HEADER HORMONE(MUSCLE RELAXANT) 21-JUN-91 6RLX
TITLE X-RAY STRUCTURE OF HUMAN RELAXIN AT 1.5 ANGSTROMS. COMPARISON TO
TITLE 2 INSULIN AND IMPLICATIONS FOR RECEPTOR BINDING DETERMINANTS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: RELAXIN, A-CHAIN;
COMPND 3 CHAIN: A, C;
COMPND 4 ENGINEERED: YES;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: RELAXIN, B-CHAIN;
COMPND 7 CHAIN: B, D;
COMPND 8 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 MOL_ID: 2;
SOURCE 8 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 9 ORGANISM_COMMON: HUMAN;
SOURCE 10 ORGANISM_TAXID: 9606;
SOURCE 11 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 12 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS HORMONE(MUSCLE RELAXANT)
EXPDTA X-RAY DIFFRACTION
AUTHOR C.EIGENBROT,M.RANDAL,A.A.KOSSIAKOFF
REVDAT 8 13-MAR-24 6RLX 1 SOURCE
REVDAT 7 25-DEC-19 6RLX 1 SEQRES
REVDAT 6 14-AUG-19 6RLX 1 REMARK
REVDAT 5 17-JUL-19 6RLX 1 REMARK LINK
REVDAT 4 16-NOV-11 6RLX 1 VERSN HETATM
REVDAT 3 24-FEB-09 6RLX 1 VERSN
REVDAT 2 01-APR-03 6RLX 1 JRNL
REVDAT 1 31-OCT-93 6RLX 0
JRNL AUTH C.EIGENBROT,M.RANDAL,C.QUAN,J.BURNIER,L.O'CONNELL,
JRNL AUTH 2 E.RINDERKNECHT,A.A.KOSSIAKOFF
JRNL TITL X-RAY STRUCTURE OF HUMAN RELAXIN AT 1.5 A. COMPARISON TO
JRNL TITL 2 INSULIN AND IMPLICATIONS FOR RECEPTOR BINDING DETERMINANTS.
JRNL REF J.MOL.BIOL. V. 221 15 1991
JRNL REFN ISSN 0022-2836
JRNL PMID 1656049
REMARK 2
REMARK 2 RESOLUTION. 1.50 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) : 1.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : NULL
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : NULL
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) : 0.187
REMARK 3 R VALUE (WORKING SET) : 0.187
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 : 768
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 73
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) : NULL ; NULL
REMARK 3 ANGLE DISTANCE (A) : NULL ; NULL
REMARK 3 INTRAPLANAR 1-4 DISTANCE (A) : NULL ; NULL
REMARK 3 H-BOND OR METAL COORDINATION (A) : NULL ; NULL
REMARK 3
REMARK 3 PLANE RESTRAINT (A) : NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINT (A**3) : NULL ; NULL
REMARK 3
REMARK 3 NON-BONDED CONTACT RESTRAINTS.
REMARK 3 SINGLE TORSION (A) : NULL ; NULL
REMARK 3 MULTIPLE TORSION (A) : NULL ; NULL
REMARK 3 H-BOND (X...Y) (A) : NULL ; NULL
REMARK 3 H-BOND (X-H...Y) (A) : NULL ; NULL
REMARK 3
REMARK 3 CONFORMATIONAL TORSION ANGLE RESTRAINTS.
REMARK 3 SPECIFIED (DEGREES) : NULL ; NULL
REMARK 3 PLANAR (DEGREES) : NULL ; NULL
REMARK 3 STAGGERED (DEGREES) : NULL ; NULL
REMARK 3 TRANSVERSE (DEGREES) : NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 6RLX 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_1000179862.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : NULL
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : NULL
REMARK 200 RADIATION SOURCE : NULL
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : NULL
REMARK 200 WAVELENGTH OR RANGE (A) : NULL
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : NULL
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : NULL
REMARK 200 RESOLUTION RANGE HIGH (A) : NULL
REMARK 200 RESOLUTION RANGE LOW (A) : NULL
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : NULL
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
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: X-PLOR
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 39.07
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.02
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 30.84000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 30.84000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 26.98500
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 28.44000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 26.98500
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 28.44000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 30.84000
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 26.98500
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 28.44000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 30.84000
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 26.98500
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 28.44000
REMARK 290 SMTRY3 8 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 300 REMARK: PSEUDO TWO-FOLD CALCULATED FROM C ALPHA PORTIONS A 6 - A 20
REMARK 300 AND B 7 - B 19 AND THE CORRESPONDING ATOMS OF MOLECULE 2.
REMARK 300 THE TRANSFORMATION PRESENTED ON *MTRIX* RECORDS BELOW WILL
REMARK 300 YIELD APPROXIMATE COORDINATES FOR CHAINS *C* AND *D* WHEN
REMARK 300 APPLIED TO CHAINS *A* AND *B*, RESPECTIVELY.
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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4330 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 5620 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -41.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, 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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH C 71 LIES ON A SPECIAL POSITION.
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 SER B 25
REMARK 465 THR D 23
REMARK 465 TRP D 24
REMARK 465 SER D 25
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 PCA A -3 CG CD OE
REMARK 470 SER D 22 CB OG
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 NH2 ARG B 9 NH2 ARG B 9 4566 1.94
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 TYR A -1 CB - CG - CD2 ANGL. DEV. = 4.7 DEGREES
REMARK 500 TYR A -1 CB - CG - CD1 ANGL. DEV. = -5.2 DEGREES
REMARK 500 ASN A 4 O - C - N ANGL. DEV. = 10.8 DEGREES
REMARK 500 LYS A 5 CA - C - N ANGL. DEV. = 14.8 DEGREES
REMARK 500 LYS A 5 O - C - N ANGL. DEV. = -12.7 DEGREES
REMARK 500 ARG A 14 CD - NE - CZ ANGL. DEV. = 11.7 DEGREES
REMARK 500 ARG A 18 CD - NE - CZ ANGL. DEV. = 10.5 DEGREES
REMARK 500 ARG A 18 NE - CZ - NH1 ANGL. DEV. = 6.2 DEGREES
REMARK 500 MET B 0 CA - CB - CG ANGL. DEV. = -10.6 DEGREES
REMARK 500 LEU B 6 O - C - N ANGL. DEV. = 12.3 DEGREES
REMARK 500 ARG B 9 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 ARG B 9 CA - C - O ANGL. DEV. = 14.5 DEGREES
REMARK 500 GLU B 10 OE1 - CD - OE2 ANGL. DEV. = 7.8 DEGREES
REMARK 500 GLU B 10 CG - CD - OE1 ANGL. DEV. = -17.9 DEGREES
REMARK 500 GLU B 10 CG - CD - OE2 ANGL. DEV. = 17.0 DEGREES
REMARK 500 GLU B 10 CG - CD - OE2 ANGL. DEV. = -19.2 DEGREES
REMARK 500 ARG B 13 NE - CZ - NH1 ANGL. DEV. = -3.2 DEGREES
REMARK 500 ALA B 14 O - C - N ANGL. DEV. = 11.9 DEGREES
REMARK 500 TYR C -1 O - C - N ANGL. DEV. = -11.4 DEGREES
REMARK 500 ARG C 14 NE - CZ - NH1 ANGL. DEV. = 5.2 DEGREES
REMARK 500 ARG C 14 NE - CZ - NH2 ANGL. DEV. = -6.7 DEGREES
REMARK 500 ALA C 17 O - C - N ANGL. DEV. = 9.9 DEGREES
REMARK 500 PHE C 19 CB - CG - CD2 ANGL. DEV. = 6.0 DEGREES
REMARK 500 MET D 0 CA - CB - CG ANGL. DEV. = -14.0 DEGREES
REMARK 500 LEU D 6 O - C - N ANGL. DEV. = 17.3 DEGREES
REMARK 500 ARG D 9 NE - CZ - NH1 ANGL. DEV. = -4.0 DEGREES
REMARK 500 GLU D 10 OE1 - CD - OE2 ANGL. DEV. = -8.3 DEGREES
REMARK 500 GLU D 10 CG - CD - OE2 ANGL. DEV. = 13.1 DEGREES
REMARK 500 ARG D 13 CD - NE - CZ ANGL. DEV. = 9.6 DEGREES
REMARK 500 ARG D 13 NE - CZ - NH1 ANGL. DEV. = 9.2 DEGREES
REMARK 500 ARG D 13 NE - CZ - NH2 ANGL. DEV. = -5.0 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 SER B 22 49.26 -83.44
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 ARG C 14 0.24 SIDE CHAIN
REMARK 500 ARG D 9 0.09 SIDE CHAIN
REMARK 500 ARG D 13 0.10 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 NUMBERING OF THE RESIDUES IS BASED ON INSULIN (EG. 1INS OF
REMARK 999 PROTEIN DATA BANK). WEAK OR NONEXISTENT ELECTRON DENSITY
REMARK 999 PREVENTS IDENTIFICATION OF THE FOLLOWING: SOME ATOMS OF
REMARK 999 PCA A(-3); RESIDUES SER B 25, THR D 23, TRP D 24 AND SER D
REMARK 999 25. MULTIPLE ATOMIC POSITIONS ARE INCLUDED FOR SIDE CHAIN
REMARK 999 ATOMS OF THE FOLLOWING RESIDUES: SER A 15, GLU B 10, TRP B
REMARK 999 24, AND ARG C 14.
DBREF 6RLX A -2 20 UNP P04090 REL2_HUMAN 162 185
DBREF 6RLX B -2 25 UNP P04090 REL2_HUMAN 26 53
DBREF 6RLX C -2 20 UNP P04090 REL2_HUMAN 162 185
DBREF 6RLX D -2 25 UNP P04090 REL2_HUMAN 26 53
SEQRES 1 A 24 PCA LEU TYR SER ALA LEU ALA ASN LYS CYS CYS HIS VAL
SEQRES 2 A 24 GLY CYS THR LYS ARG SER LEU ALA ARG PHE CYS
SEQRES 1 B 28 SER TRP MET GLU GLU VAL ILE LYS LEU CYS GLY ARG GLU
SEQRES 2 B 28 LEU VAL ARG ALA GLN ILE ALA ILE CYS GLY MET SER THR
SEQRES 3 B 28 TRP SER
SEQRES 1 C 24 PCA LEU TYR SER ALA LEU ALA ASN LYS CYS CYS HIS VAL
SEQRES 2 C 24 GLY CYS THR LYS ARG SER LEU ALA ARG PHE CYS
SEQRES 1 D 28 SER TRP MET GLU GLU VAL ILE LYS LEU CYS GLY ARG GLU
SEQRES 2 D 28 LEU VAL ARG ALA GLN ILE ALA ILE CYS GLY MET SER THR
SEQRES 3 D 28 TRP SER
MODRES 6RLX PCA A -3 GLN PYROGLUTAMIC ACID
MODRES 6RLX PCA C -3 GLN PYROGLUTAMIC ACID
HET PCA A -3 5
HET PCA C -3 8
HETNAM PCA PYROGLUTAMIC ACID
FORMUL 1 PCA 2(C5 H7 N O3)
FORMUL 5 HOH *73(H2 O)
HELIX 1 A1 PCA A -3 VAL A 9 1 13
HELIX 2 A2 LYS A 13 CYS A 20 1IRREGULAR; ALSO CLASS 5 8
HELIX 3 B1 SER B -2 GLU B 2 5 5
HELIX 4 B2 CYS B 7 SER B 22 1 16
HELIX 5 C1 PCA C -3 VAL C 9 1 13
HELIX 6 C2 LYS C 13 CYS C 20 1IRREGULAR; ALSO CLASS 5 8
HELIX 7 D1 SER D -2 GLU D 2 5 5
HELIX 8 D2 CYS D 7 SER D 22 1 16
SHEET 1 A 2 CYS A 11 THR A 12 0
SHEET 2 A 2 VAL B 3 ILE B 4 -1 O ILE B 4 N CYS A 11
SHEET 1 B 2 CYS C 11 THR C 12 0
SHEET 2 B 2 VAL D 3 ILE D 4 -1 N ILE D 4 O CYS C 11
SSBOND 1 CYS A 6 CYS A 11 1555 1555 2.06
SSBOND 2 CYS A 7 CYS B 7 1555 1555 2.06
SSBOND 3 CYS A 20 CYS B 19 1555 1555 2.00
SSBOND 4 CYS C 6 CYS C 11 1555 1555 2.01
SSBOND 5 CYS C 7 CYS D 7 1555 1555 2.06
SSBOND 6 CYS C 20 CYS D 19 1555 1555 2.02
LINK C PCA A -3 N LEU A -2 1555 1555 1.31
LINK C PCA C -3 N LEU C -2 1555 1555 1.31
CRYST1 53.970 56.880 61.680 90.00 90.00 90.00 C 2 2 21 16
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 0.018529 0.000000 0.000000 0.00000
SCALE2 0.000000 0.017581 0.000000 0.00000
SCALE3 0.000000 0.000000 0.016213 0.00000
MTRIX1 1 0.830125 0.207228 -0.517638 19.36984 1
MTRIX2 1 0.164367 -0.978064 -0.127962 28.26602 1
MTRIX3 1 -0.532801 0.021142 -0.845977 77.56604 1
HETATM 1 N PCA A -3 47.559 10.287 34.369 1.00 51.69 N
HETATM 2 CA PCA A -3 48.049 10.648 33.032 1.00 50.45 C
HETATM 3 CB PCA A -3 49.359 9.916 32.795 1.00 53.08 C
HETATM 4 C PCA A -3 47.020 10.314 31.952 1.00 49.10 C
HETATM 5 O PCA A -3 46.954 10.993 30.919 1.00 51.02 O
(ATOM LINES ARE NOT SHOWN.)
END
