRO SER THR PHE GLY GLN GLY THR LYS
SEQRES 9 L 113 VAL GLU ILE LYS ARG LEU VAL PRO ARG
SEQRES 1 S 161 HIS HIS HIS HIS HIS HIS ASN ALA MET GLN GLY ILE HIS
SEQRES 2 S 161 PHE ARG ARG HIS TYR VAL ARG HIS LEU PRO LYS GLU VAL
SEQRES 3 S 161 SER GLN ASN ASP ILE ILE LYS ALA LEU ALA SER PRO LEU
SEQRES 4 S 161 ILE ASN ASP GLY MET VAL VAL SER ASP PHE ALA ASP HIS
SEQRES 5 S 161 VAL ILE THR ARG GLU GLN ASN PHE PRO THR GLY LEU PRO
SEQRES 6 S 161 VAL GLU PRO VAL GLY VAL ALA ILE PRO HIS THR ASP SER
SEQRES 7 S 161 LYS TYR VAL ARG GLN ASN ALA ILE SER VAL GLY ILE LEU
SEQRES 8 S 161 ALA GLU PRO VAL ASN PHE GLU ASP ALA GLY GLY GLU PRO
SEQRES 9 S 161 ASP PRO VAL PRO VAL ARG VAL VAL PHE MET LEU ALA LEU
SEQRES 10 S 161 GLY ASN TRP PHE ASP ILE THR ASN VAL LEU TRP TRP ILE
SEQRES 11 S 161 MET ASP VAL ILE GLN ASP GLU ASP PHE MET GLN GLN LEU
SEQRES 12 S 161 LEU VAL MET ASN ASP ASP GLU ILE TYR GLN SER ILE TYR
SEQRES 13 S 161 THR ARG ILE SER GLU
HELIX 1 1 ARG A 83 THR A 87 5 5
HELIX 2 2 SER B 29 SER B 31 5 3
HELIX 3 3 GLU B 79 PHE B 83 5 5
HELIX 4 4 ARG C 15 HIS C 17 5 3
HELIX 5 5 SER C 27 ASP C 42 1 16
HELIX 6 6 ASP C 48 PHE C 60 1 13
HELIX 7 7 ASP C 77 VAL C 81 5 5
HELIX 8 8 ASN C 119 PHE C 121 5 3
HELIX 9 9 ASP C 122 GLN C 135 1 14
HELIX 10 10 ASP C 136 MET C 146 1 11
HELIX 11 11 ASN C 147 SER C 160 1 14
HELIX 12 12 ARG H 83 THR H 87 5 5
HELIX 13 13 SER L 29 SER L 31 5 3
HELIX 14 14 GLU L 79 PHE L 83 5 5
HELIX 15 15 ARG S 15 HIS S 17 5 3
HELIX 16 16 SER S 27 ASP S 42 1 16
HELIX 17 17 ASP S 48 PHE S 60 1 13
HELIX 18 18 ASP S 77 VAL S 81 5 5
HELIX 19 19 ASN S 119 PHE S 121 5 3
HELIX 20 20 ASP S 122 ASP S 136 1 15
HELIX 21 21 ASP S 136 LEU S 144 1 9
HELIX 22 22 ASN S 147 SER S 160 1 14
SHEET 1 A 4 GLN A 3 GLN A 6 0
SHEET 2 A 4 VAL A 18 SER A 25 -1 O LYS A 23 N VAL A 5
SHEET 3 A 4 THR A 77 LEU A 82 -1 O ALA A 78 N CYS A 22
SHEET 4 A 4 VAL A 67 ASP A 72 -1 N THR A 70 O TYR A 79
SHEET 1 B 6 GLU A 10 LYS A 12 0
SHEET 2 B 6 THR A 107 VAL A 111 1 O THR A 110 N GLU A 10
SHEET 3 B 6 ALA A 88 THR A 97 -1 N TYR A 90 O THR A 107
SHEET 4 B 6 ILE A 34 ALA A 40 -1 N VAL A 37 O TYR A 91
SHEET 5 B 6 GLY A 44 ILE A 52 -1 O GLY A 49 N TRP A 36
SHEET 6 B 6 THR A 56 TYR A 59 -1 O ASN A 58 N GLY A 50
SHEET 1 C 4 GLU A 10 LYS A 12 0
SHEET 2 C 4 THR A 107 VAL A 111 1 O THR A 110 N GLU A 10
SHEET 3 C 4 ALA A 88 THR A 97 -1 N TYR A 90 O THR A 107
SHEET 4 C 4 PRO A 100F TRP A 103 -1 O TYR A 102 N ARG A 94
SHEET 1 D 3 LEU B 4 SER B 7 0
SHEET 2 D 3 ALA B 19 VAL B 28 -1 O SER B 22 N SER B 7
SHEET 3 D 3 PHE B 62 ILE B 75 -1 O LEU B 73 N LEU B 21
SHEET 1 E12 SER B 53 ARG B 54 0
SHEET 2 E12 ARG B 45 TYR B 49 -1 N TYR B 49 O SER B 53
SHEET 3 E12 LEU B 33 GLN B 38 -1 N GLN B 37 O ARG B 45
SHEET 4 E12 ALA B 84 GLN B 90 -1 O TYR B 87 N TYR B 36
SHEET 5 E12 THR B 102 VAL B 104 -1 O THR B 102 N TYR B 86
SHEET 6 E12 THR B 10 SER B 12 1 N LEU B 11 O LYS B 103
SHEET 7 E12 THR L 10 SER L 12 -1 O SER L 12 N THR B 10
SHEET 8 E12 THR L 102 VAL L 104 1 O LYS L 103 N LEU L 11
SHEET 9 E12 VAL L 85 GLN L 90 -1 N TYR L 86 O THR L 102
SHEET 10 E12 LEU L 33 GLN L 38 -1 N TYR L 36 O TYR L 87
SHEET 11 E12 ARG L 45 TYR L 49 -1 O ARG L 45 N GLN L 37
SHEET 12 E12 SER L 53 ARG L 54 -1 O SER L 53 N TYR L 49
SHEET 1 F 8 THR B 97 PHE B 98 0
SHEET 2 F 8 ALA B 84 GLN B 90 -1 N GLN B 90 O THR B 97
SHEET 3 F 8 THR B 102 VAL B 104 -1 O THR B 102 N TYR B 86
SHEET 4 F 8 THR B 10 SER B 12 1 N LEU B 11 O LYS B 103
SHEET 5 F 8 THR L 10 SER L 12 -1 O SER L 12 N THR B 10
SHEET 6 F 8 THR L 102 VAL L 104 1 O LYS L 103 N LEU L 11
SHEET 7 F 8 VAL L 85 GLN L 90 -1 N TYR L 86 O THR L 102
SHEET 8 F 8 THR L 97 PHE L 98 -1 O THR L 97 N GLN L 90
SHEET 1 G 5 VAL C 19 LEU C 22 0
SHEET 2 G 5 ALA C 85 PHE C 97 1 O ILE C 90 N LEU C 22
SHEET 3 G 5 VAL C 107 ALA C 116 -1 O VAL C 112 N GLY C 89
SHEET 4 G 5 GLY C 70 ALA C 72 1 N ALA C 72 O PHE C 113
SHEET 5 G 5 GLY C 63 LEU C 64 -1 N LEU C 64 O VAL C 71
SHEET 1 H 4 GLN H 3 GLN H 6 0
SHEET 2 H 4 VAL H 18 SER H 25 -1 O LYS H 23 N VAL H 5
SHEET 3 H 4 THR H 77 LEU H 82 -1 O ALA H 78 N CYS H 22
SHEET 4 H 4 VAL H 67 ASP H 72 -1 N ASP H 72 O THR H 77
SHEET 1 I 6 GLU H 10 LYS H 12 0
SHEET 2 I 6 THR H 107 VAL H 111 1 O THR H 110 N GLU H 10
SHEET 3 I 6 ALA H 88 THR H 97 -1 N TYR H 90 O THR H 107
SHEET 4 I 6 ILE H 34 GLN H 39 -1 N VAL H 37 O TYR H 91
SHEET 5 I 6 LEU H 45 ILE H 52 -1 O GLY H 49 N TRP H 36
SHEET 6 I 6 THR H 56 TYR H 59 -1 O ASN H 58 N GLY H 50
SHEET 1 J 4 GLU H 10 LYS H 12 0
SHEET 2 J 4 THR H 107 VAL H 111 1 O THR H 110 N GLU H 10
SHEET 3 J 4 ALA H 88 THR H 97 -1 N TYR H 90 O THR H 107
SHEET 4 J 4 PRO H 100F TRP H 103 -1 O TYR H 102 N ARG H 94
SHEET 1 K 3 LEU L 4 SER L 7 0
SHEET 2 K 3 ALA L 19 VAL L 28 -1 O SER L 22 N SER L 7
SHEET 3 K 3 PHE L 62 ILE L 75 -1 O LEU L 73 N LEU L 21
SHEET 1 L 5 VAL S 19 LEU S 22 0
SHEET 2 L 5 ALA S 85 PHE S 97 1 O ILE S 90 N LEU S 22
SHEET 3 L 5 VAL S 107 ALA S 116 -1 O VAL S 112 N GLY S 89
SHEET 4 L 5 GLY S 70 ALA S 72 1 N ALA S 72 O PHE S 113
SHEET 5 L 5 GLY S 63 LEU S 64 -1 N LEU S 64 O VAL S 71
SSBOND 1 CYS A 22 CYS A 92 1555 1555 2.03
SSBOND 2 CYS B 23 CYS B 88 1555 1555 2.03
SSBOND 3 CYS H 22 CYS H 92 1555 1555 2.03
SSBOND 4 CYS L 23 CYS L 88 1555 1555 2.04
CISPEP 1 SER B 7 PRO B 8 0 0.14
CISPEP 2 SER B 94 PRO B 95 0 -0.47
CISPEP 3 GLU C 67 PRO C 68 0 -0.50
CISPEP 4 SER L 7 PRO L 8 0 1.15
CISPEP 5 SER L 94 PRO L 95 0 1.22
CISPEP 6 GLU S 67 PRO S 68 0 0.04
CRYST1 72.561 77.674 77.823 90.00 112.03 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 0.013782 0.000000 0.005576 0.00000
SCALE2 0.000000 0.012874 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013862 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
