HEADER HORMONE/GROWTH FACTOR 29-AUG-02 1MKK
TITLE DISULFIDE DEFICIENT MUTANT OF VASCULAR ENDOTHELIAL GROWTH FACTOR A
TITLE 2 (C61A AND C104A)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: VASCULAR ENDOTHELIAL GROWTH FACTOR A;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: RESIDUES 40-134, SEQUENCE DATABASE;
COMPND 5 SYNONYM: VEGF-A, VASCULAR PERMEABILITY FACTOR, VPF;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: 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 EXPRESSION_SYSTEM_STRAIN: B843(DE3)PLYSS;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET-3D
KEYWDS CYSTINE-KNOT GROWTH FACTOR, HORMONE-GROWTH FACTOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.A.MULLER,C.HEIRING,R.MISSELWITZ,K.WELFLE,H.WELFLE
REVDAT 4 27-OCT-21 1MKK 1 REMARK SEQADV
REVDAT 3 11-OCT-17 1MKK 1 REMARK
REVDAT 2 24-FEB-09 1MKK 1 VERSN
REVDAT 1 11-DEC-02 1MKK 0
JRNL AUTH Y.A.MULLER,C.HEIRING,R.MISSELWITZ,K.WELFLE,H.WELFLE
JRNL TITL THE CYSTINE KNOT PROMOTES FOLDING AND NOT THERMODYNAMIC
JRNL TITL 2 STABILITY IN VASCULAR ENDOTHELIAL GROWTH FACTOR
JRNL REF J.BIOL.CHEM. V. 277 43410 2002
JRNL REFN ISSN 0021-9258
JRNL PMID 12207021
JRNL DOI 10.1074/JBC.M206438200
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH C.HEIRING,Y.A.MULLER
REMARK 1 TITL FOLDING SCREENING ASSAYED BY PROTEOLYSIS: APPLICATION TO
REMARK 1 TITL 2 VARIOUS CYSTINE DELETION MUTANTS OF VASCULAR ENDOTHELIAL
REMARK 1 TITL 3 GROWTH FACTOR
REMARK 1 REF PROTEIN ENG. V. 14 183 2001
REMARK 1 REFN ISSN 0269-2139
REMARK 1 DOI 10.1093/PROTEIN/14.3.183
REMARK 2
REMARK 2 RESOLUTION. 1.32 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.0
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.32
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 28.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 53318
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RESOLUTION SHELLS
REMARK 3 R VALUE (WORKING + TEST SET) : 0.168
REMARK 3 R VALUE (WORKING SET) : 0.165
REMARK 3 FREE R VALUE : 0.195
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 9.900
REMARK 3 FREE R VALUE TEST SET COUNT : 5264
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 REFLECTION IN BIN (WORKING SET) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE SET COUNT : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1505
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 205
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 22.06
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 19.58
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.32000
REMARK 3 B22 (A**2) : -0.86000
REMARK 3 B33 (A**2) : -0.46000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.03000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.083
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.073
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.045
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.060
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : NULL
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): NULL ; 0.011 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): NULL ; 1.403 ; 1.971
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): NULL ; 4.432 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): NULL ;17.099 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): NULL ; 0.090 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): NULL ; 0.006 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): NULL ; 2.959 ; 4.000
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; 4.298 ; 6.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; 4.722 ; 7.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; 6.790 ; 9.000
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; 2.331 ; 4.000
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ;13.105 ; 7.000
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; 7.144 ; 7.000
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET'S PRINCIPLE
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1MKK COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-SEP-02.
REMARK 100 THE DEPOSITION ID IS D_1000016985.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 05-AUG-02
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.6
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) : 0.8423
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 53321
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.320
REMARK 200 RESOLUTION RANGE LOW (A) : 28.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.2
REMARK 200 DATA REDUNDANCY : 3.800
REMARK 200 R MERGE (I) : 0.07400
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 12.0800
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.32
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.35
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.5
REMARK 200 DATA REDUNDANCY IN SHELL : 3.17
REMARK 200 R MERGE FOR SHELL (I) : 0.37500
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.480
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: PDB ENTRY 2VPF
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 52.67
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.60
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: ISOPROPANOL, PEG4000, PH 5.6, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 293K
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 37.73500
REMARK 290 SMTRY3 2 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: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2560 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 11370 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -25.0 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 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 MET A 13
REMARK 465 LYS A 107
REMARK 465 LYS A 108
REMARK 465 LYS B 107
REMARK 465 LYS B 108
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 MET B 13 CG SD CE
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 OE1 GLU A 38 O HOH A 121 2.02
REMARK 500
REMARK 500 REMARK: NULL
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 CYS B 26 CA - CB - SG ANGL. DEV. = 7.2 DEGREES
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 CYS A 26 118.71 -27.53
REMARK 500 CYS B 26 117.09 -28.87
REMARK 500 GLU B 42 51.62 -118.14
REMARK 500 PRO B 85 -59.15 -26.27
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2VPF RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF WILD-TYPE VASCULAR ENDOTHELIAL GROWTH FACTOR
REMARK 900 RELATED ID: 1MJV RELATED DB: PDB
REMARK 900 DISULFIDE DEFICIENT MUTANT OF VASCULAR ENDOTHELIAL GROWTH FACTOR A
REMARK 900 (C51A AND C60A)
REMARK 900 RELATED ID: 1MKG RELATED DB: PDB
REMARK 900 DISULFIDE DEFICIENT MUTANT OF VASCULAR ENDOTHELIAL GROWTH FACTOR A
REMARK 900 (C57A AND C102A)
DBREF 1MKK A 14 108 UNP P15692 VEGFA_HUMAN 40 134
DBREF 1MKK B 14 108 UNP P15692 VEGFA_HUMAN 40 134
SEQADV 1MKK MET A 13 UNP P15692 CLONING ARTIFACT
SEQADV 1MKK ALA A 61 UNP P15692 CYS 87 ENGINEERED MUTATION
SEQADV 1MKK ALA A 104 UNP P15692 CYS 130 ENGINEERED MUTATION
SEQADV 1MKK MET B 13 UNP P15692 CLONING ARTIFACT
SEQADV 1MKK ALA B 61 UNP P15692 CYS 87 ENGINEERED MUTATION
SEQADV 1MKK ALA B 104 UNP P15692 CYS 130 ENGINEERED MUTATION
SEQRES 1 A 96 MET VAL VAL LYS PHE MET ASP VAL TYR GLN ARG SER TYR
SEQRES 2 A 96 CYS HIS PRO ILE GLU THR LEU VAL ASP ILE PHE GLN GLU
SEQRES 3 A 96 TYR PRO ASP GLU ILE GLU TYR ILE PHE LYS PRO SER CYS
SEQRES 4 A 96 VAL PRO LEU MET ARG CYS GLY GLY CYS ALA ASN ASP GLU
SEQRES 5 A 96 GLY LEU GLU CYS VAL PRO THR GLU GLU SER ASN ILE THR
SEQRES 6 A 96 MET GLN ILE MET ARG ILE LYS PRO HIS GLN GLY GLN HIS
SEQRES 7 A 96 ILE GLY GLU MET SER PHE LEU GLN HIS ASN LYS CYS GLU
SEQRES 8 A 96 ALA ARG PRO LYS LYS
SEQRES 1 B 96 MET VAL VAL LYS PHE MET ASP VAL TYR GLN ARG SER TYR
SEQRES 2 B 96 CYS HIS PRO ILE GLU THR LEU VAL ASP ILE PHE GLN GLU
SEQRES 3 B 96 TYR PRO ASP GLU ILE GLU TYR ILE PHE LYS PRO SER CYS
SEQRES 4 B 96 VAL PRO LEU MET ARG CYS GLY GLY CYS ALA ASN ASP GLU
SEQRES 5 B 96 GLY LEU GLU CYS VAL PRO THR GLU GLU SER ASN ILE THR
SEQRES 6 B 96 MET GLN ILE MET ARG ILE LYS PRO HIS GLN GLY GLN HIS
SEQRES 7 B 96 ILE GLY GLU MET SER PHE LEU GLN HIS ASN LYS CYS GLU
SEQRES 8 B 96 ALA ARG PRO LYS LYS
FORMUL 3 HOH *205(H2 O)
HELIX 1 1 LYS A 16 TYR A 25 1 10
HELIX 2 2 ILE A 35 TYR A 39 1 5
HELIX 3 3 PRO A 40 ILE A 43 5 4
HELIX 4 4 LYS B 16 TYR B 25 1 10
HELIX 5 5 ILE B 35 TYR B 39 1 5
SHEET 1 A 2 HIS A 27 ASP A 34 0
SHEET 2 A 2 CYS A 51 GLY A 58 -1 O VAL A 52 N VAL A 33
SHEET 1 B 3 HIS A 90 ARG A 105 0
SHEET 2 B 3 GLU A 67 ILE A 83 -1 N GLU A 67 O ARG A 105
SHEET 3 B 3 ILE A 46 LYS A 48 -1 N LYS A 48 O MET A 81
SHEET 1 C 3 HIS A 90 ARG A 105 0
SHEET 2 C 3 GLU A 67 ILE A 83 -1 N GLU A 67 O ARG A 105
SHEET 3 C 3 VAL B 14 VAL B 15 1 O VAL B 15 N THR A 77
SHEET 1 D 2 HIS B 27 ASP B 34 0
SHEET 2 D 2 CYS B 51 GLY B 58 -1 O LEU B 54 N THR B 31
SHEET 1 E 3 ILE B 46 LYS B 48 0
SHEET 2 E 3 GLU B 67 ILE B 83 -1 O ILE B 83 N ILE B 46
SHEET 3 E 3 HIS B 90 ARG B 105 -1 O ARG B 105 N GLU B 67
SSBOND 1 CYS A 26 CYS A 68 1555 1555 2.03
SSBOND 2 CYS A 51 CYS B 60 1555 1555 2.05
SSBOND 3 CYS A 57 CYS A 102 1555 1555 2.04
SSBOND 4 CYS A 60 CYS B 51 1555 1555 2.06
SSBOND 5 CYS B 26 CYS B 68 1555 1555 2.03
SSBOND 6 CYS B 57 CYS B 102 1555 1555 2.02
CISPEP 1 LYS A 48 PRO A 49 0 -8.08
CISPEP 2 LYS B 48 PRO B 49 0 -8.30
CRYST1 28.220 75.470 55.120 90.00 97.25 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 0.035436 0.000000 0.004508 0.00000
SCALE2 0.000000 0.013250 0.000000 0.00000
SCALE3 0.000000 0.000000 0.018288 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
