HEADER IMMUNE SYSTEM 18-SEP-00 1FV1
TITLE STRUCTURAL BASIS FOR THE BINDING OF AN IMMUNODOMINANT PEPTIDE FROM
TITLE 2 MYELIN BASIC PROTEIN IN DIFFERENT REGISTERS BY TWO HLA-DR2 ALLELES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MAJOR HISTOCOMPATIBILITY COMPLEX ALPHA CHAIN;
COMPND 3 CHAIN: A, D;
COMPND 4 ENGINEERED: YES;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: MAJOR HISTOCOMPATIBILITY COMPLEX BETA CHAIN;
COMPND 7 CHAIN: B, E;
COMPND 8 ENGINEERED: YES;
COMPND 9 MOL_ID: 3;
COMPND 10 MOLECULE: MYELIN BASIC PROTEIN;
COMPND 11 CHAIN: C, F;
COMPND 12 FRAGMENT: RESIDUES 86-105;
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: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 OTHER_DETAILS: HOMO SAPIENS;
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: ESCHERICHIA COLI;
SOURCE 13 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 14 OTHER_DETAILS: HOMO SAPIENS;
SOURCE 15 MOL_ID: 3;
SOURCE 16 SYNTHETIC: YES;
SOURCE 17 OTHER_DETAILS: THE PEPTIDE WAS CHEMICALLY SYNTHESIZED. THE SEQUENCE
SOURCE 18 OF THE PEPTIDE IS NATURALLY FOUND IN HOMO SAPIENS (HUMAN).
KEYWDS MHC CLASS II DR2A, IMMUNE SYSTEM
EXPDTA X-RAY DIFFRACTION
AUTHOR H.LI,A.R.MARIUZZA,Y.LI,R.MARTIN
REVDAT 5 13-JUL-11 1FV1 1 VERSN
REVDAT 4 24-FEB-09 1FV1 1 VERSN
REVDAT 3 01-APR-03 1FV1 1 JRNL
REVDAT 2 22-NOV-00 1FV1 1 JRNL
REVDAT 1 27-SEP-00 1FV1 0
JRNL AUTH Y.LI,H.LI,R.MARTIN,R.A.MARIUZZA
JRNL TITL STRUCTURAL BASIS FOR THE BINDING OF AN IMMUNODOMINANT
JRNL TITL 2 PEPTIDE FROM MYELIN BASIC PROTEIN IN DIFFERENT REGISTERS BY
JRNL TITL 3 TWO HLA-DR2 PROTEINS.
JRNL REF J.MOL.BIOL. V. 304 177 2000
JRNL REFN ISSN 0022-2836
JRNL PMID 11080454
JRNL DOI 10.1006/JMBI.2000.4198
REMARK 2
REMARK 2 RESOLUTION. 1.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 100.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 63997
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.233
REMARK 3 FREE R VALUE : 0.267
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 3233
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 : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
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 : 6248
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 27
REMARK 3 SOLVENT ATOMS : 494
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 20.50
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.006
REMARK 3 BOND ANGLES (DEGREES) : 1.50
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : NULL
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1FV1 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 19-SEP-00.
REMARK 100 THE RCSB ID CODE IS RCSB011923.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 07-NOV-99
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X12B
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.978
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : CCP4 (TRUNCATE)
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 49803
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900
REMARK 200 RESOLUTION RANGE LOW (A) : 100.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 0.8
REMARK 200 DATA REDUNDANCY : 2.800
REMARK 200 R MERGE (I) : 0.08100
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 0.0810
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.99
REMARK 200 COMPLETENESS FOR SHELL (%) : 0.8
REMARK 200 DATA REDUNDANCY IN SHELL : 2.80
REMARK 200 R MERGE FOR SHELL (I) : 0.34900
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: NULL
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 51.05
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.51
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 2/3 DILUTION OF 30% PEG 8000, 0.1M
REMARK 280 SODIUM CACODYLATE, PH6.5, 0.2M AMMONIUM SULFATE, EVAPORATION,
REMARK 280 TEMPERATURE 298.0K
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 57.44600
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
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: 7450 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 18500 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -49.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C
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: 7810 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 18760 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -56.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, E, 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 ILE A 1
REMARK 465 LYS A 2
REMARK 465 ILE D 1
REMARK 465 LYS D 2
REMARK 465 GLU D 3
REMARK 465 ASN F 86
REMARK 465 GLN F 105
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 LYS A 39 CD CE NZ
REMARK 470 GLU A 98 CD OE1 OE2
REMARK 470 LEU A 99 CG CD1 CD2
REMARK 470 ARG A 100 CG CD NE CZ NH1 NH2
REMARK 470 ASN B 19 CG OD1
REMARK 470 LYS B 65 CG CD CE NZ
REMARK 470 LEU B 109 CG CD1 CD2
REMARK 470 GLN B 110 CG CD OE1 NE2
REMARK 470 HIS B 111 CG ND1 CD2 CE1 NE2
REMARK 470 ARG B 130 NE CZ NH1 NH2
REMARK 470 GLN B 136 CG CD OE1 NE2
REMARK 470 GLU B 137 CG CD OE1 OE2
REMARK 470 GLU B 138 CG CD OE1 OE2
REMARK 470 LYS B 139 CG CD CE NZ
REMARK 470 GLU B 162 CG CD OE1 OE2
REMARK 470 ARG B 166 CD NE CZ NH1 NH2
REMARK 470 ARG B 189 CG CD NE CZ NH1 NH2
REMARK 470 ASN C 86 CB CG OD1
REMARK 470 GLN C 105 CB CG CD OE1 NE2
REMARK 470 ARG D 100 CG CD NE CZ NH1 NH2
REMARK 470 GLU D 158 CG CD OE1 OE2
REMARK 470 LYS E 65 CG CD CE NZ
REMARK 470 LEU E 109 CB CG CD1 CD2
REMARK 470 GLN E 110 CB CG CD OE1 NE2
REMARK 470 HIS E 111 CB CG ND1 CD2 CE1 NE2
REMARK 470 ASN E 134 CB CG OD1
REMARK 470 SER E 135 CB OG
REMARK 470 GLN E 136 CG CD OE1 NE2
REMARK 470 GLU E 138 CG CD OE1 OE2
REMARK 470 GLU E 162 CG CD OE1 OE2
REMARK 470 ARG E 166 NE CZ NH1 NH2
REMARK 470 ARG E 189 CG CD NE CZ NH1 NH2
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 ASN A 78 33.81 75.25
REMARK 500 ARG A 100 -5.19 70.85
REMARK 500 ASN B 19 77.71 49.93
REMARK 500 ASN B 33 -102.47 59.49
REMARK 500 THR B 90 -73.28 -130.55
REMARK 500 LEU B 109 117.75 85.00
REMARK 500 GLN B 110 71.17 -119.62
REMARK 500 HIS B 111 -19.03 -169.48
REMARK 500 TYR B 123 134.71 -170.53
REMARK 500 ASN B 134 -42.18 81.31
REMARK 500 SER B 135 36.69 175.28
REMARK 500 GLU B 137 109.69 -52.06
REMARK 500 PRO B 165 103.55 -45.00
REMARK 500 VAL C 88 123.63 79.13
REMARK 500 SER C 104 131.62 78.28
REMARK 500 ARG D 100 -11.50 71.19
REMARK 500 ASN E 19 78.56 47.91
REMARK 500 ASN E 33 -102.17 61.22
REMARK 500 SER E 63 3.65 -68.41
REMARK 500 GLN E 64 74.76 -107.42
REMARK 500 TYR E 78 -67.67 -108.18
REMARK 500 THR E 90 -72.54 -127.69
REMARK 500 LEU E 109 116.99 86.95
REMARK 500 GLN E 110 68.33 -117.37
REMARK 500 HIS E 111 -28.60 -160.09
REMARK 500 PRO E 124 -177.81 -70.00
REMARK 500 ASN E 134 -59.77 96.38
REMARK 500 SER E 135 38.83 -177.07
REMARK 500 PRO E 165 106.60 -47.75
REMARK 500 ARG E 189 77.25 70.35
REMARK 500 VAL F 88 127.61 80.10
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 A 212 DISTANCE = 5.12 ANGSTROMS
REMARK 525 HOH A 273 DISTANCE = 5.16 ANGSTROMS
REMARK 525 HOH A 298 DISTANCE = 6.30 ANGSTROMS
REMARK 525 HOH A 322 DISTANCE = 5.83 ANGSTROMS
REMARK 525 HOH B 239 DISTANCE = 5.42 ANGSTROMS
REMARK 525 HOH D 264 DISTANCE = 5.12 ANGSTROMS
REMARK 525 HOH D 268 DISTANCE = 5.09 ANGSTROMS
REMARK 525 HOH D 278 DISTANCE = 5.67 ANGSTROMS
REMARK 525 HOH D 284 DISTANCE = 5.33 ANGSTROMS
REMARK 525 HOH D 290 DISTANCE = 6.51 ANGSTROMS
REMARK 525 HOH D 300 DISTANCE = 6.02 ANGSTROMS
REMARK 525 HOH D 311 DISTANCE = 5.27 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 182
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 182
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 191
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL D 183
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 192
DBREF 1FV1 A 1 181 UNP P01903 2DRA_HUMAN 26 206
DBREF 1FV1 B 1 190 UNP Q30154 Q30154_HUMAN 30 219
DBREF 1FV1 C 86 105 UNP P02686 MBP_HUMAN 218 237
DBREF 1FV1 D 1 181 UNP P01903 2DRA_HUMAN 26 206
DBREF 1FV1 E 1 190 UNP Q30154 Q30154_HUMAN 30 219
DBREF 1FV1 F 86 105 UNP P02686 MBP_HUMAN 218 237
SEQRES 1 A 181 ILE LYS GLU GLU HIS VAL ILE ILE GLN ALA GLU PHE TYR
SEQRES 2 A 181 LEU ASN PRO ASP GLN SER GLY GLU PHE MET PHE ASP PHE
SEQRES 3 A 181 ASP GLY ASP GLU ILE PHE HIS VAL ASP MET ALA LYS LYS
SEQRES 4 A 181 GLU THR VAL TRP ARG LEU GLU GLU PHE GLY ARG PHE ALA
SEQRES 5 A 181 SER PHE GLU ALA GLN GLY ALA LEU ALA ASN ILE ALA VAL
SEQRES 6 A 181 ASP LYS ALA ASN LEU GLU ILE MET THR LYS ARG SER ASN
SEQRES 7 A 181 TYR THR PRO ILE THR ASN VAL PRO PRO GLU VAL THR VAL
SEQRES 8 A 181 LEU THR ASN SER PRO VAL GLU LEU ARG GLU PRO ASN VAL
SEQRES 9 A 181 LEU ILE CYS PHE ILE ASP LYS PHE THR PRO PRO VAL VAL
SEQRES 10 A 181 ASN VAL THR TRP LEU ARG ASN GLY LYS PRO VAL THR THR
SEQRES 11 A 181 GLY VAL SER GLU THR VAL PHE LEU PRO ARG GLU ASP HIS
SEQRES 12 A 181 LEU PHE ARG LYS PHE HIS TYR LEU PRO PHE LEU PRO SER
SEQRES 13 A 181 THR GLU ASP VAL TYR ASP CYS ARG VAL GLU HIS TRP GLY
SEQRES 14 A 181 LEU ASP GLU PRO LEU LEU LYS HIS TRP GLU PHE ASP
SEQRES 1 B 190 GLY ASP THR ARG PRO ARG PHE LEU GLN GLN ASP LYS TYR
SEQRES 2 B 190 GLU CYS HIS PHE PHE ASN GLY THR GLU ARG VAL ARG PHE
SEQRES 3 B 190 LEU HIS ARG ASP ILE TYR ASN GLN GLU GLU ASP LEU ARG
SEQRES 4 B 190 PHE ASP SER ASP VAL GLY GLU TYR ARG ALA VAL THR GLU
SEQRES 5 B 190 LEU GLY ARG PRO ASP ALA GLU TYR TRP ASN SER GLN LYS
SEQRES 6 B 190 ASP PHE LEU GLU ASP ARG ARG ALA ALA VAL ASP THR TYR
SEQRES 7 B 190 CYS ARG HIS ASN TYR GLY VAL GLY GLU SER PHE THR VAL
SEQRES 8 B 190 GLN ARG ARG VAL GLU PRO LYS VAL THR VAL TYR PRO ALA
SEQRES 9 B 190 ARG THR GLN THR LEU GLN HIS HIS ASN LEU LEU VAL CYS
SEQRES 10 B 190 SER VAL ASN GLY PHE TYR PRO GLY SER ILE GLU VAL ARG
SEQRES 11 B 190 TRP PHE ARG ASN SER GLN GLU GLU LYS ALA GLY VAL VAL
SEQRES 12 B 190 SER THR GLY LEU ILE GLN ASN GLY ASP TRP THR PHE GLN
SEQRES 13 B 190 THR LEU VAL MET LEU GLU THR VAL PRO ARG SER GLY GLU
SEQRES 14 B 190 VAL TYR THR CYS GLN VAL GLU HIS PRO SER VAL THR SER
SEQRES 15 B 190 PRO LEU THR VAL GLU TRP ARG ALA
SEQRES 1 C 20 ASN PRO VAL VAL HIS PHE PHE LYS ASN ILE VAL THR PRO
SEQRES 2 C 20 ARG THR PRO PRO PRO SER GLN
SEQRES 1 D 181 ILE LYS GLU GLU HIS VAL ILE ILE GLN ALA GLU PHE TYR
SEQRES 2 D 181 LEU ASN PRO ASP GLN SER GLY GLU PHE MET PHE ASP PHE
SEQRES 3 D 181 ASP GLY ASP GLU ILE PHE HIS VAL ASP MET ALA LYS LYS
SEQRES 4 D 181 GLU THR VAL TRP ARG LEU GLU GLU PHE GLY ARG PHE ALA
SEQRES 5 D 181 SER PHE GLU ALA GLN GLY ALA LEU ALA ASN ILE ALA VAL
SEQRES 6 D 181 ASP LYS ALA ASN LEU GLU ILE MET THR LYS ARG SER ASN
SEQRES 7 D 181 TYR THR PRO ILE THR ASN VAL PRO PRO GLU VAL THR VAL
SEQRES 8 D 181 LEU THR ASN SER PRO VAL GLU LEU ARG GLU PRO ASN VAL
SEQRES 9 D 181 LEU ILE CYS PHE ILE ASP LYS PHE THR PRO PRO VAL VAL
SEQRES 10 D 181 ASN VAL THR TRP LEU ARG ASN GLY LYS PRO VAL THR THR
SEQRES 11 D 181 GLY VAL SER GLU THR VAL PHE LEU PRO ARG GLU ASP HIS
SEQRES 12 D 181 LEU PHE ARG LYS PHE HIS TYR LEU PRO PHE LEU PRO SER
SEQRES 13 D 181 THR GLU ASP VAL TYR ASP CYS ARG VAL GLU HIS TRP GLY
SEQRES 14 D 181 LEU ASP GLU PRO LEU LEU LYS HIS TRP GLU PHE ASP
SEQRES 1 E 190 GLY ASP THR ARG PRO ARG PHE LEU GLN GLN ASP LYS TYR
SEQRES 2 E 190 GLU CYS HIS PHE PHE ASN GLY THR GLU ARG VAL ARG PHE
SEQRES 3 E 190 LEU HIS ARG ASP ILE TYR ASN GLN GLU GLU ASP LEU ARG
SEQRES 4 E 190 PHE ASP SER ASP VAL GLY GLU TYR ARG ALA VAL THR GLU
SEQRES 5 E 190 LEU GLY ARG PRO ASP ALA GLU TYR TRP ASN SER GLN LYS
SEQRES 6 E 190 ASP PHE LEU GLU ASP ARG ARG ALA ALA VAL ASP THR TYR
SEQRES 7 E 190 CYS ARG HIS ASN TYR GLY VAL GLY GLU SER PHE THR VAL
SEQRES 8 E 190 GLN ARG ARG VAL GLU PRO LYS VAL THR VAL TYR PRO ALA
SEQRES 9 E 190 ARG THR GLN THR LEU GLN HIS HIS ASN LEU LEU VAL CYS
SEQRES 10 E 190 SER VAL ASN GLY PHE TYR PRO GLY SER ILE GLU VAL ARG
SEQRES 11 E 190 TRP PHE ARG ASN SER GLN GLU GLU LYS ALA GLY VAL VAL
SEQRES 12 E 190 SER THR GLY LEU ILE GLN ASN GLY ASP TRP THR PHE GLN
SEQRES 13 E 190 THR LEU VAL MET LEU GLU THR VAL PRO ARG SER GLY GLU
SEQRES 14 E 190 VAL TYR THR CYS GLN VAL GLU HIS PRO SER VAL THR SER
SEQRES 15 E 190 PRO LEU THR VAL GLU TRP ARG ALA
SEQRES 1 F 20 ASN PRO VAL VAL HIS PHE PHE LYS ASN ILE VAL THR PRO
SEQRES 2 F 20 ARG THR PRO PRO PRO SER GLN
HET SO4 D 182 5
HET SO4 A 182 5
HET SO4 B 191 5
HET GOL D 183 6
HET GOL B 192 6
HETNAM SO4 SULFATE ION
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 7 SO4 3(O4 S 2-)
FORMUL 10 GOL 2(C3 H8 O3)
FORMUL 12 HOH *494(H2 O)
HELIX 1 1 LEU A 45 PHE A 51 5 7
HELIX 2 2 GLU A 55 SER A 77 1 23
HELIX 3 3 THR B 51 LEU B 53 5 3
HELIX 4 4 GLY B 54 SER B 63 1 10
HELIX 5 5 GLN B 64 ALA B 73 1 10
HELIX 6 6 ALA B 73 TYR B 78 1 6
HELIX 7 7 TYR B 78 GLU B 87 1 10
HELIX 8 8 SER B 88 THR B 90 5 3
HELIX 9 9 LEU D 45 PHE D 51 5 7
HELIX 10 10 GLU D 55 SER D 77 1 23
HELIX 11 11 THR E 51 LEU E 53 5 3
HELIX 12 12 GLY E 54 SER E 63 1 10
HELIX 13 13 GLN E 64 ALA E 73 1 10
HELIX 14 14 ALA E 73 TYR E 78 1 6
HELIX 15 15 TYR E 78 GLU E 87 1 10
HELIX 16 16 SER E 88 THR E 90 5 3
SHEET 1 A 8 GLU A 40 TRP A 43 0
SHEET 2 A 8 ASP A 29 ASP A 35 -1 O HIS A 33 N VAL A 42
SHEET 3 A 8 SER A 19 PHE A 26 -1 O PHE A 22 N VAL A 34
SHEET 4 A 8 HIS A 5 ASN A 15 -1 O ILE A 8 N ASP A 25
SHEET 5 A 8 PHE B 7 PHE B 18 -1 N PHE B 7 O ASN A 15
SHEET 6 A 8 ARG B 23 TYR B 32 -1 O ARG B 23 N PHE B 18
SHEET 7 A 8 GLU B 35 ASP B 41 -1 O GLU B 35 N TYR B 32
SHEET 8 A 8 TYR B 47 ALA B 49 -1 N ARG B 48 O ARG B 39
SHEET 1 B 4 GLU A 88 THR A 93 0
SHEET 2 B 4 ASN A 103 PHE A 112 -1 N ILE A 106 O LEU A 92
SHEET 3 B 4 PHE A 145 PHE A 153 -1 N PHE A 145 O PHE A 112
SHEET 4 B 4 SER A 133 GLU A 134 -1 O SER A 133 N TYR A 150
SHEET 1 C 4 GLU A 88 THR A 93 0
SHEET 2 C 4 ASN A 103 PHE A 112 -1 N ILE A 106 O LEU A 92
SHEET 3 C 4 PHE A 145 PHE A 153 -1 N PHE A 145 O PHE A 112
SHEET 4 C 4 LEU A 138 PRO A 139 -1 N LEU A 138 O ARG A 146
SHEET 1 D 4 LYS A 126 PRO A 127 0
SHEET 2 D 4 ASN A 118 ARG A 123 -1 N ARG A 123 O LYS A 126
SHEET 3 D 4 VAL A 160 GLU A 166 -1 O ASP A 162 N LEU A 122
SHEET 4 D 4 LEU A 174 GLU A 179 -1 N LEU A 174 O VAL A 165
SHEET 1 E 4 LYS B 98 PRO B 103 0
SHEET 2 E 4 ASN B 113 PHE B 122 -1 N VAL B 116 O TYR B 102
SHEET 3 E 4 PHE B 155 THR B 163 -1 N PHE B 155 O PHE B 122
SHEET 4 E 4 VAL B 142 SER B 144 -1 O VAL B 143 N MET B 160
SHEET 1 F 4 LYS B 98 PRO B 103 0
SHEET 2 F 4 ASN B 113 PHE B 122 -1 N VAL B 116 O TYR B 102
SHEET 3 F 4 PHE B 155 THR B 163 -1 N PHE B 155 O PHE B 122
SHEET 4 F 4 ILE B 148 GLN B 149 -1 N ILE B 148 O GLN B 156
SHEET 1 G 3 GLU B 128 ARG B 133 0
SHEET 2 G 3 VAL B 170 GLU B 176 -1 N THR B 172 O PHE B 132
SHEET 3 G 3 LEU B 184 ARG B 189 -1 O LEU B 184 N VAL B 175
SHEET 1 H 8 GLU D 40 TRP D 43 0
SHEET 2 H 8 ASP D 29 ASP D 35 -1 O HIS D 33 N VAL D 42
SHEET 3 H 8 SER D 19 PHE D 26 -1 O PHE D 22 N VAL D 34
SHEET 4 H 8 HIS D 5 ASN D 15 -1 O ILE D 8 N ASP D 25
SHEET 5 H 8 PHE E 7 PHE E 18 -1 N PHE E 7 O ASN D 15
SHEET 6 H 8 ARG E 23 TYR E 32 -1 O ARG E 23 N PHE E 18
SHEET 7 H 8 GLU E 35 ASP E 41 -1 O GLU E 35 N TYR E 32
SHEET 8 H 8 TYR E 47 ALA E 49 -1 N ARG E 48 O ARG E 39
SHEET 1 I 4 GLU D 88 THR D 93 0
SHEET 2 I 4 ASN D 103 PHE D 112 -1 N ILE D 106 O LEU D 92
SHEET 3 I 4 PHE D 145 PHE D 153 -1 N PHE D 145 O PHE D 112
SHEET 4 I 4 SER D 133 GLU D 134 -1 O SER D 133 N TYR D 150
SHEET 1 J 4 GLU D 88 THR D 93 0
SHEET 2 J 4 ASN D 103 PHE D 112 -1 N ILE D 106 O LEU D 92
SHEET 3 J 4 PHE D 145 PHE D 153 -1 N PHE D 145 O PHE D 112
SHEET 4 J 4 LEU D 138 PRO D 139 -1 N LEU D 138 O ARG D 146
SHEET 1 K 4 LYS D 126 PRO D 127 0
SHEET 2 K 4 ASN D 118 ARG D 123 -1 N ARG D 123 O LYS D 126
SHEET 3 K 4 VAL D 160 GLU D 166 -1 O ASP D 162 N LEU D 122
SHEET 4 K 4 LEU D 174 GLU D 179 -1 N LEU D 174 O VAL D 165
SHEET 1 L 4 LYS E 98 PRO E 103 0
SHEET 2 L 4 ASN E 113 PHE E 122 -1 N VAL E 116 O TYR E 102
SHEET 3 L 4 PHE E 155 THR E 163 -1 N PHE E 155 O PHE E 122
SHEET 4 L 4 VAL E 142 SER E 144 -1 O VAL E 143 N MET E 160
SHEET 1 M 4 LYS E 98 PRO E 103 0
SHEET 2 M 4 ASN E 113 PHE E 122 -1 N VAL E 116 O TYR E 102
SHEET 3 M 4 PHE E 155 THR E 163 -1 N PHE E 155 O PHE E 122
SHEET 4 M 4 ILE E 148 GLN E 149 -1 O ILE E 148 N GLN E 156
SHEET 1 N 3 GLU E 128 ARG E 133 0
SHEET 2 N 3 TYR E 171 GLU E 176 -1 N THR E 172 O PHE E 132
SHEET 3 N 3 LEU E 184 TRP E 188 -1 O LEU E 184 N VAL E 175
SSBOND 1 CYS A 107 CYS A 163 1555 1555 2.03
SSBOND 2 CYS B 15 CYS B 79 1555 1555 2.04
SSBOND 3 CYS B 117 CYS B 173 1555 1555 2.03
SSBOND 4 CYS D 107 CYS D 163 1555 1555 2.03
SSBOND 5 CYS E 15 CYS E 79 1555 1555 2.04
SSBOND 6 CYS E 117 CYS E 173 1555 1555 2.03
CISPEP 1 ASN A 15 PRO A 16 0 -0.01
CISPEP 2 THR A 113 PRO A 114 0 -0.03
CISPEP 3 TYR B 123 PRO B 124 0 1.81
CISPEP 4 ASN D 15 PRO D 16 0 -0.05
CISPEP 5 THR D 113 PRO D 114 0 1.07
CISPEP 6 TYR E 123 PRO E 124 0 0.12
SITE 1 AC1 3 ARG D 123 ASN D 124 LYS D 126
SITE 1 AC2 3 ARG A 123 ASN A 124 LYS A 126
SITE 1 AC3 8 ARG B 29 ARG B 39 HOH B 267 HOH B 268
SITE 2 AC3 8 HOH B 278 ARG E 29 ARG E 39 HOH E 270
SITE 1 AC4 4 ARG B 48 ASP D 110 LYS D 111 ARG D 140
SITE 1 AC5 5 ARG B 94 SER B 179 LYS D 67 GLU D 71
SITE 2 AC5 5 HOH D 241
CRYST1 63.189 114.892 63.175 90.00 90.90 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 0.015826 0.000000 0.000249 0.00000
SCALE2 0.000000 0.008704 0.000000 0.00000
SCALE3 0.000000 0.000000 0.015831 0.00000
(ATOM LINES ARE NOT SHOWN.)
END