Header list of 3pat.pdb file
Complete list - 16 20 Bytes
HEADER BINDING PROTEIN(CALCIUM) 22-MAR-94 3PAT
TITLE COMPARISON BETWEEN THE CRYSTAL AND THE SOLUTION STRUCTURES OF THE EF
TITLE 2 HAND PARVALBUMIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PARVALBUMIN;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESOX LUCIUS;
SOURCE 3 ORGANISM_COMMON: NORTHERN PIKE;
SOURCE 4 ORGANISM_TAXID: 8010
KEYWDS BINDING PROTEIN(CALCIUM)
EXPDTA SOLUTION NMR
AUTHOR A.PADILLA,A.CAVE,J.PARELLO,G.ETIENNE,C.BALDELLON
REVDAT 3 16-MAR-22 3PAT 1 REMARK LINK
REVDAT 2 24-FEB-09 3PAT 1 VERSN
REVDAT 1 31-JUL-94 3PAT 0
JRNL AUTH A.PADILLA,A.CAVE,J.PARELLO,G.ETIENNE,C.BALDELLON
JRNL TITL COMPARISON BETWEEN THE CRYSTAL AND THE SOLUTION STRUCTURES
JRNL TITL 2 OF THE EF HAND PARVALBUMIN
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH Y.BLANCUZZI,A.PADILLA,J.PARELLO,A.CAVE
REMARK 1 TITL SYMMETRICAL REARRANGEMENT OF CATION-BINDING SITES OF
REMARK 1 TITL 2 PARVALBUMIN UPON CA2+(SLASH)MG2+ EXCHANGE. A STUDY BY 1H 2D
REMARK 1 TITL 3 NMR
REMARK 1 REF BIOCHEMISTRY V. 32 1302 1993
REMARK 1 REFN ISSN 0006-2960
REMARK 1 REFERENCE 2
REMARK 1 AUTH A.PADILLA,G.W.VUISTER,R.BOELENS,G.KLEYWEGT,A.CAVE,J.PARELLO,
REMARK 1 AUTH 2 R.KAPTEIN
REMARK 1 TITL HOMONUCLEAR THREE-DIMENSIONAL 1H NMR SPECTROSCOPY OF PIKE
REMARK 1 TITL 2 PARVALBUMIN. COMPARISON OF SHORT-AND MEDIUM-RANGE NOES FROM
REMARK 1 TITL 3 2D AND 3D NMR
REMARK 1 REF J.AM.CHEM.SOC. V. 112 5024 1990
REMARK 1 REFN ISSN 0002-7863
REMARK 1 REFERENCE 3
REMARK 1 AUTH A.PADILLA,A.CAVE,J.PARELLO
REMARK 1 TITL TWO-DIMENSIONAL 1H NUCLEAR MAGNETIC RESONANCE STUDY OF PIKE
REMARK 1 TITL 2 PI 5.0 PARVALBUMIN (ESOX LUCIUS): SEQUENTIAL RESONANCE
REMARK 1 TITL 3 ASSIGNMENTS AND FOLDING OF THE POLYPEPTIDE CHAIN
REMARK 1 REF J.MOL.BIOL. V. 204 995 1988
REMARK 1 REFN ISSN 0022-2836
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.0
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3PAT 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_1000179081.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : NULL
REMARK 210 PH : NULL
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NULL
REMARK 210 SPECTROMETER FIELD STRENGTH : NULL
REMARK 210 SPECTROMETER MODEL : NULL
REMARK 210 SPECTROMETER MANUFACTURER : NULL
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : NULL
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : NULL
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 1
REMARK 210 CONFORMERS, SELECTION CRITERIA : NULL
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK: NULL
REMARK 215
REMARK 215 NMR STUDY
REMARK 215 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM SOLUTION
REMARK 215 NMR DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE THAT
REMARK 215 CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES ON
REMARK 215 THESE RECORDS ARE MEANINGLESS.
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: 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 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
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 O ASN A 25 N HIS A 26 0.33
REMARK 500 O ARG A 75 N ASP A 76 0.47
REMARK 500 O MET A 38 N SER A 39 0.76
REMARK 500 O LYS A 7 CB ALA A 8 0.95
REMARK 500 O LYS A 7 CA ALA A 8 1.14
REMARK 500 O LYS A 7 N ALA A 8 1.23
REMARK 500 O ALA A 71 N ALA A 72 1.29
REMARK 500 O ASP A 53 N ALA A 54 1.36
REMARK 500 C LYS A 7 CA ALA A 8 1.52
REMARK 500 O ASP A 90 N LYS A 91 1.55
REMARK 500 CA LYS A 7 N ALA A 8 1.55
REMARK 500 CB LYS A 7 N ALA A 8 1.70
REMARK 500 O THR A 78 N ASP A 79 1.73
REMARK 500 O ASN A 25 CA HIS A 26 1.80
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 ACE A 0 C ALA A 1 N -0.631
REMARK 500 ALA A 1 N ALA A 1 CA -0.277
REMARK 500 ALA A 1 CA ALA A 1 CB -0.300
REMARK 500 LYS A 3 CB LYS A 3 CG -0.742
REMARK 500 LYS A 3 CD LYS A 3 CE -0.628
REMARK 500 LYS A 3 CE LYS A 3 NZ -0.796
REMARK 500 ASP A 4 CG ASP A 4 OD1 -0.267
REMARK 500 ASP A 4 CG ASP A 4 OD2 -0.307
REMARK 500 LEU A 5 C LEU A 5 O -0.221
REMARK 500 LEU A 5 C LEU A 6 N -0.168
REMARK 500 LEU A 6 CA LEU A 6 CB -0.342
REMARK 500 LEU A 6 CG LEU A 6 CD1 -0.765
REMARK 500 LEU A 6 CG LEU A 6 CD2 -0.580
REMARK 500 LEU A 6 CA LEU A 6 C -0.398
REMARK 500 LEU A 6 C LEU A 6 O -0.409
REMARK 500 LYS A 7 N LYS A 7 CA -0.343
REMARK 500 LYS A 7 CA LYS A 7 CB -1.143
REMARK 500 LYS A 7 CB LYS A 7 CG -0.842
REMARK 500 LYS A 7 CG LYS A 7 CD -0.907
REMARK 500 LYS A 7 CD LYS A 7 CE -1.104
REMARK 500 LYS A 7 CE LYS A 7 NZ -0.814
REMARK 500 LYS A 7 CA LYS A 7 C -0.200
REMARK 500 LYS A 7 C LYS A 7 O -0.223
REMARK 500 LYS A 7 C ALA A 8 N -0.808
REMARK 500 ALA A 8 N ALA A 8 CA -0.184
REMARK 500 ALA A 8 CA ALA A 8 CB -0.154
REMARK 500 ASP A 10 CG ASP A 10 OD1 -0.185
REMARK 500 ASP A 10 CG ASP A 10 OD2 -0.220
REMARK 500 LYS A 12 CB LYS A 12 CG -0.361
REMARK 500 LYS A 12 CG LYS A 12 CD -0.428
REMARK 500 LYS A 12 CD LYS A 12 CE -0.456
REMARK 500 LYS A 12 CE LYS A 12 NZ -1.049
REMARK 500 LYS A 13 CB LYS A 13 CG -0.247
REMARK 500 LYS A 13 CG LYS A 13 CD -0.470
REMARK 500 LYS A 13 CD LYS A 13 CE -0.387
REMARK 500 LYS A 13 CE LYS A 13 NZ -0.778
REMARK 500 LEU A 15 CG LEU A 15 CD1 -0.763
REMARK 500 LEU A 15 CG LEU A 15 CD2 -0.701
REMARK 500 ASP A 16 CG ASP A 16 OD1 -0.224
REMARK 500 ASP A 16 CG ASP A 16 OD2 -0.183
REMARK 500 LYS A 19 CB LYS A 19 CG -0.201
REMARK 500 LYS A 19 CG LYS A 19 CD -0.473
REMARK 500 LYS A 19 CD LYS A 19 CE -0.634
REMARK 500 LYS A 19 CE LYS A 19 NZ -0.846
REMARK 500 GLU A 21 CG GLU A 21 CD -0.841
REMARK 500 GLU A 21 CD GLU A 21 OE1 -0.362
REMARK 500 GLU A 21 CD GLU A 21 OE2 -0.463
REMARK 500 PHE A 24 CG PHE A 24 CD2 -0.195
REMARK 500 PHE A 24 CG PHE A 24 CD1 -0.244
REMARK 500 PHE A 24 CE1 PHE A 24 CZ -0.181
REMARK 500
REMARK 500 THIS ENTRY HAS 223 BOND DEVIATIONS.
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 ACE A 0 O - C - N ANGL. DEV. = -16.7 DEGREES
REMARK 500 LYS A 3 CA - CB - CG ANGL. DEV. = 28.1 DEGREES
REMARK 500 LYS A 3 CB - CG - CD ANGL. DEV. = 28.4 DEGREES
REMARK 500 LYS A 3 CG - CD - CE ANGL. DEV. = 18.8 DEGREES
REMARK 500 LYS A 3 CD - CE - NZ ANGL. DEV. = 23.5 DEGREES
REMARK 500 ASP A 4 CB - CG - OD1 ANGL. DEV. = 6.9 DEGREES
REMARK 500 LEU A 6 CB - CA - C ANGL. DEV. = -11.9 DEGREES
REMARK 500 LEU A 6 CA - CB - CG ANGL. DEV. = 23.1 DEGREES
REMARK 500 LEU A 6 CD1 - CG - CD2 ANGL. DEV. = -39.1 DEGREES
REMARK 500 LEU A 6 CB - CG - CD1 ANGL. DEV. = 18.9 DEGREES
REMARK 500 LEU A 6 CB - CG - CD2 ANGL. DEV. = 34.4 DEGREES
REMARK 500 LEU A 6 CA - C - O ANGL. DEV. = -21.6 DEGREES
REMARK 500 LEU A 6 CA - C - N ANGL. DEV. = 14.8 DEGREES
REMARK 500 LYS A 7 N - CA - CB ANGL. DEV. = -27.5 DEGREES
REMARK 500 LYS A 7 CB - CG - CD ANGL. DEV. = 58.6 DEGREES
REMARK 500 LYS A 7 CG - CD - CE ANGL. DEV. = 55.4 DEGREES
REMARK 500 LYS A 7 CD - CE - NZ ANGL. DEV. = 40.5 DEGREES
REMARK 500 LYS A 7 N - CA - C ANGL. DEV. = 48.8 DEGREES
REMARK 500 LYS A 7 CA - C - O ANGL. DEV. = 32.7 DEGREES
REMARK 500 LYS A 7 O - C - N ANGL. DEV. = -20.6 DEGREES
REMARK 500 ASP A 10 CB - CG - OD1 ANGL. DEV. = 5.6 DEGREES
REMARK 500 LYS A 12 CB - CG - CD ANGL. DEV. = 28.7 DEGREES
REMARK 500 LYS A 12 CG - CD - CE ANGL. DEV. = 26.9 DEGREES
REMARK 500 LYS A 12 CD - CE - NZ ANGL. DEV. = 37.0 DEGREES
REMARK 500 LYS A 13 CB - CG - CD ANGL. DEV. = 46.9 DEGREES
REMARK 500 LYS A 13 CG - CD - CE ANGL. DEV. = 54.5 DEGREES
REMARK 500 LYS A 13 CD - CE - NZ ANGL. DEV. = 39.3 DEGREES
REMARK 500 LEU A 15 CD1 - CG - CD2 ANGL. DEV. = -31.3 DEGREES
REMARK 500 LEU A 15 CB - CG - CD1 ANGL. DEV. = 19.0 DEGREES
REMARK 500 LEU A 15 CB - CG - CD2 ANGL. DEV. = 23.9 DEGREES
REMARK 500 ASP A 16 CB - CG - OD2 ANGL. DEV. = 6.4 DEGREES
REMARK 500 LYS A 19 CB - CG - CD ANGL. DEV. = 24.1 DEGREES
REMARK 500 LYS A 19 CG - CD - CE ANGL. DEV. = 36.3 DEGREES
REMARK 500 LYS A 19 CD - CE - NZ ANGL. DEV. = 35.1 DEGREES
REMARK 500 GLU A 21 OE1 - CD - OE2 ANGL. DEV. = 22.4 DEGREES
REMARK 500 GLU A 21 CG - CD - OE2 ANGL. DEV. = -22.0 DEGREES
REMARK 500 PHE A 24 CB - CG - CD2 ANGL. DEV. = 7.3 DEGREES
REMARK 500 PHE A 24 CD1 - CG - CD2 ANGL. DEV. = -11.1 DEGREES
REMARK 500 PHE A 24 CG - CD2 - CE2 ANGL. DEV. = 7.3 DEGREES
REMARK 500 PHE A 24 CD1 - CE1 - CZ ANGL. DEV. = 7.9 DEGREES
REMARK 500 PHE A 24 CE1 - CZ - CE2 ANGL. DEV. = -12.8 DEGREES
REMARK 500 ASN A 25 OD1 - CG - ND2 ANGL. DEV. = -61.6 DEGREES
REMARK 500 ASN A 25 CB - CG - OD1 ANGL. DEV. = 30.8 DEGREES
REMARK 500 ASN A 25 CB - CG - ND2 ANGL. DEV. = 30.6 DEGREES
REMARK 500 ASN A 25 CA - C - O ANGL. DEV. = 52.0 DEGREES
REMARK 500 ASN A 25 CA - C - N ANGL. DEV. = 58.2 DEGREES
REMARK 500 ASN A 25 O - C - N ANGL. DEV. = 110.5 DEGREES
REMARK 500 HIS A 26 C - N - CA ANGL. DEV. = 54.0 DEGREES
REMARK 500 LYS A 27 CG - CD - CE ANGL. DEV. = 31.4 DEGREES
REMARK 500 LYS A 27 CD - CE - NZ ANGL. DEV. = 62.4 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 192 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 ALA A 8 -79.75 119.53
REMARK 500 ALA A 20 175.35 -55.22
REMARK 500 ASN A 25 -97.38 -130.83
REMARK 500 HIS A 26 -32.75 -165.93
REMARK 500 MET A 38 -100.10 -79.38
REMARK 500 ALA A 40 -32.40 -35.52
REMARK 500 ALA A 54 48.90 76.83
REMARK 500 ALA A 72 -38.43 -33.91
REMARK 500 ASP A 76 101.68 -44.61
REMARK 500 ASP A 79 -60.06 113.79
REMARK 500 ILE A 99 -72.97 -71.26
REMARK 500 ASP A 100 -37.22 -38.47
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 ASN A 25 -14.58
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 A 110 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 51 OD1
REMARK 620 2 ASP A 53 OD1 62.3
REMARK 620 3 ASP A 53 OD2 102.6 41.2
REMARK 620 4 SER A 55 OG 79.4 77.5 75.5
REMARK 620 5 PHE A 57 O 64.5 125.5 166.6 104.1
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 111 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 90 OD1
REMARK 620 2 ASP A 92 OD2 96.7
REMARK 620 3 ASP A 92 OD1 62.5 37.1
REMARK 620 4 ASP A 94 OD1 53.3 62.0 52.9
REMARK 620 5 LYS A 96 O 84.1 106.7 114.2 61.6
REMARK 620 6 GLU A 101 OE2 139.9 83.8 100.9 145.8 134.3
REMARK 620 7 GLU A 101 OE1 159.6 89.9 116.6 144.5 112.5 21.8
REMARK 620 N 1 2 3 4 5 6
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: CD
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: NULL
REMARK 800
REMARK 800 SITE_IDENTIFIER: EF
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: NULL
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 110
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 111
DBREF 3PAT A 2 109 UNP P02628 PRVA_ESOLU 1 108
SEQRES 1 A 110 ACE ALA ALA LYS ASP LEU LEU LYS ALA ASP ASP ILE LYS
SEQRES 2 A 110 LYS ALA LEU ASP ALA VAL LYS ALA GLU GLY SER PHE ASN
SEQRES 3 A 110 HIS LYS LYS PHE PHE ALA LEU VAL GLY LEU LYS ALA MET
SEQRES 4 A 110 SER ALA ASN ASP VAL LYS LYS VAL PHE LYS ALA ILE ASP
SEQRES 5 A 110 ALA ASP ALA SER GLY PHE ILE GLU GLU GLU GLU LEU LYS
SEQRES 6 A 110 PHE VAL LEU LYS SER PHE ALA ALA ASP GLY ARG ASP LEU
SEQRES 7 A 110 THR ASP ALA GLU THR LYS ALA PHE LEU LYS ALA ALA ASP
SEQRES 8 A 110 LYS ASP GLY ASP GLY LYS ILE GLY ILE ASP GLU PHE GLU
SEQRES 9 A 110 THR LEU VAL HIS GLU ALA
HET ACE A 0 3
HET CA A 110 1
HET CA A 111 1
HETNAM ACE ACETYL GROUP
HETNAM CA CALCIUM ION
FORMUL 1 ACE C2 H4 O
FORMUL 2 CA 2(CA 2+)
HELIX 1 A ASP A 9 VAL A 18 1 10
HELIX 2 B HIS A 26 VAL A 33 1 8
HELIX 3 C ALA A 40 ILE A 50 1 11
HELIX 4 D GLU A 60 ALA A 71 1BENDING AT RESIDUE 65 12
HELIX 5 E ASP A 79 ALA A 89 1 11
HELIX 6 F ILE A 99 GLU A 108 1 10
SHEET 1 A 2 ILE A 58 GLU A 59 0
SHEET 2 A 2 LYS A 96 ILE A 97 -1 N ILE A 97 O ILE A 58
LINK O ACE A 0 CA ALA A 1 1555 1555 1.48
LINK C ACE A 0 CA ALA A 1 1555 1555 1.62
LINK CH3 ACE A 0 N ALA A 1 1555 1555 1.65
LINK O ACE A 0 CB ALA A 1 1555 1555 1.62
LINK O ACE A 0 N ALA A 1 1555 1555 1.28
LINK C ACE A 0 CB ALA A 1 1555 1555 2.05
LINK OD1 ASP A 51 CA CA A 110 1555 1555 2.79
LINK OD1 ASP A 53 CA CA A 110 1555 1555 2.34
LINK OD2 ASP A 53 CA CA A 110 1555 1555 2.60
LINK OG SER A 55 CA CA A 110 1555 1555 2.91
LINK O PHE A 57 CA CA A 110 1555 1555 2.27
LINK OD1 ASP A 90 CA CA A 111 1555 1555 2.80
LINK OD2 ASP A 92 CA CA A 111 1555 1555 3.17
LINK OD1 ASP A 92 CA CA A 111 1555 1555 2.92
LINK OD1 ASP A 94 CA CA A 111 1555 1555 2.76
LINK O LYS A 96 CA CA A 111 1555 1555 2.89
LINK OE2 GLU A 101 CA CA A 111 1555 1555 3.35
LINK OE1 GLU A 101 CA CA A 111 1555 1555 2.95
SITE 1 CD 12 ASP A 51 ALA A 52 ASP A 53 ALA A 54
SITE 2 CD 12 SER A 55 GLY A 56 PHE A 57 ILE A 58
SITE 3 CD 12 GLU A 59 GLU A 60 GLU A 61 GLU A 62
SITE 1 EF 12 ASP A 90 LYS A 91 ASP A 92 GLY A 93
SITE 2 EF 12 ASP A 94 GLY A 95 LYS A 96 ILE A 97
SITE 3 EF 12 GLY A 98 ILE A 99 ASP A 100 GLU A 101
SITE 1 AC1 6 ASP A 51 ASP A 53 SER A 55 PHE A 57
SITE 2 AC1 6 GLU A 59 GLU A 62
SITE 1 AC2 5 ASP A 90 ASP A 92 ASP A 94 LYS A 96
SITE 2 AC2 5 GLU A 101
CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 1 1
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 1.000000 0.000000 0.000000 0.00000
SCALE2 0.000000 1.000000 0.000000 0.00000
SCALE3 0.000000 0.000000 1.000000 0.00000
Complete list - 16 20 Bytes