HEADER SERINE PROTEASE 03-DEC-95 1CEA
TITLE THE STRUCTURE OF THE NON-COVALENT COMPLEX OF RECOMBINANT KRINGLE 1
TITLE 2 DOMAIN OF HUMAN PLASMINOGEN WITH EACA (EPSILON-AMINOCAPROIC ACID)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PLASMINOGEN;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: KRINGLE 1;
COMPND 5 SYNONYM: K1PG;
COMPND 6 EC: 3.4.21.7;
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 ORGAN: BLOOD;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS SERINE PROTEASE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.TULINSKY,I.I.MATHEWS
REVDAT 4 15-NOV-23 1CEA 1 REMARK ATOM
REVDAT 3 29-NOV-17 1CEA 1 HELIX
REVDAT 2 24-FEB-09 1CEA 1 VERSN
REVDAT 1 03-APR-96 1CEA 0
JRNL AUTH I.I.MATHEWS,P.VANDERHOFF-HANAVER,F.J.CASTELLINO,A.TULINSKY
JRNL TITL CRYSTAL STRUCTURES OF THE RECOMBINANT KRINGLE 1 DOMAIN OF
JRNL TITL 2 HUMAN PLASMINOGEN IN COMPLEXES WITH THE LIGANDS
JRNL TITL 3 EPSILON-AMINOCAPROIC ACID AND
JRNL TITL 4 TRANS-4-(AMINOMETHYL)CYCLOHEXANE-1-CARBOXYLIC ACID.
JRNL REF BIOCHEMISTRY V. 35 2567 1996
JRNL REFN ISSN 0006-2960
JRNL PMID 8611560
JRNL DOI 10.1021/BI9521351
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH M.R.REJANTE,M.LLINAS
REMARK 1 TITL 1H-NMR ASSIGNMENTS AND SECONDARY STRUCTURE OF HUMAN
REMARK 1 TITL 2 PLASMINOGEN KRINGLE 1
REMARK 1 REF EUR.J.BIOCHEM. V. 221 939 1994
REMARK 1 REFN ISSN 0014-2956
REMARK 1 REFERENCE 2
REMARK 1 AUTH T.-P.WU,K.P.PADMANABHAN,A.TULINSKY
REMARK 1 TITL THE STRUCTURE OF RECOMBINANT PLASMINOGEN KRINGLE 1 AND THE
REMARK 1 TITL 2 FIBRIN BINDING SITE
REMARK 1 REF BLOOD COAGULATION V. 5 157 1994
REMARK 1 REF 2 FIBRINOLYSIS
REMARK 1 REFN ISSN 0957-5235
REMARK 1 REFERENCE 3
REMARK 1 AUTH A.TULINSKY,C.H.PARK,B.MAO,M.LLINAS
REMARK 1 TITL LYSINE(SLASH)FIBRIN BINDING SITES OF KRINGLES MODELED AFTER
REMARK 1 TITL 2 THE STRUCTURE OF KRINGLE 1 OF PROTHROMBIN
REMARK 1 REF PROTEINS V. 3 85 1988
REMARK 1 REFN ISSN 0887-3585
REMARK 2
REMARK 2 RESOLUTION. 2.06 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PROLSQ
REMARK 3 AUTHORS : KONNERT,HENDRICKSON
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.06
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 7.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 3.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 83.4
REMARK 3 NUMBER OF REFLECTIONS : 8461
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING + TEST SET) : 0.168
REMARK 3 R VALUE (WORKING SET) : NULL
REMARK 3 FREE R VALUE : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : NULL
REMARK 3
REMARK 3 FIT/AGREEMENT OF MODEL WITH ALL DATA.
REMARK 3 R VALUE (WORKING + TEST SET, NO CUTOFF) : NULL
REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : NULL
REMARK 3 FREE R VALUE (NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : NULL
REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1276
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 18
REMARK 3 SOLVENT ATOMS : 148
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) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 DISTANCE RESTRAINTS. RMS SIGMA
REMARK 3 BOND LENGTH (A) : 0.020 ; 0.020
REMARK 3 ANGLE DISTANCE (A) : 0.050 ; 0.040
REMARK 3 INTRAPLANAR 1-4 DISTANCE (A) : 0.060 ; 0.060
REMARK 3 H-BOND OR METAL COORDINATION (A) : NULL ; NULL
REMARK 3
REMARK 3 PLANE RESTRAINT (A) : 0.040 ; 0.040
REMARK 3 CHIRAL-CENTER RESTRAINT (A**3) : 0.060 ; 0.150
REMARK 3
REMARK 3 NON-BONDED CONTACT RESTRAINTS.
REMARK 3 SINGLE TORSION (A) : 0.230 ; 0.600
REMARK 3 MULTIPLE TORSION (A) : 0.280 ; 0.600
REMARK 3 H-BOND (X...Y) (A) : NULL ; NULL
REMARK 3 H-BOND (X-H...Y) (A) : 0.320 ; 0.600
REMARK 3
REMARK 3 CONFORMATIONAL TORSION ANGLE RESTRAINTS.
REMARK 3 SPECIFIED (DEGREES) : NULL ; NULL
REMARK 3 PLANAR (DEGREES) : 3.800 ; 3.000
REMARK 3 STAGGERED (DEGREES) : 22.000; 15.000
REMARK 3 TRANSVERSE (DEGREES) : NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 1.200 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 1.700 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 2.500 ; 2.500
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 3.100 ; 3.000
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 NO ELECTRON DENSITY WAS OBSERVED FOR THE INTERKRINGLE
REMARK 3 RESIDUES 3A - 2A AND 80 - 86 IN BOTH MOLECULES. ARG A 34
REMARK 3 HAS NO SIDE CHAIN ATOMS BEYOND CB DUE TO WEAK ELECTRON
REMARK 3 DENSITY.
REMARK 4
REMARK 4 1CEA COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000172270.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 295
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU RU200
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IIC
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : R-AXIS
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 9309
REMARK 200 RESOLUTION RANGE HIGH (A) : NULL
REMARK 200 RESOLUTION RANGE LOW (A) : NULL
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.060
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 93.9
REMARK 200 DATA REDUNDANCY : 4.200
REMARK 200 R MERGE (I) : 0.07630
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 1.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 34.78
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.89
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
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 25.80000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: 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: 2
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 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 LEU A -1
REMARK 465 SER A 0
REMARK 465 GLU A 80
REMARK 465 GLU A 81
REMARK 465 GLU A 82
REMARK 465 CYS A 83
REMARK 465 MET A 84
REMARK 465 HIS A 85
REMARK 465 LEU B -1
REMARK 465 SER B 0
REMARK 465 GLU B 80
REMARK 465 GLU B 81
REMARK 465 GLU B 82
REMARK 465 CYS B 83
REMARK 465 MET B 84
REMARK 465 HIS B 85
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 ARG A 34 CG CD NE CZ NH1 NH2
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 OD1 ASN A 18 OD2 ASP A 72 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 GLU A 46 CG GLU A 46 CD 0.092
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 GLU A 1A CA - CB - CG ANGL. DEV. = 21.8 DEGREES
REMARK 500 LYS A 2 CB - CA - C ANGL. DEV. = -13.2 DEGREES
REMARK 500 ARG A 10 CD - NE - CZ ANGL. DEV. = 24.1 DEGREES
REMARK 500 ARG A 10 NE - CZ - NH1 ANGL. DEV. = 4.9 DEGREES
REMARK 500 ARG A 10 NE - CZ - NH2 ANGL. DEV. = -6.8 DEGREES
REMARK 500 SER A 14 N - CA - CB ANGL. DEV. = -9.1 DEGREES
REMARK 500 SER A 27 CB - CA - C ANGL. DEV. = 14.3 DEGREES
REMARK 500 ARG A 32 CD - NE - CZ ANGL. DEV. = 13.7 DEGREES
REMARK 500 THR A 39 N - CA - CB ANGL. DEV. = -12.6 DEGREES
REMARK 500 THR A 39 CA - CB - CG2 ANGL. DEV. = 12.1 DEGREES
REMARK 500 GLU A 46 OE1 - CD - OE2 ANGL. DEV. = -8.1 DEGREES
REMARK 500 ARG A 51 NE - CZ - NH1 ANGL. DEV. = 5.4 DEGREES
REMARK 500 TYR A 63 CB - CG - CD1 ANGL. DEV. = -3.7 DEGREES
REMARK 500 THR A 64 C - N - CA ANGL. DEV. = 18.6 DEGREES
REMARK 500 ASP A 66 CB - CG - OD2 ANGL. DEV. = 9.0 DEGREES
REMARK 500 ARG A 70 CD - NE - CZ ANGL. DEV. = 9.6 DEGREES
REMARK 500 ARG A 70 NE - CZ - NH1 ANGL. DEV. = 8.0 DEGREES
REMARK 500 TYR A 71 CB - CG - CD2 ANGL. DEV. = -3.8 DEGREES
REMARK 500 TYR A 73 CB - CG - CD2 ANGL. DEV. = -6.7 DEGREES
REMARK 500 ASP A 75 CB - CG - OD2 ANGL. DEV. = -9.1 DEGREES
REMARK 500 LEU A 77 CB - CA - C ANGL. DEV. = 15.6 DEGREES
REMARK 500 CYS A 79 CA - CB - SG ANGL. DEV. = 9.0 DEGREES
REMARK 500 ASN B 8 CB - CG - OD1 ANGL. DEV. = -12.9 DEGREES
REMARK 500 TYR B 9 CG - CD2 - CE2 ANGL. DEV. = 5.1 DEGREES
REMARK 500 TYR B 9 CZ - CE2 - CD2 ANGL. DEV. = -5.7 DEGREES
REMARK 500 ARG B 10 CD - NE - CZ ANGL. DEV. = 15.2 DEGREES
REMARK 500 ARG B 10 NE - CZ - NH1 ANGL. DEV. = 10.2 DEGREES
REMARK 500 ARG B 10 NE - CZ - NH2 ANGL. DEV. = -12.5 DEGREES
REMARK 500 GLY B 11 C - N - CA ANGL. DEV. = 14.0 DEGREES
REMARK 500 MET B 13 CA - CB - CG ANGL. DEV. = 12.7 DEGREES
REMARK 500 CYS B 22 O - C - N ANGL. DEV. = 14.2 DEGREES
REMARK 500 SER B 27 N - CA - CB ANGL. DEV. = -11.2 DEGREES
REMARK 500 ARG B 32 NE - CZ - NH1 ANGL. DEV. = -3.3 DEGREES
REMARK 500 ARG B 34 NE - CZ - NH1 ANGL. DEV. = 9.9 DEGREES
REMARK 500 ARG B 34 NE - CZ - NH2 ANGL. DEV. = -9.0 DEGREES
REMARK 500 THR B 39 N - CA - CB ANGL. DEV. = -14.6 DEGREES
REMARK 500 THR B 39 OG1 - CB - CG2 ANGL. DEV. = 14.2 DEGREES
REMARK 500 GLU B 46 C - N - CA ANGL. DEV. = 17.8 DEGREES
REMARK 500 GLU B 46 CB - CG - CD ANGL. DEV. = 20.5 DEGREES
REMARK 500 GLU B 46 OE1 - CD - OE2 ANGL. DEV. = -7.6 DEGREES
REMARK 500 GLU B 46 CG - CD - OE1 ANGL. DEV. = 14.9 DEGREES
REMARK 500 TYR B 49 CB - CG - CD2 ANGL. DEV. = -4.5 DEGREES
REMARK 500 ARG B 51 NE - CZ - NH1 ANGL. DEV. = 7.4 DEGREES
REMARK 500 ARG B 51 NE - CZ - NH2 ANGL. DEV. = -7.2 DEGREES
REMARK 500 ASP B 56 CB - CG - OD1 ANGL. DEV. = 8.8 DEGREES
REMARK 500 ARG B 70 NE - CZ - NH2 ANGL. DEV. = 4.2 DEGREES
REMARK 500 TYR B 73 CB - CG - CD2 ANGL. DEV. = -3.8 DEGREES
REMARK 500 ASP B 75 CB - CA - C ANGL. DEV. = -16.4 DEGREES
REMARK 500 ASP B 75 OD1 - CG - OD2 ANGL. DEV. = 16.4 DEGREES
REMARK 500 ASP B 75 CB - CG - OD1 ANGL. DEV. = -7.4 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 51 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 ARG A 10 45.37 -142.23
REMARK 500 GLU A 47 -128.97 39.33
REMARK 500 GLU B 47 -127.39 54.57
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 TYR A 9 0.06 SIDE CHAIN
REMARK 500 ASN A 48 0.07 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 GLU A 1A -11.17
REMARK 500 GLY A 6 12.21
REMARK 500 THR A 28 -10.91
REMARK 500 GLN A 58 11.80
REMARK 500 THR A 65 11.39
REMARK 500 ARG B 10 -12.93
REMARK 500 TRP B 25 10.35
REMARK 500 PRO B 30 10.58
REMARK 500 GLU B 47 11.52
REMARK 500 TYR B 49 -12.11
REMARK 500 ARG B 70 -10.55
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 ACA A 90
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACA B 90
DBREF 1CEA A -1 85 UNP P00747 PLMN_HUMAN 100 187
DBREF 1CEA B -1 85 UNP P00747 PLMN_HUMAN 100 187
SEQRES 1 A 88 LEU SER GLU CYS LYS THR GLY ASN GLY LYS ASN TYR ARG
SEQRES 2 A 88 GLY THR MET SER LYS THR LYS ASN GLY ILE THR CYS GLN
SEQRES 3 A 88 LYS TRP SER SER THR SER PRO HIS ARG PRO ARG PHE SER
SEQRES 4 A 88 PRO ALA THR HIS PRO SER GLU GLY LEU GLU GLU ASN TYR
SEQRES 5 A 88 CYS ARG ASN PRO ASP ASN ASP PRO GLN GLY PRO TRP CYS
SEQRES 6 A 88 TYR THR THR ASP PRO GLU LYS ARG TYR ASP TYR CYS ASP
SEQRES 7 A 88 ILE LEU GLU CYS GLU GLU GLU CYS MET HIS
SEQRES 1 B 88 LEU SER GLU CYS LYS THR GLY ASN GLY LYS ASN TYR ARG
SEQRES 2 B 88 GLY THR MET SER LYS THR LYS ASN GLY ILE THR CYS GLN
SEQRES 3 B 88 LYS TRP SER SER THR SER PRO HIS ARG PRO ARG PHE SER
SEQRES 4 B 88 PRO ALA THR HIS PRO SER GLU GLY LEU GLU GLU ASN TYR
SEQRES 5 B 88 CYS ARG ASN PRO ASP ASN ASP PRO GLN GLY PRO TRP CYS
SEQRES 6 B 88 TYR THR THR ASP PRO GLU LYS ARG TYR ASP TYR CYS ASP
SEQRES 7 B 88 ILE LEU GLU CYS GLU GLU GLU CYS MET HIS
HET ACA A 90 9
HET ACA B 90 9
HETNAM ACA 6-AMINOHEXANOIC ACID
HETSYN ACA AMINOCAPROIC ACID
FORMUL 3 ACA 2(C6 H13 N O2)
FORMUL 5 HOH *148(H2 O)
HELIX 1 1 HIS A 40 GLY A 44 5 5
SHEET 1 SA1 2 SER A 14 THR A 16 0
SHEET 2 SA1 2 ILE A 20 CYS A 22 -1
SHEET 1 SA2 2 GLN A 23 TRP A 25 0
SHEET 2 SA2 2 GLU A 47 TYR A 49 -1
SHEET 1 SB1 2 SER B 14 THR B 16 0
SHEET 2 SB1 2 ILE B 20 CYS B 22 -1
SHEET 1 SB2 2 GLN B 23 TRP B 25 0
SHEET 2 SB2 2 GLU B 47 TYR B 49 -1
SSBOND 1 CYS A 1 CYS A 79 1555 1555 1.97
SSBOND 2 CYS A 22 CYS A 62 1555 1555 2.14
SSBOND 3 CYS A 50 CYS A 74 1555 1555 2.02
SSBOND 4 CYS B 1 CYS B 79 1555 1555 2.02
SSBOND 5 CYS B 22 CYS B 62 1555 1555 2.02
SSBOND 6 CYS B 50 CYS B 74 1555 1555 2.01
CISPEP 1 SER A 29 PRO A 30 0 -0.64
CISPEP 2 SER B 29 PRO B 30 0 2.66
SITE 1 AC1 7 ARG A 34 ASP A 54 ASP A 56 TRP A 61
SITE 2 AC1 7 TYR A 63 ARG A 70 THR B 12
SITE 1 AC2 9 THR A 12 ARG B 34 PHE B 35 ASP B 54
SITE 2 AC2 9 ASP B 56 TRP B 61 TYR B 63 ARG B 70
SITE 3 AC2 9 TYR B 71
CRYST1 34.500 51.600 46.500 90.00 112.00 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 0.028986 0.000000 0.011711 0.00000
SCALE2 0.000000 0.019380 0.000000 0.00000
SCALE3 0.000000 0.000000 0.023194 0.00000
MTRIX1 1 -0.723800 -0.004600 -0.690000 20.94263 1
MTRIX2 1 0.000400 -1.000000 0.006300 0.64469 1
MTRIX3 1 -0.690000 0.004200 0.723800 33.39790 1
(ATOM LINES ARE NOT SHOWN.)
END