HEADER TRANSFERASE 11-MAY-99 1QH4
TITLE CRYSTAL STRUCTURE OF CHICKEN BRAIN-TYPE CREATINE KINASE AT 1.41
TITLE 2 ANGSTROM RESOLUTION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CREATINE KINASE;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 FRAGMENT: B CHAIN;
COMPND 5 SYNONYM: BB-CK, BRAIN-TYPE CREATINE KINASE;
COMPND 6 EC: 2.7.3.2;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: GALLUS GALLUS;
SOURCE 3 ORGANISM_COMMON: CHICKEN;
SOURCE 4 ORGANISM_TAXID: 9031;
SOURCE 5 ORGAN: BRAIN;
SOURCE 6 CELLULAR_LOCATION: CYTOPLASM;
SOURCE 7 GENE: EMBL-NR. X03509;
SOURCE 8 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 9 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 10 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)PLYSS;
SOURCE 11 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 12 EXPRESSION_SYSTEM_VECTOR: PET-3B;
SOURCE 13 EXPRESSION_SYSTEM_PLASMID: PRF23
KEYWDS BRAIN-TYPE CREATINE KINASE, CANCER, CELLULAR ENERGY METABOLISM,
KEYWDS 2 GUANIDINO KINASE, NEURODEGENERATIVE DISORDERS, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.EDER,U.SCHLATTNER,A.BECKER,T.WALLIMANN,W.KABSCH,K.FRITZ-WOLF
REVDAT 4 16-AUG-23 1QH4 1 REMARK LINK
REVDAT 3 24-JUL-19 1QH4 1 REMARK
REVDAT 2 24-FEB-09 1QH4 1 VERSN
REVDAT 1 19-NOV-99 1QH4 0
JRNL AUTH M.EDER,U.SCHLATTNER,A.BECKER,T.WALLIMANN,W.KABSCH,
JRNL AUTH 2 K.FRITZ-WOLF
JRNL TITL CRYSTAL STRUCTURE OF BRAIN-TYPE CREATINE KINASE AT 1.41 A
JRNL TITL 2 RESOLUTION.
JRNL REF PROTEIN SCI. V. 8 2258 1999
JRNL REFN ISSN 0961-8368
JRNL PMID 10595529
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH G.ZHOU,T.SOMASUNDARAM,E.BLANC,G.PARTHASARATHY,W.R.ELLINGTON,
REMARK 1 AUTH 2 M.S.CHAPMAN
REMARK 1 TITL TRANSITION STATE STRUCTURE OF ARGININE KINASE: IMPLICATIONS
REMARK 1 TITL 2 FOR CATALYSIS OF BIMOLECULAR REACTIONS
REMARK 1 REF PROC.NATL.ACAD.SCI.USA V. 95 8449 1998
REMARK 1 REFN ISSN 0027-8424
REMARK 1 DOI 10.1073/PNAS.95.15.8449
REMARK 1 REFERENCE 2
REMARK 1 AUTH K.FRITZ-WOLF,T.SCHNYDER,T.WALLIMANN,W.KABSCH
REMARK 1 TITL STRUCTURE OF MITOCHONDRIAL CREATINE KINASE.
REMARK 1 REF NATURE V. 381 341 1996
REMARK 1 REFN ISSN 0028-0836
REMARK 1 DOI 10.1038/381341A0
REMARK 2
REMARK 2 RESOLUTION. 1.41 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : SHELXL-97
REMARK 3 AUTHORS : G.M.SHELDRICK
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.41
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 6.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.1
REMARK 3 CROSS-VALIDATION METHOD : FREE R
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (NO CUTOFF).
REMARK 3 R VALUE (WORKING + TEST SET, NO CUTOFF) : 0.137
REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : 0.134
REMARK 3 FREE R VALUE (NO CUTOFF) : 0.188
REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : 5.300
REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : 14886
REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : 282461
REMARK 3
REMARK 3 FIT/AGREEMENT OF MODEL FOR DATA WITH F>4SIG(F).
REMARK 3 R VALUE (WORKING + TEST SET, F>4SIG(F)) : NULL
REMARK 3 R VALUE (WORKING SET, F>4SIG(F)) : NULL
REMARK 3 FREE R VALUE (F>4SIG(F)) : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%, F>4SIG(F)) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT (F>4SIG(F)) : NULL
REMARK 3 TOTAL NUMBER OF REFLECTIONS (F>4SIG(F)) : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 12020
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 25
REMARK 3 SOLVENT ATOMS : 1467
REMARK 3
REMARK 3 MODEL REFINEMENT.
REMARK 3 OCCUPANCY SUM OF NON-HYDROGEN ATOMS : 13358.
REMARK 3 OCCUPANCY SUM OF HYDROGEN ATOMS : 11644.
REMARK 3 NUMBER OF DISCRETELY DISORDERED RESIDUES : 15
REMARK 3 NUMBER OF LEAST-SQUARES PARAMETERS : 12204
REMARK 3 NUMBER OF RESTRAINTS : 14868
REMARK 3
REMARK 3 RMS DEVIATIONS FROM RESTRAINT TARGET VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 ANGLE DISTANCES (A) : 0.029
REMARK 3 SIMILAR DISTANCES (NO TARGET VALUES) (A) : NULL
REMARK 3 DISTANCES FROM RESTRAINT PLANES (A) : 0.022
REMARK 3 ZERO CHIRAL VOLUMES (A**3) : 0.059
REMARK 3 NON-ZERO CHIRAL VOLUMES (A**3) : 0.067
REMARK 3 ANTI-BUMPING DISTANCE RESTRAINTS (A) : 0.014
REMARK 3 RIGID-BOND ADP COMPONENTS (A**2) : 0.004
REMARK 3 SIMILAR ADP COMPONENTS (A**2) : 0.055
REMARK 3 APPROXIMATELY ISOTROPIC ADPS (A**2) : 0.079
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED: MOEWS & KRETSINGER, J.MOL.BIOL.91(1973)201-2
REMARK 3
REMARK 3 STEREOCHEMISTRY TARGET VALUES : ENGH AND HUBER
REMARK 3 SPECIAL CASE: NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 X-PLOR AND CNS WERE USED FOR INITIAL REFINEMENT. ANISOTROPIC
REMARK 3 REFINEMENT IN
REMARK 3 SHELX REDUCED FREE R (NO CUTOFF) BY 2.6%
REMARK 3
REMARK 3 DISORDERED RESIDUES 321 - 330 (CHAIN A-D) WERE MODELED
REMARK 4
REMARK 4 1QH4 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-MAY-99.
REMARK 100 THE DEPOSITION ID IS D_1000001035.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 22-JUL-98
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : EMBL/DESY, HAMBURG
REMARK 200 BEAMLINE : BW7B
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.84
REMARK 200 MONOCHROMATOR : GE SINGLE CRYSTAL
REMARK 200 OPTICS : BENT CRYSTAL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MAR SCANNER 345 MM PLATE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS V. 99
REMARK 200 DATA SCALING SOFTWARE : XDS V. 99
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 301191
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.410
REMARK 200 RESOLUTION RANGE LOW (A) : 38.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.1
REMARK 200 DATA REDUNDANCY : 4.000
REMARK 200 R MERGE (I) : 0.04200
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 17.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.41
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.50
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.1
REMARK 200 DATA REDUNDANCY IN SHELL : 3.50
REMARK 200 R MERGE FOR SHELL (I) : 0.21500
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 5.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE, CNS, SHELXL-97
REMARK 200 STARTING MODEL: 1CRK, MITOCHONDRIAL CREATINE KINASE
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 48.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.37
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M MES, 0.4M CA(OAC)2, 15% PE 2MM
REMARK 280 DTT, PH 6.5, 8 MG/ML PROTEIN
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 87.99500
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4080 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 31080 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -8.0 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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4120 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 30640 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -7.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, 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: 3
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 10280 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 59730 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -37.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, 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 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 2 -1.000000 0.000000 0.000000 38.70641
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 87.99500
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 94.90317
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ARG A 43 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 TYR A 82 CB - CG - CD1 ANGL. DEV. = -3.6 DEGREES
REMARK 500 ARG A 130 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES
REMARK 500 ARG A 151 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 PHE A 192 O - C - N ANGL. DEV. = -10.9 DEGREES
REMARK 500 ARG A 209 NE - CZ - NH1 ANGL. DEV. = 5.1 DEGREES
REMARK 500 ARG A 209 NE - CZ - NH2 ANGL. DEV. = -3.3 DEGREES
REMARK 500 MET A 240 CA - CB - CG ANGL. DEV. = 12.9 DEGREES
REMARK 500 ARG A 252 NE - CZ - NH2 ANGL. DEV. = -5.3 DEGREES
REMARK 500 ARG A 292 NE - CZ - NH1 ANGL. DEV. = 4.3 DEGREES
REMARK 500 ARG A 316 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 GLY A 331 C - N - CA ANGL. DEV. = 17.7 DEGREES
REMARK 500 ARG B 43 NE - CZ - NH1 ANGL. DEV. = 4.9 DEGREES
REMARK 500 ARG B 43 NE - CZ - NH2 ANGL. DEV. = -5.6 DEGREES
REMARK 500 GLN B 46 CA - CB - CG ANGL. DEV. = 14.4 DEGREES
REMARK 500 ARG B 96 NE - CZ - NH2 ANGL. DEV. = -4.0 DEGREES
REMARK 500 GLU B 105 OE1 - CD - OE2 ANGL. DEV. = -7.7 DEGREES
REMARK 500 ARG B 130 NE - CZ - NH1 ANGL. DEV. = 4.1 DEGREES
REMARK 500 ARG B 132 NE - CZ - NH2 ANGL. DEV. = -4.6 DEGREES
REMARK 500 ARG B 151 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 LYS B 156 CD - CE - NZ ANGL. DEV. = 14.7 DEGREES
REMARK 500 ARG B 209 NE - CZ - NH1 ANGL. DEV. = 4.5 DEGREES
REMARK 500 ARG B 236 NE - CZ - NH2 ANGL. DEV. = -4.4 DEGREES
REMARK 500 ARG B 252 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES
REMARK 500 ARG B 292 NE - CZ - NH1 ANGL. DEV. = 5.0 DEGREES
REMARK 500 ARG B 292 NE - CZ - NH2 ANGL. DEV. = -4.1 DEGREES
REMARK 500 ARG C 43 CD - NE - CZ ANGL. DEV. = 14.0 DEGREES
REMARK 500 ARG C 43 NE - CZ - NH1 ANGL. DEV. = 5.3 DEGREES
REMARK 500 ARG C 45 NE - CZ - NH1 ANGL. DEV. = -3.5 DEGREES
REMARK 500 GLN C 46 CA - CB - CG ANGL. DEV. = 16.5 DEGREES
REMARK 500 ARG C 130 CD - NE - CZ ANGL. DEV. = 41.2 DEGREES
REMARK 500 ARG C 130 NE - CZ - NH1 ANGL. DEV. = 4.2 DEGREES
REMARK 500 ARG C 132 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 ARG C 132 NE - CZ - NH2 ANGL. DEV. = -4.7 DEGREES
REMARK 500 ARG C 138 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES
REMARK 500 ARG C 148 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 ARG C 151 NE - CZ - NH1 ANGL. DEV. = 4.4 DEGREES
REMARK 500 ARG C 209 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES
REMARK 500 ARG C 236 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 ARG C 236 NE - CZ - NH2 ANGL. DEV. = -4.8 DEGREES
REMARK 500 PHE C 264 CB - CG - CD1 ANGL. DEV. = 4.5 DEGREES
REMARK 500 PHE C 271 CB - CG - CD1 ANGL. DEV. = 4.6 DEGREES
REMARK 500 ARG C 292 NE - CZ - NH1 ANGL. DEV. = 5.8 DEGREES
REMARK 500 THR C 322 C - N - CA ANGL. DEV. = 18.7 DEGREES
REMARK 500 ARG C 341 NE - CZ - NH2 ANGL. DEV. = 4.1 DEGREES
REMARK 500 ASP C 375 CB - CG - OD1 ANGL. DEV. = -6.2 DEGREES
REMARK 500 PHE D 3 CB - CG - CD1 ANGL. DEV. = 5.3 DEGREES
REMARK 500 ARG D 43 NE - CZ - NH1 ANGL. DEV. = 4.4 DEGREES
REMARK 500 ARG D 96 NE - CZ - NH1 ANGL. DEV. = -3.9 DEGREES
REMARK 500 ARG D 130 NE - CZ - NH2 ANGL. DEV. = -3.7 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 60 ANGLE DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 PHE A 68 -82.48 -91.53
REMARK 500 GLU A 231 -110.09 -87.88
REMARK 500 VAL A 325 -178.17 -69.12
REMARK 500 ASP A 326 95.44 -69.55
REMARK 500 THR A 327 -36.14 163.48
REMARK 500 ALA A 329 -155.63 47.81
REMARK 500 ARG A 341 -41.78 -134.48
REMARK 500 PHE B 3 -155.04 55.97
REMARK 500 ILE B 69 97.13 -160.92
REMARK 500 ASP B 122 109.48 -48.88
REMARK 500 GLU B 231 -111.13 -87.10
REMARK 500 VAL B 325 169.96 49.47
REMARK 500 THR B 327 -67.30 -170.21
REMARK 500 ALA B 328 151.10 179.63
REMARK 500 ALA B 329 143.64 -35.93
REMARK 500 ARG B 341 -40.73 -134.30
REMARK 500 PHE C 3 -150.19 55.58
REMARK 500 PHE C 68 -6.87 -154.23
REMARK 500 ASP C 120 56.40 -149.11
REMARK 500 GLU C 231 -111.31 -91.26
REMARK 500 THR C 322 -21.56 117.65
REMARK 500 ASP C 326 -16.59 87.15
REMARK 500 ARG C 341 -36.98 -131.54
REMARK 500 ASN D 5 64.56 -101.02
REMARK 500 ASP D 122 108.35 -48.64
REMARK 500 ASN D 230 34.84 70.26
REMARK 500 GLU D 231 -110.30 -89.38
REMARK 500 VAL D 325 -84.33 -131.17
REMARK 500 THR D 327 -30.02 54.48
REMARK 500 ALA D 328 171.23 -49.41
REMARK 500 ARG D 341 -41.97 -130.20
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA D 382 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 LYS D 41 O
REMARK 620 2 ASP D 44 OD1 70.6
REMARK 620 3 ASP D 44 OD2 117.8 53.2
REMARK 620 N 1 2
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA D 382
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT B 1501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A 1502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT B 1503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT C 1504
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT C 1505
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT D 1506
DBREF 1QH4 A 2 381 UNP P05122 KCRB_CHICK 2 381
DBREF 1QH4 B 2 381 UNP P05122 KCRB_CHICK 2 381
DBREF 1QH4 C 2 381 UNP P05122 KCRB_CHICK 2 381
DBREF 1QH4 D 2 381 UNP P05122 KCRB_CHICK 2 381
SEQRES 1 A 380 PRO PHE SER ASN SER HIS ASN LEU LEU LYS MET LYS TYR
SEQRES 2 A 380 SER VAL ASP ASP GLU TYR PRO ASP LEU SER VAL HIS ASN
SEQRES 3 A 380 ASN HIS MET ALA LYS VAL LEU THR LEU ASP LEU TYR LYS
SEQRES 4 A 380 LYS LEU ARG ASP ARG GLN THR SER SER GLY PHE THR LEU
SEQRES 5 A 380 ASP ASP VAL ILE GLN THR GLY VAL ASP ASN PRO GLY HIS
SEQRES 6 A 380 PRO PHE ILE MET THR VAL GLY CYS VAL ALA GLY ASP GLU
SEQRES 7 A 380 GLU SER TYR GLU VAL PHE LYS GLU LEU PHE ASP PRO VAL
SEQRES 8 A 380 ILE GLU ASP ARG HIS GLY GLY TYR LYS PRO THR ASP GLU
SEQRES 9 A 380 HIS LYS THR ASP LEU ASN ALA ASP ASN LEU GLN GLY GLY
SEQRES 10 A 380 ASP ASP LEU ASP PRO ASN TYR VAL LEU SER SER ARG VAL
SEQRES 11 A 380 ARG THR GLY ARG SER ILE ARG GLY PHE CYS LEU PRO PRO
SEQRES 12 A 380 HIS CYS SER ARG GLY GLU ARG ARG ALA ILE GLU LYS LEU
SEQRES 13 A 380 SER VAL GLU ALA LEU GLY SER LEU GLY GLY ASP LEU LYS
SEQRES 14 A 380 GLY LYS TYR TYR ALA LEU ARG ASN MET THR ASP ALA GLU
SEQRES 15 A 380 GLN GLN GLN LEU ILE ASP ASP HIS PHE LEU PHE ASP LYS
SEQRES 16 A 380 PRO VAL SER PRO LEU LEU LEU ALA SER GLY MET ALA ARG
SEQRES 17 A 380 ASP TRP PRO ASP ALA ARG GLY ILE TRP HIS ASN ASP ASN
SEQRES 18 A 380 LYS THR PHE LEU VAL TRP ILE ASN GLU GLU ASP HIS LEU
SEQRES 19 A 380 ARG VAL ILE SER MET GLN LYS GLY GLY ASN MET LYS GLU
SEQRES 20 A 380 VAL PHE THR ARG PHE CYS THR GLY LEU THR GLN ILE GLU
SEQRES 21 A 380 THR LEU PHE LYS SER LYS ASN TYR GLU PHE MET TRP ASN
SEQRES 22 A 380 PRO HIS LEU GLY TYR ILE LEU THR CYS PRO SER ASN LEU
SEQRES 23 A 380 GLY THR GLY LEU ARG ALA GLY VAL HIS ILE LYS LEU PRO
SEQRES 24 A 380 ASN LEU GLY LYS HIS GLU LYS PHE GLY GLU VAL LEU LYS
SEQRES 25 A 380 ARG LEU ARG LEU GLN LYS ARG GLY THR GLY GLY VAL ASP
SEQRES 26 A 380 THR ALA ALA VAL GLY GLY VAL PHE ASP VAL SER ASN ALA
SEQRES 27 A 380 ASP ARG LEU GLY PHE SER GLU VAL GLU LEU VAL GLN MET
SEQRES 28 A 380 VAL VAL ASP GLY VAL LYS LEU LEU ILE GLU MET GLU LYS
SEQRES 29 A 380 ARG LEU GLU LYS GLY GLN SER ILE ASP ASP LEU MET PRO
SEQRES 30 A 380 ALA GLN LYS
SEQRES 1 B 380 PRO PHE SER ASN SER HIS ASN LEU LEU LYS MET LYS TYR
SEQRES 2 B 380 SER VAL ASP ASP GLU TYR PRO ASP LEU SER VAL HIS ASN
SEQRES 3 B 380 ASN HIS MET ALA LYS VAL LEU THR LEU ASP LEU TYR LYS
SEQRES 4 B 380 LYS LEU ARG ASP ARG GLN THR SER SER GLY PHE THR LEU
SEQRES 5 B 380 ASP ASP VAL ILE GLN THR GLY VAL ASP ASN PRO GLY HIS
SEQRES 6 B 380 PRO PHE ILE MET THR VAL GLY CYS VAL ALA GLY ASP GLU
SEQRES 7 B 380 GLU SER TYR GLU VAL PHE LYS GLU LEU PHE ASP PRO VAL
SEQRES 8 B 380 ILE GLU ASP ARG HIS GLY GLY TYR LYS PRO THR ASP GLU
SEQRES 9 B 380 HIS LYS THR ASP LEU ASN ALA ASP ASN LEU GLN GLY GLY
SEQRES 10 B 380 ASP ASP LEU ASP PRO ASN TYR VAL LEU SER SER ARG VAL
SEQRES 11 B 380 ARG THR GLY ARG SER ILE ARG GLY PHE CYS LEU PRO PRO
SEQRES 12 B 380 HIS CYS SER ARG GLY GLU ARG ARG ALA ILE GLU LYS LEU
SEQRES 13 B 380 SER VAL GLU ALA LEU GLY SER LEU GLY GLY ASP LEU LYS
SEQRES 14 B 380 GLY LYS TYR TYR ALA LEU ARG ASN MET THR ASP ALA GLU
SEQRES 15 B 380 GLN GLN GLN LEU ILE ASP ASP HIS PHE LEU PHE ASP LYS
SEQRES 16 B 380 PRO VAL SER PRO LEU LEU LEU ALA SER GLY MET ALA ARG
SEQRES 17 B 380 ASP TRP PRO ASP ALA ARG GLY ILE TRP HIS ASN ASP ASN
SEQRES 18 B 380 LYS THR PHE LEU VAL TRP ILE ASN GLU GLU ASP HIS LEU
SEQRES 19 B 380 ARG VAL ILE SER MET GLN LYS GLY GLY ASN MET LYS GLU
SEQRES 20 B 380 VAL PHE THR ARG PHE CYS THR GLY LEU THR GLN ILE GLU
SEQRES 21 B 380 THR LEU PHE LYS SER LYS ASN TYR GLU PHE MET TRP ASN
SEQRES 22 B 380 PRO HIS LEU GLY TYR ILE LEU THR CYS PRO SER ASN LEU
SEQRES 23 B 380 GLY THR GLY LEU ARG ALA GLY VAL HIS ILE LYS LEU PRO
SEQRES 24 B 380 ASN LEU GLY LYS HIS GLU LYS PHE GLY GLU VAL LEU LYS
SEQRES 25 B 380 ARG LEU ARG LEU GLN LYS ARG GLY THR GLY GLY VAL ASP
SEQRES 26 B 380 THR ALA ALA VAL GLY GLY VAL PHE ASP VAL SER ASN ALA
SEQRES 27 B 380 ASP ARG LEU GLY PHE SER GLU VAL GLU LEU VAL GLN MET
SEQRES 28 B 380 VAL VAL ASP GLY VAL LYS LEU LEU ILE GLU MET GLU LYS
SEQRES 29 B 380 ARG LEU GLU LYS GLY GLN SER ILE ASP ASP LEU MET PRO
SEQRES 30 B 380 ALA GLN LYS
SEQRES 1 C 380 PRO PHE SER ASN SER HIS ASN LEU LEU LYS MET LYS TYR
SEQRES 2 C 380 SER VAL ASP ASP GLU TYR PRO ASP LEU SER VAL HIS ASN
SEQRES 3 C 380 ASN HIS MET ALA LYS VAL LEU THR LEU ASP LEU TYR LYS
SEQRES 4 C 380 LYS LEU ARG ASP ARG GLN THR SER SER GLY PHE THR LEU
SEQRES 5 C 380 ASP ASP VAL ILE GLN THR GLY VAL ASP ASN PRO GLY HIS
SEQRES 6 C 380 PRO PHE ILE MET THR VAL GLY CYS VAL ALA GLY ASP GLU
SEQRES 7 C 380 GLU SER TYR GLU VAL PHE LYS GLU LEU PHE ASP PRO VAL
SEQRES 8 C 380 ILE GLU ASP ARG HIS GLY GLY TYR LYS PRO THR ASP GLU
SEQRES 9 C 380 HIS LYS THR ASP LEU ASN ALA ASP ASN LEU GLN GLY GLY
SEQRES 10 C 380 ASP ASP LEU ASP PRO ASN TYR VAL LEU SER SER ARG VAL
SEQRES 11 C 380 ARG THR GLY ARG SER ILE ARG GLY PHE CYS LEU PRO PRO
SEQRES 12 C 380 HIS CYS SER ARG GLY GLU ARG ARG ALA ILE GLU LYS LEU
SEQRES 13 C 380 SER VAL GLU ALA LEU GLY SER LEU GLY GLY ASP LEU LYS
SEQRES 14 C 380 GLY LYS TYR TYR ALA LEU ARG ASN MET THR ASP ALA GLU
SEQRES 15 C 380 GLN GLN GLN LEU ILE ASP ASP HIS PHE LEU PHE ASP LYS
SEQRES 16 C 380 PRO VAL SER PRO LEU LEU LEU ALA SER GLY MET ALA ARG
SEQRES 17 C 380 ASP TRP PRO ASP ALA ARG GLY ILE TRP HIS ASN ASP ASN
SEQRES 18 C 380 LYS THR PHE LEU VAL TRP ILE ASN GLU GLU ASP HIS LEU
SEQRES 19 C 380 ARG VAL ILE SER MET GLN LYS GLY GLY ASN MET LYS GLU
SEQRES 20 C 380 VAL PHE THR ARG PHE CYS THR GLY LEU THR GLN ILE GLU
SEQRES 21 C 380 THR LEU PHE LYS SER LYS ASN TYR GLU PHE MET TRP ASN
SEQRES 22 C 380 PRO HIS LEU GLY TYR ILE LEU THR CYS PRO SER ASN LEU
SEQRES 23 C 380 GLY THR GLY LEU ARG ALA GLY VAL HIS ILE LYS LEU PRO
SEQRES 24 C 380 ASN LEU GLY LYS HIS GLU LYS PHE GLY GLU VAL LEU LYS
SEQRES 25 C 380 ARG LEU ARG LEU GLN LYS ARG GLY THR GLY GLY VAL ASP
SEQRES 26 C 380 THR ALA ALA VAL GLY GLY VAL PHE ASP VAL SER ASN ALA
SEQRES 27 C 380 ASP ARG LEU GLY PHE SER GLU VAL GLU LEU VAL GLN MET
SEQRES 28 C 380 VAL VAL ASP GLY VAL LYS LEU LEU ILE GLU MET GLU LYS
SEQRES 29 C 380 ARG LEU GLU LYS GLY GLN SER ILE ASP ASP LEU MET PRO
SEQRES 30 C 380 ALA GLN LYS
SEQRES 1 D 380 PRO PHE SER ASN SER HIS ASN LEU LEU LYS MET LYS TYR
SEQRES 2 D 380 SER VAL ASP ASP GLU TYR PRO ASP LEU SER VAL HIS ASN
SEQRES 3 D 380 ASN HIS MET ALA LYS VAL LEU THR LEU ASP LEU TYR LYS
SEQRES 4 D 380 LYS LEU ARG ASP ARG GLN THR SER SER GLY PHE THR LEU
SEQRES 5 D 380 ASP ASP VAL ILE GLN THR GLY VAL ASP ASN PRO GLY HIS
SEQRES 6 D 380 PRO PHE ILE MET THR VAL GLY CYS VAL ALA GLY ASP GLU
SEQRES 7 D 380 GLU SER TYR GLU VAL PHE LYS GLU LEU PHE ASP PRO VAL
SEQRES 8 D 380 ILE GLU ASP ARG HIS GLY GLY TYR LYS PRO THR ASP GLU
SEQRES 9 D 380 HIS LYS THR ASP LEU ASN ALA ASP ASN LEU GLN GLY GLY
SEQRES 10 D 380 ASP ASP LEU ASP PRO ASN TYR VAL LEU SER SER ARG VAL
SEQRES 11 D 380 ARG THR GLY ARG SER ILE ARG GLY PHE CYS LEU PRO PRO
SEQRES 12 D 380 HIS CYS SER ARG GLY GLU ARG ARG ALA ILE GLU LYS LEU
SEQRES 13 D 380 SER VAL GLU ALA LEU GLY SER LEU GLY GLY ASP LEU LYS
SEQRES 14 D 380 GLY LYS TYR TYR ALA LEU ARG ASN MET THR ASP ALA GLU
SEQRES 15 D 380 GLN GLN GLN LEU ILE ASP ASP HIS PHE LEU PHE ASP LYS
SEQRES 16 D 380 PRO VAL SER PRO LEU LEU LEU ALA SER GLY MET ALA ARG
SEQRES 17 D 380 ASP TRP PRO ASP ALA ARG GLY ILE TRP HIS ASN ASP ASN
SEQRES 18 D 380 LYS THR PHE LEU VAL TRP ILE ASN GLU GLU ASP HIS LEU
SEQRES 19 D 380 ARG VAL ILE SER MET GLN LYS GLY GLY ASN MET LYS GLU
SEQRES 20 D 380 VAL PHE THR ARG PHE CYS THR GLY LEU THR GLN ILE GLU
SEQRES 21 D 380 THR LEU PHE LYS SER LYS ASN TYR GLU PHE MET TRP ASN
SEQRES 22 D 380 PRO HIS LEU GLY TYR ILE LEU THR CYS PRO SER ASN LEU
SEQRES 23 D 380 GLY THR GLY LEU ARG ALA GLY VAL HIS ILE LYS LEU PRO
SEQRES 24 D 380 ASN LEU GLY LYS HIS GLU LYS PHE GLY GLU VAL LEU LYS
SEQRES 25 D 380 ARG LEU ARG LEU GLN LYS ARG GLY THR GLY GLY VAL ASP
SEQRES 26 D 380 THR ALA ALA VAL GLY GLY VAL PHE ASP VAL SER ASN ALA
SEQRES 27 D 380 ASP ARG LEU GLY PHE SER GLU VAL GLU LEU VAL GLN MET
SEQRES 28 D 380 VAL VAL ASP GLY VAL LYS LEU LEU ILE GLU MET GLU LYS
SEQRES 29 D 380 ARG LEU GLU LYS GLY GLN SER ILE ASP ASP LEU MET PRO
SEQRES 30 D 380 ALA GLN LYS
HET ACT A1502 4
HET ACT B1501 4
HET ACT B1503 4
HET ACT C1504 4
HET ACT C1505 4
HET CA D 382 1
HET ACT D1506 4
HETNAM ACT ACETATE ION
HETNAM CA CALCIUM ION
FORMUL 5 ACT 6(C2 H3 O2 1-)
FORMUL 10 CA CA 2+
FORMUL 12 HOH *1467(H2 O)
HELIX 1 1 SER A 6 LYS A 13 1 8
HELIX 2 2 VAL A 16 GLU A 19 1 4
HELIX 3 3 HIS A 29 VAL A 33 1 5
HELIX 4 4 LEU A 36 LEU A 42 1 7
HELIX 5 5 LEU A 53 ASP A 62 1 10
HELIX 6 6 GLU A 79 VAL A 84 5 6
HELIX 7 7 LYS A 86 ARG A 96 1 11
HELIX 8 8 ALA A 112 ASN A 114 5 3
HELIX 9 9 ARG A 148 SER A 164 1 17
HELIX 10 10 GLY A 167 LEU A 169 5 3
HELIX 11 11 LEU A 176 ASN A 178 5 3
HELIX 12 12 ASP A 181 ASP A 189 1 9
HELIX 13 13 PRO A 200 SER A 205 1 6
HELIX 14 14 MET A 246 LYS A 267 1 22
HELIX 15 15 PRO A 284 ASN A 286 5 3
HELIX 16 16 PRO A 300 LYS A 304 1 5
HELIX 17 17 PHE A 308 LEU A 315 1 8
HELIX 18 18 GLU A 346 LYS A 369 1 24
HELIX 19 19 ASP A 374 LEU A 376 5 3
HELIX 20 20 PHE B 3 HIS B 7 5 5
HELIX 21 21 LEU B 9 LYS B 13 5 5
HELIX 22 22 VAL B 16 GLU B 19 1 4
HELIX 23 23 HIS B 29 VAL B 33 1 5
HELIX 24 24 LEU B 36 LEU B 42 1 7
HELIX 25 25 LEU B 53 ASP B 62 1 10
HELIX 26 26 GLU B 79 VAL B 84 5 6
HELIX 27 27 LYS B 86 ARG B 96 1 11
HELIX 28 28 ALA B 112 ASN B 114 5 3
HELIX 29 29 ARG B 148 SER B 164 1 17
HELIX 30 30 GLY B 167 LEU B 169 5 3
HELIX 31 31 ASP B 181 ASP B 190 1 10
HELIX 32 32 PRO B 200 SER B 205 1 6
HELIX 33 33 MET B 246 LYS B 267 1 22
HELIX 34 34 PRO B 284 ASN B 286 5 3
HELIX 35 35 PRO B 300 LYS B 304 1 5
HELIX 36 36 PHE B 308 LEU B 315 1 8
HELIX 37 37 GLU B 346 LYS B 369 1 24
HELIX 38 38 ASP B 374 LEU B 376 5 3
HELIX 39 39 PHE C 3 HIS C 7 5 5
HELIX 40 40 LEU C 9 LYS C 13 5 5
HELIX 41 41 VAL C 16 GLU C 19 1 4
HELIX 42 42 HIS C 29 VAL C 33 1 5
HELIX 43 43 LEU C 36 LEU C 42 1 7
HELIX 44 44 LEU C 53 ASP C 62 1 10
HELIX 45 45 GLU C 79 VAL C 84 5 6
HELIX 46 46 LYS C 86 ARG C 96 1 11
HELIX 47 47 ALA C 112 ASN C 114 5 3
HELIX 48 48 ARG C 148 SER C 164 1 17
HELIX 49 49 GLY C 167 LEU C 169 5 3
HELIX 50 50 ASP C 181 ASP C 189 1 9
HELIX 51 51 PRO C 200 SER C 205 1 6
HELIX 52 52 MET C 246 LYS C 267 1 22
HELIX 53 53 PRO C 284 ASN C 286 5 3
HELIX 54 54 PRO C 300 LYS C 304 1 5
HELIX 55 55 PHE C 308 LEU C 315 1 8
HELIX 56 56 VAL C 325 THR C 327 5 3
HELIX 57 57 GLU C 346 LYS C 369 1 24
HELIX 58 58 ASP C 374 LEU C 376 5 3
HELIX 59 59 SER D 6 LYS D 13 1 8
HELIX 60 60 VAL D 16 GLU D 19 1 4
HELIX 61 61 HIS D 29 VAL D 33 1 5
HELIX 62 62 LEU D 36 LEU D 42 1 7
HELIX 63 63 LEU D 53 ASP D 62 1 10
HELIX 64 64 GLU D 79 VAL D 84 5 6
HELIX 65 65 LYS D 86 ARG D 96 1 11
HELIX 66 66 ALA D 112 ASN D 114 5 3
HELIX 67 67 ARG D 148 GLY D 163 1 16
HELIX 68 68 GLY D 167 LEU D 169 5 3
HELIX 69 69 ASP D 181 ASP D 189 1 9
HELIX 70 70 PRO D 200 SER D 205 1 6
HELIX 71 71 MET D 246 LYS D 267 1 22
HELIX 72 72 PRO D 284 ASN D 286 5 3
HELIX 73 73 PRO D 300 LYS D 304 1 5
HELIX 74 74 PHE D 308 ARG D 314 1 7
HELIX 75 75 GLU D 346 LYS D 369 1 24
HELIX 76 76 ASP D 374 LEU D 376 5 3
SHEET 1 A 8 GLY A 171 ALA A 175 0
SHEET 2 A 8 GLY A 216 ASN A 220 -1 N HIS A 219 O LYS A 172
SHEET 3 A 8 PHE A 225 ILE A 229 -1 N ILE A 229 O GLY A 216
SHEET 4 A 8 LEU A 235 LYS A 242 -1 N ILE A 238 O LEU A 226
SHEET 5 A 8 VAL A 126 ARG A 135 -1 N ARG A 135 O LEU A 235
SHEET 6 A 8 ARG A 292 LYS A 298 -1 N HIS A 296 O LEU A 127
SHEET 7 A 8 VAL A 333 ASN A 338 -1 N VAL A 336 O VAL A 295
SHEET 8 A 8 LEU A 317 ARG A 320 -1 N ARG A 320 O ASP A 335
SHEET 1 B 8 GLY B 171 ALA B 175 0
SHEET 2 B 8 GLY B 216 ASN B 220 -1 N HIS B 219 O LYS B 172
SHEET 3 B 8 PHE B 225 ILE B 229 -1 N ILE B 229 O GLY B 216
SHEET 4 B 8 LEU B 235 LYS B 242 -1 N ILE B 238 O LEU B 226
SHEET 5 B 8 VAL B 126 ARG B 135 -1 N ARG B 135 O LEU B 235
SHEET 6 B 8 ARG B 292 LYS B 298 -1 N HIS B 296 O LEU B 127
SHEET 7 B 8 VAL B 333 ASN B 338 -1 N VAL B 336 O VAL B 295
SHEET 8 B 8 LEU B 317 GLY B 321 -1 N ARG B 320 O ASP B 335
SHEET 1 C 8 GLY C 171 ALA C 175 0
SHEET 2 C 8 GLY C 216 ASN C 220 -1 N HIS C 219 O LYS C 172
SHEET 3 C 8 PHE C 225 ILE C 229 -1 N ILE C 229 O GLY C 216
SHEET 4 C 8 LEU C 235 LYS C 242 -1 N ILE C 238 O LEU C 226
SHEET 5 C 8 VAL C 126 ARG C 135 -1 N ARG C 135 O LEU C 235
SHEET 6 C 8 ARG C 292 LYS C 298 -1 N HIS C 296 O LEU C 127
SHEET 7 C 8 VAL C 333 ASN C 338 -1 N VAL C 336 O VAL C 295
SHEET 8 C 8 LEU C 317 GLY C 321 -1 N ARG C 320 O ASP C 335
SHEET 1 D 8 GLY D 171 ALA D 175 0
SHEET 2 D 8 GLY D 216 ASN D 220 -1 N HIS D 219 O LYS D 172
SHEET 3 D 8 PHE D 225 ILE D 229 -1 N ILE D 229 O GLY D 216
SHEET 4 D 8 LEU D 235 LYS D 242 -1 N ILE D 238 O LEU D 226
SHEET 5 D 8 VAL D 126 ARG D 135 -1 N ARG D 135 O LEU D 235
SHEET 6 D 8 ARG D 292 LYS D 298 -1 N HIS D 296 O LEU D 127
SHEET 7 D 8 VAL D 333 ASN D 338 -1 N VAL D 336 O VAL D 295
SHEET 8 D 8 LEU D 317 LYS D 319 -1 N GLN D 318 O SER D 337
LINK O LYS D 41 CA CA D 382 1555 1555 2.64
LINK OD1 ASP D 44 CA CA D 382 1555 1555 2.46
LINK OD2 ASP D 44 CA CA D 382 1555 1555 2.44
CISPEP 1 TRP A 211 PRO A 212 0 4.72
CISPEP 2 TRP B 211 PRO B 212 0 3.05
CISPEP 3 TRP C 211 PRO C 212 0 1.27
CISPEP 4 TRP D 211 PRO D 212 0 1.00
SITE 1 AC1 2 LYS D 41 ASP D 44
SITE 1 AC2 4 SER B 15 VAL B 16 ARG B 43 HOH B1850
SITE 1 AC3 6 THR A 71 VAL A 72 LEU A 201 HOH A1662
SITE 2 AC3 6 HOH A1692 HOH A1834
SITE 1 AC4 6 THR B 71 VAL B 72 LEU B 201 HOH B1574
SITE 2 AC4 6 HOH B1706 HOH B1833
SITE 1 AC5 6 THR C 71 VAL C 72 LEU C 201 HOH C1638
SITE 2 AC5 6 HOH C1728 HOH C1788
SITE 1 AC6 5 ASN C 222 THR C 224 GLN C 241 LYS C 242
SITE 2 AC6 5 HOH C1653
SITE 1 AC7 6 THR D 71 VAL D 72 LEU D 201 HOH D1552
SITE 2 AC7 6 HOH D1604 HOH D1616
CRYST1 48.430 175.990 95.400 90.00 95.85 90.00 P 1 21 1 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 0.020648 0.000000 0.002115 0.00000
SCALE2 0.000000 0.005682 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010537 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
