HEADER CELL ADHESION 18-OCT-18 6MSV
TITLE STRUCTURE OF THE 6TH TYPE III DOMAIN FROM HUMAN FIBRONECTIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: FIBRONECTIN;
COMPND 3 CHAIN: A, B, C, D, E, F, G, H, I, J, K, L;
COMPND 4 SYNONYM: FN,COLD-INSOLUBLE GLOBULIN,CIG;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: FN1, FN;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS CELL ADHESION
EXPDTA X-RAY DIFFRACTION
AUTHOR S.LOA,T.C.MOU,S.R.SPRANG,K.BRIKNAROVA
REVDAT 3 11-OCT-23 6MSV 1 REMARK
REVDAT 2 01-JAN-20 6MSV 1 REMARK
REVDAT 1 23-OCT-19 6MSV 0
JRNL AUTH S.LOA,T.C.MOU,S.R.SPRANG,K.BRIKNAROVA
JRNL TITL STRUCTURE OF THE 6TH TYPE III DOMAIN FROM HUMAN FIBRONECTIN
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.14_3260: ???)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 26.64
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.100
REMARK 3 COMPLETENESS FOR RANGE (%) : 91.8
REMARK 3 NUMBER OF REFLECTIONS : 39570
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.238
REMARK 3 R VALUE (WORKING SET) : 0.235
REMARK 3 FREE R VALUE : 0.295
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.250
REMARK 3 FREE R VALUE TEST SET COUNT : 1680
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 26.6411 - 5.4800 0.97 3341 149 0.2053 0.2436
REMARK 3 2 5.4800 - 4.3558 0.97 3323 146 0.1819 0.2614
REMARK 3 3 4.3558 - 3.8070 0.97 3344 149 0.2187 0.2610
REMARK 3 4 3.8070 - 3.4597 0.97 3285 145 0.2176 0.2781
REMARK 3 5 3.4597 - 3.2122 0.96 3298 146 0.2406 0.3158
REMARK 3 6 3.2122 - 3.0231 0.94 3245 142 0.2461 0.3007
REMARK 3 7 3.0231 - 2.8719 0.93 3188 144 0.2714 0.4010
REMARK 3 8 2.8719 - 2.7470 0.90 3122 139 0.2999 0.3423
REMARK 3 9 2.7470 - 2.6413 0.86 2959 132 0.3258 0.4040
REMARK 3 10 2.6413 - 2.5503 0.86 2928 137 0.3178 0.3837
REMARK 3 11 2.5503 - 2.4706 0.85 2955 128 0.3408 0.3912
REMARK 3 12 2.4706 - 2.4000 0.84 2902 123 0.3635 0.4006
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.440
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 35.620
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 41.30
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 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.004 7846
REMARK 3 ANGLE : 0.702 10779
REMARK 3 CHIRALITY : 0.053 1303
REMARK 3 PLANARITY : 0.006 1401
REMARK 3 DIHEDRAL : 9.499 4749
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 6MSV COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 19-OCT-18.
REMARK 100 THE DEPOSITION ID IS D_1000237512.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 07-MAY-17
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRL
REMARK 200 BEAMLINE : BL14-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.033
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 325 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 46905
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.300
REMARK 200 RESOLUTION RANGE LOW (A) : 26.640
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 90.2
REMARK 200 DATA REDUNDANCY : 3.600
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.08000
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 13.1000
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) : 2.38
REMARK 200 COMPLETENESS FOR SHELL (%) : 78.1
REMARK 200 DATA REDUNDANCY IN SHELL : 3.20
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.66000
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.600
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: 5DFT
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.44
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.48
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 2.0 M AMMONIUM SULFATE, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,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
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15
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: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
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: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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: 4
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D
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: 5
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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: 6
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 350
REMARK 350 BIOMOLECULE: 7
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: G
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: 8
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: H
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: 9
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: I
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: 10
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: J
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: 11
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: K
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: 12
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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: 13
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 5410 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 14810 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -25.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, G, H, J
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: 14
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 5230 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 15170 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -22.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, D, F, 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: 15
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 5270 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 14450 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -24.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, E, I, K
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 1082
REMARK 465 SER A 1083
REMARK 465 GLY A 1084
REMARK 465 LEU A 1085
REMARK 465 GLN A 1086
REMARK 465 PRO A 1087
REMARK 465 GLY B 1082
REMARK 465 SER B 1083
REMARK 465 GLY B 1084
REMARK 465 LEU B 1085
REMARK 465 GLN B 1086
REMARK 465 PRO B 1087
REMARK 465 GLY B 1088
REMARK 465 SER B 1089
REMARK 465 SER B 1090
REMARK 465 GLY C 1082
REMARK 465 SER C 1083
REMARK 465 GLY C 1084
REMARK 465 LEU C 1085
REMARK 465 GLN C 1086
REMARK 465 PRO C 1087
REMARK 465 GLY C 1088
REMARK 465 GLY D 1082
REMARK 465 SER D 1083
REMARK 465 GLY E 1082
REMARK 465 SER E 1083
REMARK 465 GLY E 1084
REMARK 465 LEU E 1085
REMARK 465 GLN E 1086
REMARK 465 PRO E 1087
REMARK 465 GLY E 1088
REMARK 465 SER E 1089
REMARK 465 GLY F 1082
REMARK 465 SER F 1083
REMARK 465 GLY F 1084
REMARK 465 LEU F 1085
REMARK 465 GLN F 1086
REMARK 465 PRO F 1087
REMARK 465 GLY F 1088
REMARK 465 SER F 1089
REMARK 465 GLY G 1082
REMARK 465 SER G 1083
REMARK 465 GLY G 1084
REMARK 465 LEU G 1085
REMARK 465 GLN G 1086
REMARK 465 PRO G 1087
REMARK 465 GLY G 1088
REMARK 465 SER G 1089
REMARK 465 SER G 1090
REMARK 465 GLY H 1082
REMARK 465 SER H 1083
REMARK 465 GLY H 1084
REMARK 465 GLY I 1082
REMARK 465 SER I 1083
REMARK 465 GLY I 1084
REMARK 465 LEU I 1085
REMARK 465 GLN I 1086
REMARK 465 PRO I 1087
REMARK 465 GLY I 1088
REMARK 465 SER I 1089
REMARK 465 GLN I 1123
REMARK 465 GLY I 1124
REMARK 465 GLY I 1125
REMARK 465 GLY J 1082
REMARK 465 SER J 1083
REMARK 465 GLY J 1084
REMARK 465 LEU J 1085
REMARK 465 GLN J 1086
REMARK 465 PRO J 1087
REMARK 465 GLY J 1088
REMARK 465 SER J 1089
REMARK 465 SER J 1090
REMARK 465 GLY K 1082
REMARK 465 SER K 1083
REMARK 465 GLY K 1084
REMARK 465 LEU K 1085
REMARK 465 GLN K 1086
REMARK 465 PRO K 1087
REMARK 465 GLY K 1088
REMARK 465 SER K 1089
REMARK 465 GLY L 1082
REMARK 465 SER L 1083
REMARK 465 GLY L 1084
REMARK 465 LEU L 1085
REMARK 465 GLN L 1086
REMARK 465 PRO L 1087
REMARK 465 GLY L 1088
REMARK 465 SER L 1089
REMARK 465 SER L 1090
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 THR A1099 -168.56 -117.86
REMARK 500 THR C1101 -32.98 -132.57
REMARK 500 THR D1099 -158.32 -118.72
REMARK 500 THR D1101 -12.15 -141.27
REMARK 500 ARG D1112 8.52 81.43
REMARK 500 GLU D1161 98.91 -69.66
REMARK 500 THR E1099 -168.98 -127.38
REMARK 500 ARG E1112 -10.12 74.24
REMARK 500 THR G1099 -165.54 -122.64
REMARK 500 THR G1101 -4.49 -143.22
REMARK 500 SER H1090 125.73 -30.31
REMARK 500 THR H1099 -157.85 -117.05
REMARK 500 ILE I1091 113.62 -161.58
REMARK 500 ARG I1112 -5.70 76.35
REMARK 500 THR J1099 -168.26 -121.19
REMARK 500 ARG J1157 112.71 -163.78
REMARK 500 THR K1099 -162.91 -122.96
REMARK 500 GLN K1123 -71.21 -90.32
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 GOL B 1201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL F 1201
DBREF 6MSV A 1085 1173 UNP P02751 FINC_HUMAN 1085 1173
DBREF 6MSV B 1085 1173 UNP P02751 FINC_HUMAN 1085 1173
DBREF 6MSV C 1085 1173 UNP P02751 FINC_HUMAN 1085 1173
DBREF 6MSV D 1085 1173 UNP P02751 FINC_HUMAN 1085 1173
DBREF 6MSV E 1085 1173 UNP P02751 FINC_HUMAN 1085 1173
DBREF 6MSV F 1085 1173 UNP P02751 FINC_HUMAN 1085 1173
DBREF 6MSV G 1085 1173 UNP P02751 FINC_HUMAN 1085 1173
DBREF 6MSV H 1085 1173 UNP P02751 FINC_HUMAN 1085 1173
DBREF 6MSV I 1085 1173 UNP P02751 FINC_HUMAN 1085 1173
DBREF 6MSV J 1085 1173 UNP P02751 FINC_HUMAN 1085 1173
DBREF 6MSV K 1085 1173 UNP P02751 FINC_HUMAN 1085 1173
DBREF 6MSV L 1085 1173 UNP P02751 FINC_HUMAN 1085 1173
SEQADV 6MSV GLY A 1082 UNP P02751 EXPRESSION TAG
SEQADV 6MSV SER A 1083 UNP P02751 EXPRESSION TAG
SEQADV 6MSV GLY A 1084 UNP P02751 EXPRESSION TAG
SEQADV 6MSV GLY B 1082 UNP P02751 EXPRESSION TAG
SEQADV 6MSV SER B 1083 UNP P02751 EXPRESSION TAG
SEQADV 6MSV GLY B 1084 UNP P02751 EXPRESSION TAG
SEQADV 6MSV GLY C 1082 UNP P02751 EXPRESSION TAG
SEQADV 6MSV SER C 1083 UNP P02751 EXPRESSION TAG
SEQADV 6MSV GLY C 1084 UNP P02751 EXPRESSION TAG
SEQADV 6MSV GLY D 1082 UNP P02751 EXPRESSION TAG
SEQADV 6MSV SER D 1083 UNP P02751 EXPRESSION TAG
SEQADV 6MSV GLY D 1084 UNP P02751 EXPRESSION TAG
SEQADV 6MSV GLY E 1082 UNP P02751 EXPRESSION TAG
SEQADV 6MSV SER E 1083 UNP P02751 EXPRESSION TAG
SEQADV 6MSV GLY E 1084 UNP P02751 EXPRESSION TAG
SEQADV 6MSV GLY F 1082 UNP P02751 EXPRESSION TAG
SEQADV 6MSV SER F 1083 UNP P02751 EXPRESSION TAG
SEQADV 6MSV GLY F 1084 UNP P02751 EXPRESSION TAG
SEQADV 6MSV GLY G 1082 UNP P02751 EXPRESSION TAG
SEQADV 6MSV SER G 1083 UNP P02751 EXPRESSION TAG
SEQADV 6MSV GLY G 1084 UNP P02751 EXPRESSION TAG
SEQADV 6MSV GLY H 1082 UNP P02751 EXPRESSION TAG
SEQADV 6MSV SER H 1083 UNP P02751 EXPRESSION TAG
SEQADV 6MSV GLY H 1084 UNP P02751 EXPRESSION TAG
SEQADV 6MSV GLY I 1082 UNP P02751 EXPRESSION TAG
SEQADV 6MSV SER I 1083 UNP P02751 EXPRESSION TAG
SEQADV 6MSV GLY I 1084 UNP P02751 EXPRESSION TAG
SEQADV 6MSV GLY J 1082 UNP P02751 EXPRESSION TAG
SEQADV 6MSV SER J 1083 UNP P02751 EXPRESSION TAG
SEQADV 6MSV GLY J 1084 UNP P02751 EXPRESSION TAG
SEQADV 6MSV GLY K 1082 UNP P02751 EXPRESSION TAG
SEQADV 6MSV SER K 1083 UNP P02751 EXPRESSION TAG
SEQADV 6MSV GLY K 1084 UNP P02751 EXPRESSION TAG
SEQADV 6MSV GLY L 1082 UNP P02751 EXPRESSION TAG
SEQADV 6MSV SER L 1083 UNP P02751 EXPRESSION TAG
SEQADV 6MSV GLY L 1084 UNP P02751 EXPRESSION TAG
SEQRES 1 A 92 GLY SER GLY LEU GLN PRO GLY SER SER ILE PRO PRO TYR
SEQRES 2 A 92 ASN THR GLU VAL THR GLU THR THR ILE VAL ILE THR TRP
SEQRES 3 A 92 THR PRO ALA PRO ARG ILE GLY PHE LYS LEU GLY VAL ARG
SEQRES 4 A 92 PRO SER GLN GLY GLY GLU ALA PRO ARG GLU VAL THR SER
SEQRES 5 A 92 ASP SER GLY SER ILE VAL VAL SER GLY LEU THR PRO GLY
SEQRES 6 A 92 VAL GLU TYR VAL TYR THR ILE GLN VAL LEU ARG ASP GLY
SEQRES 7 A 92 GLN GLU ARG ASP ALA PRO ILE VAL ASN LYS VAL VAL THR
SEQRES 8 A 92 PRO
SEQRES 1 B 92 GLY SER GLY LEU GLN PRO GLY SER SER ILE PRO PRO TYR
SEQRES 2 B 92 ASN THR GLU VAL THR GLU THR THR ILE VAL ILE THR TRP
SEQRES 3 B 92 THR PRO ALA PRO ARG ILE GLY PHE LYS LEU GLY VAL ARG
SEQRES 4 B 92 PRO SER GLN GLY GLY GLU ALA PRO ARG GLU VAL THR SER
SEQRES 5 B 92 ASP SER GLY SER ILE VAL VAL SER GLY LEU THR PRO GLY
SEQRES 6 B 92 VAL GLU TYR VAL TYR THR ILE GLN VAL LEU ARG ASP GLY
SEQRES 7 B 92 GLN GLU ARG ASP ALA PRO ILE VAL ASN LYS VAL VAL THR
SEQRES 8 B 92 PRO
SEQRES 1 C 92 GLY SER GLY LEU GLN PRO GLY SER SER ILE PRO PRO TYR
SEQRES 2 C 92 ASN THR GLU VAL THR GLU THR THR ILE VAL ILE THR TRP
SEQRES 3 C 92 THR PRO ALA PRO ARG ILE GLY PHE LYS LEU GLY VAL ARG
SEQRES 4 C 92 PRO SER GLN GLY GLY GLU ALA PRO ARG GLU VAL THR SER
SEQRES 5 C 92 ASP SER GLY SER ILE VAL VAL SER GLY LEU THR PRO GLY
SEQRES 6 C 92 VAL GLU TYR VAL TYR THR ILE GLN VAL LEU ARG ASP GLY
SEQRES 7 C 92 GLN GLU ARG ASP ALA PRO ILE VAL ASN LYS VAL VAL THR
SEQRES 8 C 92 PRO
SEQRES 1 D 92 GLY SER GLY LEU GLN PRO GLY SER SER ILE PRO PRO TYR
SEQRES 2 D 92 ASN THR GLU VAL THR GLU THR THR ILE VAL ILE THR TRP
SEQRES 3 D 92 THR PRO ALA PRO ARG ILE GLY PHE LYS LEU GLY VAL ARG
SEQRES 4 D 92 PRO SER GLN GLY GLY GLU ALA PRO ARG GLU VAL THR SER
SEQRES 5 D 92 ASP SER GLY SER ILE VAL VAL SER GLY LEU THR PRO GLY
SEQRES 6 D 92 VAL GLU TYR VAL TYR THR ILE GLN VAL LEU ARG ASP GLY
SEQRES 7 D 92 GLN GLU ARG ASP ALA PRO ILE VAL ASN LYS VAL VAL THR
SEQRES 8 D 92 PRO
SEQRES 1 E 92 GLY SER GLY LEU GLN PRO GLY SER SER ILE PRO PRO TYR
SEQRES 2 E 92 ASN THR GLU VAL THR GLU THR THR ILE VAL ILE THR TRP
SEQRES 3 E 92 THR PRO ALA PRO ARG ILE GLY PHE LYS LEU GLY VAL ARG
SEQRES 4 E 92 PRO SER GLN GLY GLY GLU ALA PRO ARG GLU VAL THR SER
SEQRES 5 E 92 ASP SER GLY SER ILE VAL VAL SER GLY LEU THR PRO GLY
SEQRES 6 E 92 VAL GLU TYR VAL TYR THR ILE GLN VAL LEU ARG ASP GLY
SEQRES 7 E 92 GLN GLU ARG ASP ALA PRO ILE VAL ASN LYS VAL VAL THR
SEQRES 8 E 92 PRO
SEQRES 1 F 92 GLY SER GLY LEU GLN PRO GLY SER SER ILE PRO PRO TYR
SEQRES 2 F 92 ASN THR GLU VAL THR GLU THR THR ILE VAL ILE THR TRP
SEQRES 3 F 92 THR PRO ALA PRO ARG ILE GLY PHE LYS LEU GLY VAL ARG
SEQRES 4 F 92 PRO SER GLN GLY GLY GLU ALA PRO ARG GLU VAL THR SER
SEQRES 5 F 92 ASP SER GLY SER ILE VAL VAL SER GLY LEU THR PRO GLY
SEQRES 6 F 92 VAL GLU TYR VAL TYR THR ILE GLN VAL LEU ARG ASP GLY
SEQRES 7 F 92 GLN GLU ARG ASP ALA PRO ILE VAL ASN LYS VAL VAL THR
SEQRES 8 F 92 PRO
SEQRES 1 G 92 GLY SER GLY LEU GLN PRO GLY SER SER ILE PRO PRO TYR
SEQRES 2 G 92 ASN THR GLU VAL THR GLU THR THR ILE VAL ILE THR TRP
SEQRES 3 G 92 THR PRO ALA PRO ARG ILE GLY PHE LYS LEU GLY VAL ARG
SEQRES 4 G 92 PRO SER GLN GLY GLY GLU ALA PRO ARG GLU VAL THR SER
SEQRES 5 G 92 ASP SER GLY SER ILE VAL VAL SER GLY LEU THR PRO GLY
SEQRES 6 G 92 VAL GLU TYR VAL TYR THR ILE GLN VAL LEU ARG ASP GLY
SEQRES 7 G 92 GLN GLU ARG ASP ALA PRO ILE VAL ASN LYS VAL VAL THR
SEQRES 8 G 92 PRO
SEQRES 1 H 92 GLY SER GLY LEU GLN PRO GLY SER SER ILE PRO PRO TYR
SEQRES 2 H 92 ASN THR GLU VAL THR GLU THR THR ILE VAL ILE THR TRP
SEQRES 3 H 92 THR PRO ALA PRO ARG ILE GLY PHE LYS LEU GLY VAL ARG
SEQRES 4 H 92 PRO SER GLN GLY GLY GLU ALA PRO ARG GLU VAL THR SER
SEQRES 5 H 92 ASP SER GLY SER ILE VAL VAL SER GLY LEU THR PRO GLY
SEQRES 6 H 92 VAL GLU TYR VAL TYR THR ILE GLN VAL LEU ARG ASP GLY
SEQRES 7 H 92 GLN GLU ARG ASP ALA PRO ILE VAL ASN LYS VAL VAL THR
SEQRES 8 H 92 PRO
SEQRES 1 I 92 GLY SER GLY LEU GLN PRO GLY SER SER ILE PRO PRO TYR
SEQRES 2 I 92 ASN THR GLU VAL THR GLU THR THR ILE VAL ILE THR TRP
SEQRES 3 I 92 THR PRO ALA PRO ARG ILE GLY PHE LYS LEU GLY VAL ARG
SEQRES 4 I 92 PRO SER GLN GLY GLY GLU ALA PRO ARG GLU VAL THR SER
SEQRES 5 I 92 ASP SER GLY SER ILE VAL VAL SER GLY LEU THR PRO GLY
SEQRES 6 I 92 VAL GLU TYR VAL TYR THR ILE GLN VAL LEU ARG ASP GLY
SEQRES 7 I 92 GLN GLU ARG ASP ALA PRO ILE VAL ASN LYS VAL VAL THR
SEQRES 8 I 92 PRO
SEQRES 1 J 92 GLY SER GLY LEU GLN PRO GLY SER SER ILE PRO PRO TYR
SEQRES 2 J 92 ASN THR GLU VAL THR GLU THR THR ILE VAL ILE THR TRP
SEQRES 3 J 92 THR PRO ALA PRO ARG ILE GLY PHE LYS LEU GLY VAL ARG
SEQRES 4 J 92 PRO SER GLN GLY GLY GLU ALA PRO ARG GLU VAL THR SER
SEQRES 5 J 92 ASP SER GLY SER ILE VAL VAL SER GLY LEU THR PRO GLY
SEQRES 6 J 92 VAL GLU TYR VAL TYR THR ILE GLN VAL LEU ARG ASP GLY
SEQRES 7 J 92 GLN GLU ARG ASP ALA PRO ILE VAL ASN LYS VAL VAL THR
SEQRES 8 J 92 PRO
SEQRES 1 K 92 GLY SER GLY LEU GLN PRO GLY SER SER ILE PRO PRO TYR
SEQRES 2 K 92 ASN THR GLU VAL THR GLU THR THR ILE VAL ILE THR TRP
SEQRES 3 K 92 THR PRO ALA PRO ARG ILE GLY PHE LYS LEU GLY VAL ARG
SEQRES 4 K 92 PRO SER GLN GLY GLY GLU ALA PRO ARG GLU VAL THR SER
SEQRES 5 K 92 ASP SER GLY SER ILE VAL VAL SER GLY LEU THR PRO GLY
SEQRES 6 K 92 VAL GLU TYR VAL TYR THR ILE GLN VAL LEU ARG ASP GLY
SEQRES 7 K 92 GLN GLU ARG ASP ALA PRO ILE VAL ASN LYS VAL VAL THR
SEQRES 8 K 92 PRO
SEQRES 1 L 92 GLY SER GLY LEU GLN PRO GLY SER SER ILE PRO PRO TYR
SEQRES 2 L 92 ASN THR GLU VAL THR GLU THR THR ILE VAL ILE THR TRP
SEQRES 3 L 92 THR PRO ALA PRO ARG ILE GLY PHE LYS LEU GLY VAL ARG
SEQRES 4 L 92 PRO SER GLN GLY GLY GLU ALA PRO ARG GLU VAL THR SER
SEQRES 5 L 92 ASP SER GLY SER ILE VAL VAL SER GLY LEU THR PRO GLY
SEQRES 6 L 92 VAL GLU TYR VAL TYR THR ILE GLN VAL LEU ARG ASP GLY
SEQRES 7 L 92 GLN GLU ARG ASP ALA PRO ILE VAL ASN LYS VAL VAL THR
SEQRES 8 L 92 PRO
HET GOL B1201 6
HET GOL F1201 6
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 13 GOL 2(C3 H8 O3)
FORMUL 15 HOH *148(H2 O)
SHEET 1 AA1 6 SER A1137 VAL A1140 0
SHEET 2 AA1 6 ILE A1103 TRP A1107 -1 N ILE A1105 O ILE A1138
SHEET 3 AA1 6 TYR A1094 VAL A1098 -1 N GLU A1097 O VAL A1104
SHEET 4 AA1 6 ASN J1095 VAL J1098 -1 O THR J1096 N VAL A1098
SHEET 5 AA1 6 ILE J1103 THR J1106 -1 O VAL J1104 N GLU J1097
SHEET 6 AA1 6 SER J1137 VAL J1140 -1 O ILE J1138 N ILE J1105
SHEET 1 AA2 8 ILE A1166 VAL A1171 0
SHEET 2 AA2 8 GLU A1148 ARG A1157 -1 N TYR A1149 O VAL A1170
SHEET 3 AA2 8 ILE A1113 PRO A1121 -1 N ARG A1120 O VAL A1150
SHEET 4 AA2 8 ARG A1129 SER A1133 -1 O VAL A1131 N LEU A1117
SHEET 5 AA2 8 ARG E1129 SER E1133 1 O THR E1132 N GLU A1130
SHEET 6 AA2 8 ILE E1113 PRO E1121 -1 N LEU E1117 O VAL E1131
SHEET 7 AA2 8 GLU E1148 ARG E1157 -1 O VAL E1150 N ARG E1120
SHEET 8 AA2 8 ILE E1166 VAL E1171 -1 O VAL E1170 N TYR E1149
SHEET 1 AA3 6 SER B1137 VAL B1140 0
SHEET 2 AA3 6 ILE B1103 TRP B1107 -1 N ILE B1105 O ILE B1138
SHEET 3 AA3 6 TYR B1094 VAL B1098 -1 N ASN B1095 O THR B1106
SHEET 4 AA3 6 ASN L1095 VAL L1098 -1 O VAL L1098 N THR B1096
SHEET 5 AA3 6 ILE L1103 THR L1106 -1 O THR L1106 N ASN L1095
SHEET 6 AA3 6 SER L1137 VAL L1140 -1 O ILE L1138 N ILE L1105
SHEET 1 AA4 8 ILE B1166 VAL B1171 0
SHEET 2 AA4 8 GLU B1148 ARG B1157 -1 N TYR B1149 O VAL B1170
SHEET 3 AA4 8 ILE B1113 PRO B1121 -1 N GLY B1114 O LEU B1156
SHEET 4 AA4 8 ARG B1129 SER B1133 -1 O VAL B1131 N LEU B1117
SHEET 5 AA4 8 ARG C1129 SER C1133 1 O THR C1132 N GLU B1130
SHEET 6 AA4 8 GLY C1114 PRO C1121 -1 N PHE C1115 O SER C1133
SHEET 7 AA4 8 GLU C1148 LEU C1156 -1 O VAL C1150 N ARG C1120
SHEET 8 AA4 8 ILE C1166 VAL C1171 -1 O VAL C1170 N TYR C1149
SHEET 1 AA5 6 SER C1137 VAL C1140 0
SHEET 2 AA5 6 ILE C1103 TRP C1107 -1 N ILE C1105 O ILE C1138
SHEET 3 AA5 6 TYR C1094 VAL C1098 -1 N ASN C1095 O THR C1106
SHEET 4 AA5 6 TYR I1094 VAL I1098 -1 O VAL I1098 N THR C1096
SHEET 5 AA5 6 ILE I1103 TRP I1107 -1 O THR I1106 N ASN I1095
SHEET 6 AA5 6 SER I1137 VAL I1140 -1 O ILE I1138 N ILE I1105
SHEET 1 AA6 6 SER D1137 VAL D1140 0
SHEET 2 AA6 6 ILE D1103 THR D1106 -1 N ILE D1105 O ILE D1138
SHEET 3 AA6 6 ASN D1095 VAL D1098 -1 N ASN D1095 O THR D1106
SHEET 4 AA6 6 TYR F1094 VAL F1098 -1 O THR F1096 N VAL D1098
SHEET 5 AA6 6 ILE F1103 TRP F1107 -1 O THR F1106 N ASN F1095
SHEET 6 AA6 6 SER F1137 VAL F1140 -1 O ILE F1138 N ILE F1105
SHEET 1 AA7 4 ARG D1129 SER D1133 0
SHEET 2 AA7 4 ILE D1113 PRO D1121 -1 N LEU D1117 O VAL D1131
SHEET 3 AA7 4 GLU D1148 ARG D1157 -1 O VAL D1150 N ARG D1120
SHEET 4 AA7 4 GLN D1160 GLU D1161 -1 O GLN D1160 N ARG D1157
SHEET 1 AA8 4 ARG D1129 SER D1133 0
SHEET 2 AA8 4 ILE D1113 PRO D1121 -1 N LEU D1117 O VAL D1131
SHEET 3 AA8 4 GLU D1148 ARG D1157 -1 O VAL D1150 N ARG D1120
SHEET 4 AA8 4 ILE D1166 VAL D1171 -1 O VAL D1170 N TYR D1149
SHEET 1 AA9 6 SER E1137 VAL E1140 0
SHEET 2 AA9 6 ILE E1103 TRP E1107 -1 N ILE E1105 O ILE E1138
SHEET 3 AA9 6 TYR E1094 VAL E1098 -1 N ASN E1095 O THR E1106
SHEET 4 AA9 6 TYR K1094 VAL K1098 -1 O THR K1096 N VAL E1098
SHEET 5 AA9 6 ILE K1103 TRP K1107 -1 O VAL K1104 N GLU K1097
SHEET 6 AA9 6 SER K1137 VAL K1140 -1 O ILE K1138 N ILE K1105
SHEET 1 AB1 4 ARG F1129 SER F1133 0
SHEET 2 AB1 4 ILE F1113 PRO F1121 -1 N PHE F1115 O SER F1133
SHEET 3 AB1 4 GLU F1148 ARG F1157 -1 O VAL F1150 N ARG F1120
SHEET 4 AB1 4 ILE F1166 VAL F1171 -1 O VAL F1170 N TYR F1149
SHEET 1 AB2 6 SER G1137 VAL G1140 0
SHEET 2 AB2 6 ILE G1103 TRP G1107 -1 N ILE G1105 O ILE G1138
SHEET 3 AB2 6 TYR G1094 VAL G1098 -1 N GLU G1097 O VAL G1104
SHEET 4 AB2 6 ASN H1095 VAL H1098 -1 O VAL H1098 N THR G1096
SHEET 5 AB2 6 ILE H1103 THR H1106 -1 O THR H1106 N ASN H1095
SHEET 6 AB2 6 SER H1137 VAL H1140 -1 O ILE H1138 N ILE H1105
SHEET 1 AB3 4 ARG G1129 SER G1133 0
SHEET 2 AB3 4 ILE G1113 PRO G1121 -1 N LEU G1117 O VAL G1131
SHEET 3 AB3 4 GLU G1148 ARG G1157 -1 O VAL G1150 N ARG G1120
SHEET 4 AB3 4 GLN G1160 GLU G1161 -1 O GLN G1160 N ARG G1157
SHEET 1 AB4 4 ARG G1129 SER G1133 0
SHEET 2 AB4 4 ILE G1113 PRO G1121 -1 N LEU G1117 O VAL G1131
SHEET 3 AB4 4 GLU G1148 ARG G1157 -1 O VAL G1150 N ARG G1120
SHEET 4 AB4 4 ILE G1166 VAL G1171 -1 O VAL G1170 N TYR G1149
SHEET 1 AB5 4 ARG H1129 SER H1133 0
SHEET 2 AB5 4 ILE H1113 PRO H1121 -1 N LEU H1117 O VAL H1131
SHEET 3 AB5 4 GLU H1148 ARG H1157 -1 O VAL H1150 N ARG H1120
SHEET 4 AB5 4 ILE H1166 VAL H1171 -1 O VAL H1170 N TYR H1149
SHEET 1 AB6 4 ARG I1129 SER I1133 0
SHEET 2 AB6 4 ILE I1113 PRO I1121 -1 N LEU I1117 O VAL I1131
SHEET 3 AB6 4 GLU I1148 ARG I1157 -1 O LEU I1156 N GLY I1114
SHEET 4 AB6 4 ILE I1166 VAL I1171 -1 O ILE I1166 N ILE I1153
SHEET 1 AB7 4 ARG J1129 SER J1133 0
SHEET 2 AB7 4 PHE J1115 PRO J1121 -1 N LEU J1117 O VAL J1131
SHEET 3 AB7 4 GLU J1148 VAL J1155 -1 O VAL J1150 N ARG J1120
SHEET 4 AB7 4 ILE J1166 VAL J1171 -1 O VAL J1170 N TYR J1149
SHEET 1 AB8 4 ARG K1129 SER K1133 0
SHEET 2 AB8 4 ILE K1113 PRO K1121 -1 N LEU K1117 O VAL K1131
SHEET 3 AB8 4 GLU K1148 ARG K1157 -1 O VAL K1150 N ARG K1120
SHEET 4 AB8 4 ILE K1166 VAL K1171 -1 O VAL K1170 N TYR K1149
SHEET 1 AB9 4 ARG L1129 SER L1133 0
SHEET 2 AB9 4 ILE L1113 PRO L1121 -1 N PHE L1115 O SER L1133
SHEET 3 AB9 4 GLU L1148 ARG L1157 -1 O VAL L1150 N ARG L1120
SHEET 4 AB9 4 ILE L1166 VAL L1171 -1 O VAL L1170 N TYR L1149
SITE 1 AC1 2 LYS B1169 LYS L1169
SITE 1 AC2 4 GLN F1123 GLU F1148 HOH F1303 GLY G1146
CRYST1 48.520 79.460 80.886 112.33 95.88 94.48 P 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 0.020610 0.001616 0.002995 0.00000
SCALE2 0.000000 0.012624 0.005366 0.00000
SCALE3 0.000000 0.000000 0.013505 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
