HEADER CELL ADHESION 04-JAN-08 2VKW
TITLE HUMAN NCAM, FN3 DOMAINS 1 AND 2
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: NEURAL CELL ADHESION MOLECULE 1,140 KDA ISOFORM;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: FN3 DOMAINS, RESIDUES 496-598,601-692;
COMPND 5 SYNONYM: N-CAM 140, NCAM-140, CD56 ANTIGEN, NEURAL CELL ADHESION
COMPND 6 MOLECULE;
COMPND 7 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: HOMO SAPIENS;
SOURCE 6 EXPRESSION_SYSTEM_COMMON: HUMAN;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 9606;
SOURCE 8 EXPRESSION_SYSTEM_CELL_LINE: 293-EBNA;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR: PCEP-PU
KEYWDS ADHESION RECEPTOR, CELL ADHESION
EXPDTA X-RAY DIFFRACTION
AUTHOR F.CARAFOLI,J.L.SAFFELL,E.HOHENESTER
REVDAT 4 08-NOV-17 2VKW 1 SOURCE
REVDAT 3 24-FEB-09 2VKW 1 VERSN
REVDAT 2 18-MAR-08 2VKW 1 JRNL
REVDAT 1 26-FEB-08 2VKW 0
JRNL AUTH F.CARAFOLI,J.L.SAFFELL,E.HOHENESTER
JRNL TITL STRUCTURE OF THE TANDEM FIBRONECTIN TYPE 3 DOMAINS OF NEURAL
JRNL TITL 2 CELL ADHESION MOLECULE
JRNL REF J.MOL.BIOL. V. 377 524 2008
JRNL REFN ISSN 0022-2836
JRNL PMID 18261743
JRNL DOI 10.1016/J.JMB.2008.01.030
REMARK 2
REMARK 2 RESOLUTION. 2.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1
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 : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 10000.000
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 99.2
REMARK 3 NUMBER OF REFLECTIONS : 16920
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 SET) : 0.218
REMARK 3 FREE R VALUE : 0.272
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 9.900
REMARK 3 FREE R VALUE TEST SET COUNT : 1691
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 : 3058
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 25
REMARK 3 SOLVENT ATOMS : 98
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.76900
REMARK 3 B22 (A**2) : -0.08400
REMARK 3 B33 (A**2) : -1.68400
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) : 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) : 1.400
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 1.330 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.250 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 2.100 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 3.320 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : 0.45
REMARK 3 BSOL : 38.39
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 2VKW COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 04-JAN-08.
REMARK 100 THE DEPOSITION ID IS D_1290034906.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-FEB-06
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.2
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SRS
REMARK 200 BEAMLINE : PX14.1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.49
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 16957
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.300
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 200 DATA REDUNDANCY : 4.800
REMARK 200 R MERGE (I) : 0.06000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 19.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.42
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 4.80
REMARK 200 R MERGE FOR SHELL (I) : 0.12000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 11.10
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: AUTOSHARP
REMARK 200 STARTING MODEL: NONE
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 40.28
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.08
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 5.2
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-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 26.38500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 49.10850
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 35.67300
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 49.10850
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 26.38500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 35.67300
REMARK 290 SMTRY3 4 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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 3310 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 23740 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -5.8 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 ALA A 492
REMARK 465 PRO A 493
REMARK 465 LEU A 494
REMARK 465 ALA A 495
REMARK 465 ALA A 694
REMARK 465 HIS A 695
REMARK 465 HIS A 696
REMARK 465 HIS A 697
REMARK 465 HIS A 698
REMARK 465 HIS A 699
REMARK 465 HIS A 700
REMARK 465 ALA B 492
REMARK 465 PRO B 493
REMARK 465 LEU B 494
REMARK 465 ALA B 495
REMARK 465 GLN B 496
REMARK 465 ALA B 693
REMARK 465 ALA B 694
REMARK 465 HIS B 695
REMARK 465 HIS B 696
REMARK 465 HIS B 697
REMARK 465 HIS B 698
REMARK 465 HIS B 699
REMARK 465 HIS B 700
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 ALA A 693 CA C O CB
REMARK 470 ALA B 692 CA C O CB
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 511 -150.99 -121.51
REMARK 500 ARG A 599 -158.65 -152.73
REMARK 500 TYR B 511 -148.41 -119.32
REMARK 500 ASN B 615 49.70 -93.48
REMARK 500 HIS B 633 164.94 177.65
REMARK 500 SER B 643 -165.73 -125.02
REMARK 500 ASN B 677 -168.39 -123.25
REMARK 500 THR B 691 -174.35 -66.90
REMARK 500
REMARK 500 REMARK: NULL
REMARK 700
REMARK 700 SHEET
REMARK 700 THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN
REMARK 700 ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW,
REMARK 700 TWO SHEETS ARE DEFINED.
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B1692
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B1693
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1693
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B1694
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B1695
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2VKX RELATED DB: PDB
REMARK 900 HUMAN NCAM, FN3 DOMAINS 1 AND 2, M610R MUTANT
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 N-TERMINAL APLA AND C-TERMINAL AAAHHHHHH ARE VECTOR-
REMARK 999 DERIVED. QG (POSITIONS 599-600) OF P13591 REPLACED BY R (
REMARK 999 NATURAL MUSCLE- AND BRAIN-SPECIFIC SPLICE VARIANT)
DBREF 2VKW A 492 495 PDB 2VKW 2VKW 492 495
DBREF 2VKW A 496 598 UNP P13591 NCA11_HUMAN 496 598
DBREF 2VKW A 599 599 PDB 2VKW 2VKW 599 599
DBREF 2VKW A 600 691 UNP P13591 NCA11_HUMAN 601 692
DBREF 2VKW A 692 700 PDB 2VKW 2VKW 692 700
DBREF 2VKW B 492 495 PDB 2VKW 2VKW 492 495
DBREF 2VKW B 496 598 UNP P13591 NCA11_HUMAN 496 598
DBREF 2VKW B 599 599 PDB 2VKW 2VKW 599 599
DBREF 2VKW B 600 691 UNP P13591 NCA11_HUMAN 601 692
DBREF 2VKW B 692 700 PDB 2VKW 2VKW 692 700
SEQRES 1 A 209 ALA PRO LEU ALA GLN ALA ASP THR PRO SER SER PRO SER
SEQRES 2 A 209 ILE ASP GLN VAL GLU PRO TYR SER SER THR ALA GLN VAL
SEQRES 3 A 209 GLN PHE ASP GLU PRO GLU ALA THR GLY GLY VAL PRO ILE
SEQRES 4 A 209 LEU LYS TYR LYS ALA GLU TRP ARG ALA VAL GLY GLU GLU
SEQRES 5 A 209 VAL TRP HIS SER LYS TRP TYR ASP ALA LYS GLU ALA SER
SEQRES 6 A 209 MET GLU GLY ILE VAL THR ILE VAL GLY LEU LYS PRO GLU
SEQRES 7 A 209 THR THR TYR ALA VAL ARG LEU ALA ALA LEU ASN GLY LYS
SEQRES 8 A 209 GLY LEU GLY GLU ILE SER ALA ALA SER GLU PHE LYS THR
SEQRES 9 A 209 GLN PRO VAL ARG GLU PRO SER ALA PRO LYS LEU GLU GLY
SEQRES 10 A 209 GLN MET GLY GLU ASP GLY ASN SER ILE LYS VAL ASN LEU
SEQRES 11 A 209 ILE LYS GLN ASP ASP GLY GLY SER PRO ILE ARG HIS TYR
SEQRES 12 A 209 LEU VAL ARG TYR ARG ALA LEU SER SER GLU TRP LYS PRO
SEQRES 13 A 209 GLU ILE ARG LEU PRO SER GLY SER ASP HIS VAL MET LEU
SEQRES 14 A 209 LYS SER LEU ASP TRP ASN ALA GLU TYR GLU VAL TYR VAL
SEQRES 15 A 209 VAL ALA GLU ASN GLN GLN GLY LYS SER LYS ALA ALA HIS
SEQRES 16 A 209 PHE VAL PHE ARG THR ALA ALA ALA HIS HIS HIS HIS HIS
SEQRES 17 A 209 HIS
SEQRES 1 B 209 ALA PRO LEU ALA GLN ALA ASP THR PRO SER SER PRO SER
SEQRES 2 B 209 ILE ASP GLN VAL GLU PRO TYR SER SER THR ALA GLN VAL
SEQRES 3 B 209 GLN PHE ASP GLU PRO GLU ALA THR GLY GLY VAL PRO ILE
SEQRES 4 B 209 LEU LYS TYR LYS ALA GLU TRP ARG ALA VAL GLY GLU GLU
SEQRES 5 B 209 VAL TRP HIS SER LYS TRP TYR ASP ALA LYS GLU ALA SER
SEQRES 6 B 209 MET GLU GLY ILE VAL THR ILE VAL GLY LEU LYS PRO GLU
SEQRES 7 B 209 THR THR TYR ALA VAL ARG LEU ALA ALA LEU ASN GLY LYS
SEQRES 8 B 209 GLY LEU GLY GLU ILE SER ALA ALA SER GLU PHE LYS THR
SEQRES 9 B 209 GLN PRO VAL ARG GLU PRO SER ALA PRO LYS LEU GLU GLY
SEQRES 10 B 209 GLN MET GLY GLU ASP GLY ASN SER ILE LYS VAL ASN LEU
SEQRES 11 B 209 ILE LYS GLN ASP ASP GLY GLY SER PRO ILE ARG HIS TYR
SEQRES 12 B 209 LEU VAL ARG TYR ARG ALA LEU SER SER GLU TRP LYS PRO
SEQRES 13 B 209 GLU ILE ARG LEU PRO SER GLY SER ASP HIS VAL MET LEU
SEQRES 14 B 209 LYS SER LEU ASP TRP ASN ALA GLU TYR GLU VAL TYR VAL
SEQRES 15 B 209 VAL ALA GLU ASN GLN GLN GLY LYS SER LYS ALA ALA HIS
SEQRES 16 B 209 PHE VAL PHE ARG THR ALA ALA ALA HIS HIS HIS HIS HIS
SEQRES 17 B 209 HIS
HET SO4 A1693 5
HET SO4 B1692 5
HET SO4 B1693 5
HET SO4 B1694 5
HET SO4 B1695 5
HETNAM SO4 SULFATE ION
FORMUL 3 SO4 5(O4 S 2-)
FORMUL 8 HOH *98(H2 O)
HELIX 1 1 ALA A 552 GLY A 559 1 8
HELIX 2 2 ALA B 552 GLY B 559 1 8
SHEET 1 AA 3 SER A 504 PRO A 510 0
SHEET 2 AA 3 ALA A 515 ASP A 520 -1 O GLN A 516 N GLU A 509
SHEET 3 AA 3 ILE A 560 ILE A 563 -1 O VAL A 561 N VAL A 517
SHEET 1 AB 4 HIS A 546 ASP A 551 0
SHEET 2 AB 4 LYS A 532 ALA A 539 -1 O TYR A 533 N TYR A 550
SHEET 3 AB 4 THR A 571 ASN A 580 -1 O ALA A 573 N ARG A 538
SHEET 4 AB 4 SER A 591 LYS A 594 -1 O SER A 591 N VAL A 574
SHEET 1 AC 4 HIS A 546 ASP A 551 0
SHEET 2 AC 4 LYS A 532 ALA A 539 -1 O TYR A 533 N TYR A 550
SHEET 3 AC 4 THR A 571 ASN A 580 -1 O ALA A 573 N ARG A 538
SHEET 4 AC 4 GLY A 583 LEU A 584 -1 O GLY A 583 N ASN A 580
SHEET 1 AD 3 LYS A 605 MET A 610 0
SHEET 2 AD 3 ILE A 617 ILE A 622 -1 O LYS A 618 N GLN A 609
SHEET 3 AD 3 HIS A 657 LEU A 660 -1 O VAL A 658 N VAL A 619
SHEET 1 AE 7 ILE A 649 LEU A 651 0
SHEET 2 AE 7 HIS A 633 ALA A 640 -1 O TYR A 634 N LEU A 651
SHEET 3 AE 7 GLU A 668 ASN A 677 -1 O GLU A 670 N ARG A 639
SHEET 4 AE 7 ALA A 685 ARG A 690 -1 O ALA A 685 N VAL A 673
SHEET 5 AE 7 LYS B 605 MET B 610 1 O LEU B 606 N VAL A 688
SHEET 6 AE 7 ILE B 617 ILE B 622 -1 O LYS B 618 N GLN B 609
SHEET 7 AE 7 HIS B 657 LEU B 660 -1 O VAL B 658 N VAL B 619
SHEET 1 AF 4 ILE A 649 LEU A 651 0
SHEET 2 AF 4 HIS A 633 ALA A 640 -1 O TYR A 634 N LEU A 651
SHEET 3 AF 4 GLU A 668 ASN A 677 -1 O GLU A 670 N ARG A 639
SHEET 4 AF 4 GLY A 680 LYS A 681 -1 O GLY A 680 N ASN A 677
SHEET 1 BA 3 SER B 504 PRO B 510 0
SHEET 2 BA 3 ALA B 515 ASP B 520 -1 O GLN B 516 N GLU B 509
SHEET 3 BA 3 VAL B 561 ILE B 563 -1 O VAL B 561 N VAL B 517
SHEET 1 BB 4 HIS B 546 ASP B 551 0
SHEET 2 BB 4 ILE B 530 ALA B 539 -1 O TYR B 533 N TYR B 550
SHEET 3 BB 4 THR B 571 ASN B 580 -1 O ALA B 573 N ARG B 538
SHEET 4 BB 4 SER B 591 LYS B 594 -1 O SER B 591 N VAL B 574
SHEET 1 BC 4 HIS B 546 ASP B 551 0
SHEET 2 BC 4 ILE B 530 ALA B 539 -1 O TYR B 533 N TYR B 550
SHEET 3 BC 4 THR B 571 ASN B 580 -1 O ALA B 573 N ARG B 538
SHEET 4 BC 4 GLY B 583 LEU B 584 -1 O GLY B 583 N ASN B 580
SHEET 1 BD 4 ILE B 649 PRO B 652 0
SHEET 2 BD 4 ILE B 631 ALA B 640 -1 O TYR B 634 N LEU B 651
SHEET 3 BD 4 GLU B 668 ASN B 677 -1 O GLU B 670 N ARG B 639
SHEET 4 BD 4 ALA B 685 ARG B 690 -1 O ALA B 685 N VAL B 673
SITE 1 AC1 7 LYS A 534 TRP A 549 ARG A 639 LYS B 532
SITE 2 AC1 7 ASP B 551 HOH B2044 HOH B2045
SITE 1 AC2 6 LYS A 548 TRP A 549 LYS B 548 TRP B 549
SITE 2 AC2 6 HOH B2046 HOH B2047
SITE 1 AC3 5 LYS A 532 ASP A 551 HOH A2051 TRP B 549
SITE 2 AC3 5 ARG B 639
SITE 1 AC4 1 ARG B 637
SITE 1 AC5 2 HIS B 546 SER B 547
CRYST1 52.770 71.346 98.217 90.00 90.00 90.00 P 21 21 21 8
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 0.018950 0.000000 0.000000 0.00000
SCALE2 0.000000 0.014016 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010182 0.00000
MTRIX1 1 -0.711740 0.701500 0.036370 42.05063 1
MTRIX2 1 0.702440 0.710990 0.032850 -17.72883 1
MTRIX3 1 -0.002820 0.048930 -0.998800 21.91621 1
(ATOM LINES ARE NOT SHOWN.)
END